Bacterium comprising phytate-degradation pathway

Abstract

The invention is concerned with a bacterium comprising a phytate to 3-hydroxoypropionate pathway gene set that allows said bacterium to convert phytate to 3-hydroxypropionate or a salt or ester thereof. The bacterium can be used as a probiotic or supplement to promote production of propionate in the Gl tract, thereby preventing and / or treating conditions or diseases that benefit from the production of propionate, for example metabolic disease, metabolic syndrome, obesity, insulin resistance or insulin resistance-related conditions, particularly dyslipidemia, (M)ASLD-(M)ASH, type 2 diabetes mellitus and insulin-resistance in endocrine diseases.

Description

Technical field The present invention relates to the field of preventing and / or treating metabolic diseases, such as metabolic syndrome and insulin resistance or insulin resistance-related conditions, including dyslipidemia and type 2 diabetes mellitus as well as insulin-resistance in endocrine diseases or obesity. Background of the disclosure Phytate, a well-known phytochemical, is widely distributed in the plant kingdom, and especially abundant in wheat, rice and nuts. Dietary supplementation of phytate has been reported for various health benefits, including anti-diabetic activity. In particular, dietary phytate supplementation reportedly promotes epithelial repair resulting in improved gut barrier function (Wu et al., Nature 2020, 586 (7827), 108-112), reduces serum levels of glycated hemoglobin HbA1c and Advanced Glycation End products (Sanchis et al., Trial. Sci. Rep. 2018, 8 91), 9619), improves glucose metabolism (Lee et al., Nutr Res 2006, 26(9), 474-479), reduced inflammation (Liu et al., Br J. Nutr2018, 120(2), 121-130) and exerts protective effects against colon cancer (Vucenik et al., Nutr Cancer 2006, 55(2), 109-25). However, the molecular mechanism by which dietary phytate confers its health benefits is largely unknown. It was recently reported that under anaerobic conditions, the human fecal microbiome is able to fully convert phytate into short-chain fatty acids (SCFAs), including propionate and butyrate (Bui et al., Nat. Commun 2021, 12(1), 4798), which are well known microbial signaling molecules and strongly associated with host health. Nevertheless, the microbes responsible for metabolizing phytate in the human gut are unknown. Previous efforts to detect and cultivate phytate-degrading microbes from human fecal samples have remained unsuccessful (Curr Issues Intest Microbiol. 2004 Sep;5(2):23-39). This contrasts with animal studies that identified phytase-producing Mitsuokella spp. in ruminants (Haros et al., FEMS Microbiology Letters, 2005, 247(2), 231-239). Mitsuokella spp. are Gram-negative gut anaerobes belonging to the Negativicutes and the rumen isolate M. multacida possesses a phytase that is located in the outer membrane (d’Silva et al., Can J Microbiol 2000, 46(4), 391-5). There remains a need to unravel how dietary phytate is metabolized by human gut bacteria and in the human gut and to identify their phytate degradation pathway. It is an objective of the present disclosure to provide a new or improved strategy for obtaining the health benefits of phytate. In particular, it is an objective of the present invention, to provide for new means for preventing and / or treating metabolic diseases, in particular metabolic syndrome and insulin resistance or insulin resistance-related conditions, including dyslipidemia and type 2 diabetes mellitus as well as insulin-resistance in endocrine diseases (e.g., obese subjects with type 1 diabetes mellitus, Cushing's disease or lipodystrophy syndromes). Summary of the disclosure The present inventors identified Mitsuokella jalaludinii as an efficient phytate degrader in the human gut. Subsequently, a complete phytate degradation pathway in Mitsuokella jalaludinii was elucidated with NMR spectroscopy using 13C-isotope labelling and transcriptomic and genomic analysis. The genes involved in the pathway are disclosed herein and can be introduced in any suitable host bacterium to achieve phytate degradation activity. The host bacterium may, for example, be Escherichia coli, Bifidobacterium spp., Lactobacillus spp., Lactococcus spp., or Lactobacillus spp. A major end product of the pathway is the antimicrobial 3-hydroxypropionate. In addition, it was found that 3-hydroxypropionate can be converted into propionate in a synergistic interaction with Anaerostipes rhamnosivorans both in vitro and in vivo. The pathway for converting 3-hydroxypropionate into propionate has also been unravelled. Furthermore, it has been found that the supernatant of the phytate-digesting coculture of Mitsuokella jalaludinii and Anaerostipes rhamnosivorans leads to an improved intestinal barrier integrity via activating tight junction genes. These results suggest that the conversion of phytate to propionate by Mitsuokella jalaludinii and optionally Anaerostipes rhamnosivorans is responsible for phytate-driven health benefits. The present inventors envisage supplementation of a subject with a bacterium according to the present disclosure, or the synergistic combination of bacteria according to the present disclosure, to provide for a direct or synergistic effect via in situ (3-hydroxy)propionate production. Detailed description of the disclosure The present disclosure relates to a first bacterium comprising a gene set encoding a pathway for the conversion of phytate to 3-hydroxypropionate or a salt or ester thereof that allows said bacterium to convert phytate to 3-hydroxypropionate or a salt or ester thereof, for use in preventing and / or treating metabolic syndrome, insulin resistance and / or insulin resistance related condition. Specifically, the bacterium is capable of converting phytate into 3-hydroxypropionate or a derivative thereof via phytate metabolism and 3-hydroxypropionate synthesis. The term phytate is well-known to the skilled person and can be interchangeable with the terms myo-inositol-hexakisphosphate or myo-inositol-1,2,3,4,5,6-hexakisphosphate or InsPe. In addition, the present disclosure relates to a second bacterium comprising a gene set encoding a pathway for the conversion of 3-hydroxypropionate or a salt or ester thereof to propionate or a salt or ester thereof that allows said bacterium to convert 3-hydroxypropionate or a salt or ester thereof to propionate or a salt or ester thereof, for use in preventing and / or treating metabolic syndrome, insulin resistance and / or insulin resistance related condition. Also foreseen is to combine the gene set of the first bacterium and the gene set of the second bacterium, e.g. in a single bacterium. Accordingly, provided is a bacterium that comprises a gene set encoding a pathway for the conversion of phytate to 3-hydroxypropionate or a salt or ester thereof and a gene set encoding a pathway for the conversion of 3-hydroxypropionate or a salt or ester thereof to propionate or a salt or ester thereof, that allows said bacterium to convert phytate to propionate or a salt or ester thereof, for example for use in preventing and / or treating metabolic syndrome, insulin resistance and / or insulin resistance related condition. The bacteria according to the present disclosure (or strains derived therefrom), when administered to a human being or when ingested by a human being in an adequate amount, are able to survive and at least transiently colonize the gastrointestinal (Gl) tract of said human being. Colonization of the first bacterium enables greater in situ production of 3-hydroxypropionate and together with colonization of the second bacterium greater in situ production of propionate is enabled. Increased in situ production of 3-hydroxypropionate and / or propionate is believed to underlie beneficial effects as taught herein, e.g. preventing and / or treating conditions or diseases such as metabolic diseases, such as metabolic syndrome and insulin resistance or insulin resistance-related complications, such as dyslipidemia and type 2 diabetes mellitus as well as insulin-resistance in endocrine diseases (e.g., obese subjects with type 1 diabetes mellitus, Cushing's disease or lipodystrophy syndromes). Bacterium In a first aspect, the present disclosure relates to a first bacterium comprising a gene set encoding a pathway for the conversion of phytate to 3-hydroxypropionate or a salt or ester thereof that allows said bacterium to convert phytate to 3-hydroxypropionate or a salt or ester thereof, in particular but not necessarily under anaerobic conditions, such as wherein the bacterium and / or its medium is not in contact with gas comprising more than 0.1 vol%, 1 vol%, 2 vol%, 3 vol%, 4 vol%, 5 vol%, or 10 vol% of oxygen. The bacterial strain is preferably, but not necessarily, an isolate, e.g. a human intestinal isolate. The phytate to 3-hydroxypropionate or a salt or ester thereof pathway gene set may comprise one or more (e.g., at least two or three, or all) of the genes encoding the proteins: phytase, major myo-inositol transporter lolT, myo-inositol 2-dehydrogenase, inosose dehydratase, 3D-(3,5 / 4)-trihydroxycyclohexane-1,2-dione hydrolase, 5-deoxy-glucuronate isomerase, 5-keto-2-deoxygluconokinase, 5-keto-2-deoxy-D-gluconate-6 phosphate aldolase, 2-hydroxy-3-oxopropionate reductase, D-beta-hydroxypropionate permease. Additionally, the phytate to 3-hydroxypropionate or a salt or ester thereof pathway gene set may comprise the gene(s) encoding the proteins phosphate ABC transporter PstS, Phosphate ABC transporter PstC, Phosphate ABC transporter PstA, Na+ / H+ antiporter NhaA type, phosphoglycerate mutase, triosephosphate isomerase, enolase, phosphoglycerate kinase, pyruvate kinase, NAD-dependent glyceraldehyde-3-phosphate dehydrogenase, D-lactate dehydrogenase, pyruvate-flavodoxin oxidoreductase, acetyl-CoA hydrolase, D-lactate dehydrogenase, pyruvate carboxylase, malate dehydrogenase, NADP-dependent malic enzyme, fumarate hydratase alpha subunit, fumarate hydratase beta subunit, succinate dehydrogenase cytochrome b558 subunit, succinate dehydrogenase flavoprotein subunit, succinate dehydrogenase iron-sulfur protein and / or ATP synthase epsilon chain_MJ_0869, ATP synthase beta chain, ATP synthase gamma chain, ATP synthase alpha chain, ATP synthase delta chain, ATP synthase F0 sector subunit b, ATP synthase F0 sector subunit c, ATP synthase F0 sector subunit a, and / or ATP synthase protein I. In a preferred embodiment, at least one (or at least two or three or all) of the proteins: phytase, major myo-inositol transporter lolT, myo-inositol 2-dehydrogenase, inosose dehydratase, 3D-(3,5 / 4)-trihydroxycyclohexane-1,2-dione hydrolase, 5-deoxy-glucuronate isomerase, 5-keto-2-deoxygluconokinase, 5-keto-2-deoxy-D-gluconate-6 phosphate aldolase, 2-hydroxy-3-oxopropionate reductase, D-beta-hydroxypropionate permease, phosphate ABC transporter PstS, Phosphate ABC transporter PstC, Phosphate ABC transporter PstA, Na+ / H+ antiporter NhaA type, phosphoglycerate mutase, triosephosphate isomerase, enolase, phosphoglycerate kinase, pyruvate kinase, NAD-dependent glyceraldehyde-3-phosphate dehydrogenase, D-lactate dehydrogenase, pyruvate-flavodoxin oxidoreductase, acetyl-CoA hydrolase, D-lactate dehydrogenase, pyruvate carboxylase, malate dehydrogenase, NADP-dependent malic enzyme, fumarate hydratase alpha subunit, fumarate hydratase beta subunit, succinate dehydrogenase cytochrome b558 subunit, succinate dehydrogenase flavoprotein subunit, succinate dehydrogenase iron-sulfur protein, ATP synthase epsilon chain, ATP synthase beta chain, ATP synthase gamma chain, ATP synthase alpha chain, ATP synthase delta chain, ATP synthase F0 sector subunit b, ATP synthase F0 sector subunit c, ATP synthase F0 sector subunit a, and / or ATP synthase protein I may be overproduced (or the genes encoding therefor overexpressed) when the bacterium is grown in the presence of phytate as compared to when the bacterium is grown in the absence of phytate. In the context of the present disclosure, the amount of phytate used to determine whether genes are upregulated or proteins are overexpressed in a bacterium as compared to when said bacterium is grown in absence of phytate may be in the range of from about 5 mM to about 100 mM, preferably from about 10 mM to about 50 mM, more preferably from about 15 mM to about 25 mM, and even more preferably about 20 mM. In an embodiment, the first bacterium according to the present disclosure may be an isolated intestinal bacterial strain, or strain derived therefrom, and / or may be an intestinal bacterium isolated from a human being, which naturally comprises an phytate to 3-hydroxypropionate or a salt or ester pathway gene set as taught herein and which is capable of converting phytate to 3-hydroxypropionate or a salt or ester (or a derivative) thereof. In a further aspect, the first bacterium according to the disclosure may be a Mitsuokella species, preferably Mitsuokella jalaludinii or relative thereof or relative thereof having a 16S rRNA gene sequence with at least 97% sequence identity with SEQ ID NO:93. In particular, the first bacterium may be Mitsuokella jalaludinii H1-1 deposited by Wageningen University on December 1, 2023 at the Westerdijk Fungal Biodiversity Institute (CBS) located at Uppsalalaan 8, 3584CT Utrecht, the Netherlands, assigned the deposit number CBS 150836. Also encompassed is any bacterial strain derived from the deposited bacterium. Alternatively, the first bacterium according to the present disclosure may be a bacterium which has been transfected with the phytate to 3-hydroxypropionate or a salt or ester thereof pathway gene set as taught herein, and which is capable of converting phytate to 3-hydroxypropionate or a salt or ester (or a derivative) thereof. The skilled person is well-acquainted with methods for transforming bacteria with a desired genetic construct (i.e. pathway gene set). In a second aspect, the present disclosure relates to a (second) bacterium comprising a gene set encoding a pathway for conversion of 3-hydroxypropionate or a salt or ester thereof to propionate or a salt or ester thereof that allows said second bacterium to convert 3-hydroxypropionate or a salt or ester thereof to propionate or a salt or ester thereof, in particular but not necessarily under anaerobic conditions, such as wherein the bacterium and / or its medium is not in contact with gas comprising more than 1 vol%, 2 vol%, 3 vol%, 4 vol%, 5 vol%, or 10 vol% of oxygen. The bacterial strain is preferably, but not necessarily, an isolate, e.g. a human intestinal isolate. The 3-hydroxypropionate or a salt or ester thereof to propionate or a salt or ester thereof pathway gene set may comprise one or more (e.g., at least two or three, or all) of the genes encoding the proteins: permease, oxoacid CoA transferase, dehydratase, electron transfer flavoprotein beta subunit, electron transfer flavoprotein alpha subunit, and / or acyl dehydrogenase. Additionally, the 3-hydroxypropionate or a salt or ester thereof to propionate or a salt or ester thereof pathway gene set may comprise the genes encoding the proteins ATP synthase epsilon chain, ATP synthase beta chain, ATP synthase gamma chain, ATP synthase alpha chain, ATP synthase delta chain, ATP synthase F0 sector subunit b, ATP synthase F0 sector subunit c, ATP synthase F0 sector subunit a, and / or ATP synthase protein I. Preferably, the first bacterium as disclosed herein is combined with the second bacterium as disclosed herein. Preferably, the first bacterium and / or second bacterium as disclosed herein are live bacteria. Preferably, the first bacterium and / or second bacterium as disclosed herein have (machinery for) ATP production and / or NADH production. In a preferred embodiment, at least one (or at least two or three or all) of the proteins: permease, oxoacid CoA transferase, dehydratase, electron transfer flavoprotein, beta subunit, electron transfer flavoprotein, alpha subunit, and / or acyl dehydrogenase, ATP synthase epsilon chain, ATP synthase beta chain, ATP synthase gamma chain, ATP synthase alpha chain, ATP synthase delta chain, ATP synthase F0 sector subunit b, ATP synthase F0 sector subunit c, ATP synthase F0 sector subunit a, and / or ATP synthase protein I may be overproduced (or the genes encoding therefor overexpressed) when the bacterium is grown in the presence of 3-hydroxypropionate as compared to when the (second) bacterium is grown in the absence of 3-hydroxypropionate. In the context of the present disclosure, the amount of 3-hydroxypropionate used to determine whether genes are upregulated or proteins are overexpressed in a bacterium as compared to when said bacterium is grown in absence of 3-hydroxypropionate may be in the range of from about 5 mM to about 100 mM, preferably from about 10 mM to about 50 mM, more preferably from about 15 mM to about 25 mM, and even more preferably about 20 mM. In an embodiment, the (second) bacterium according to the present disclosure may be an isolated intestinal bacterial strain, or strain derived therefrom, and / or may be an intestinal bacterium isolated from a human being, which naturally comprises a 3-hydroxypropionate or a salt or ester to propionate or salt or ester thereof pathway gene set as taught herein and which is capable of converting 3-hydroxypropionate or a salt or ester (or a derivative) thereof to propionate or a salt or ester (or derivative) thereof. In a further aspect, the (second) bacterium according to the disclosure may be an Anaerostipes species (which has ability to convert 3-hydroxypropionate to propionate), although preferably not Anaerostipes butyraticus (e.g. DSM22094T) but for example Anaerostipes caccae (e.g. DSM14662) or Anaerostipes hadrus (preferably PEL85, but preferably not DSM3319T, and / or preferably not DSM108065). Particularly preferred is Anaerostipes rhamnosivorans (1y2) or relative thereof or relative thereof having a 16S rRNA gene sequence with at least 97% sequence identity with SEQ ID NO:94. In particular, the first bacterium may be Anaerostipes rhamnosivorans 1y2 deposited by Wageningen University on June 26, 2015 at the Centraalbureau voor Schimmelcultures (now named Westerdijk Fungal Biodiversity Institute) located at Uppsalalaan 8, 3584CT Utrecht, the Netherlands, assigned the deposit number CBS 140182. Alternatively, the (second) bacterium according to the present disclosure may be a bacterium which has been transfected with the 3-hydroxypropionate or a salt or ester thereof to propionate or salt or ester thereof pathway gene set as taught herein, and which is capable of converting 3-hydroxypropionate or a salt or ester (or a derivative) thereof to propionate or a salt or ester (or derivative) thereof. The skilled person is well-acquainted with methods for transforming bacteria with a desired genetic construct (i.e. pathway gene set). The phytate to 3-hydroxypropionate ora salt or ester thereof pathway gene set The gene encoding phytase may have at least 70%, 80%, 90%, 95%, 99%, or 100% sequence identity with SEQ ID NO:1. Additionally or alternatively, the gene encoding phytase may encode a phytase that has at least 70%, 80%, 90%, 95%, 99%, or 100% sequence identity with SEQ ID NO:2. The function of the gene phytase can be seen in the conversion of phytate to (myo-)inositol and phosphate. The gene encoding major myo-inositol transporter lolT may have at least 70%, 80%, 90%, 95%, 99%, or 100% sequence identity with SEQ ID NO:3. Additionally or alternatively, the gene encoding major myo-inositol transporter lolT may encode a major myo-inositol transporter lolT that has at least 70%, 80%, 90%, 95%, 99%, or 100% sequence identity with SEQ ID NO:4. The function of the gene major myo-inositol transporter lolT can be seen in the transport of inositol (across the cell membrane). The gene encoding myo-inositol 2-dehydrogenase may have at least 70, 80, 90, 95, 99, 100% sequence identity with SEQ ID NO:45. Additionally or alternatively the gene encoding myo-inositol 2-dehydrogenase may encode an myo-inositol 2-dehydrogenase that has at least 70, 80, 90, 95, 99, 100% sequence identity with SEQ ID NO:46. The function of the gene myo-inositol 2-dehydrogenase can be seen in the conversion of myo-inositol to scyllo-inosose. The gene encoding inosose dehydratase may have at least 70%, 80%, 90%, 95%, 99%, or 100% sequence identity with SEQ ID NO:5. Additionally or alternatively, the gene encoding inosose dehydratase may encode an inosose dehydratase that has at least 70%, 80%, 90%, 95%, 99%, or 100%sequence identity with SEQ ID NO: 6. The function of the gene inosose dehydratase can be seen in the conversion of scyllo-inosose to 3,5 / 4-trihydroxycyclohexa-1,2-dione. The gene encoding 3D-(3,5 / 4)-trihydroxycyclohexane-1,2-dione hydrolase may have at least 70%, 80%, 90%, 95%, 99%, or 100% sequence identity with SEQ ID NO:7. Additionally or alternatively, the gene encoding 3D-(3,5 / 4)-trihydroxycyclohexane-1,2-dione hydrolase may encode an 3D-(3,5 / 4)-trihydroxycyclohexane-1,2-dione hydrolase that has at least 70%, 80%, 90%, 95%, 99%, or 100% sequence identity with SEQ ID NO:8. The function of the gene 3D-(3,5 / 4)-trihydroxycyclohexane-1,2-dione hydrolase can be seen in the conversion of 3,5 / 4-trihydroxycyclohexa-1,2-dione to 5-deoxy-D-glucuronate. The gene encoding 5-deoxy-glucuronate isomerase may have at least 70%, 80%, 90%, 95%, 99%, or 100% sequence identity with SEQ ID NO:9. Additionally or alternatively, the gene encoding 5-deoxy-glucuronate isomerase may encode a 5-deoxy-glucuronate isomerase that has at least 70%, 80%, 90%, 95%, 99%, or 100% sequence identity with SEQ ID NO: 10. The function of the gene 5-deoxy-glucuronate isomerase can be seen in the conversion of 5-deoxy-D-glucuronate to 2-deoxy-5-keto-D-gluconate. The gene encoding 5-keto-2-deoxygluconokinase may have at least 70%, 80%, 90%, 95%, 99%, or 100% sequence identity with SEQ ID NO:11. Additionally or alternatively, the gene encoding 5-keto-2-deoxygluconokinase may encode a 5-keto-2-deoxygluconokinase that has at least 70%, 80%, 90%, 95%, 99%, or 100% sequence identity with SEQ ID NO: 12. The function of the gene 5-keto-2-deoxygluconokinase can be seen in the conversion of 2-deoxy-5-keto-D-gluconate to 2-deoxy-5-keto-D-gluconate-6P. The gene encoding 5-keto-2-deoxy-D-gluconate-6 phosphate aldolase may have at least 70%, 80%, 90%, 95%, 99%, or 100% sequence identity with SEQ ID NO:13. Additionally or alternatively, the gene encoding 5-keto-2-deoxy-D-gluconate-6 phosphate aldolase may encode a 5-keto-2-deoxy-D-gluconate-6 phosphate aldolase that has at least 70%, 80%, 90%, 95%, 99%, or 100% sequence identity with SEQ ID NO:14. The function of the gene 5-keto-2-deoxy-D-gluconate-6 phosphate aldolase can be seen in the conversion of 5-dehydro-2-deoxy-D- Gluconate-6-phosphate to 3-oxopropionate (and / or in the conversion of 5-dehydro-2-deoxy-D- Gluconate-6-phosphate to glycerone phosphate). The gene encoding 2-hydroxy-3-oxopropionate reductase may have at least 70%, 80%, 90%, 95%, 99%, or 100% sequence identity with SEQ ID NO:15. Additionally or alternatively, the gene encoding 2-hydroxy-3-oxopropionate reductase may encode a 2-hydroxy-3-oxopropionate reductase that has at least 70%, 80%, 90%, 95%, 99%, or 100% sequence identity with SEQ ID NO: 16. The function of the gene 2-hydroxy-3-oxopropionate reductase can be seen in the conversion of 3-oxopropionate to 3-hydroxypropionate. The gene encoding D-beta-hydroxypropionate permease may have at least 70%, 80%, 90%, 95%, 99%, or 100% sequence identity with SEQ ID NO:17. Additionally or alternatively, the gene encoding D-beta-hydroxypropionate permease may encode a D-beta-hydroxypropionate permease that has at least 70%, 80%, 90%, 95%, 99%, or 100% sequence identity with SEQ ID NO: 18. The function of the gene D-beta-hydroxypropionate permease can be seen in 3-hydroxypropionate transport (across cell membrane). The gene encoding phosphate ABC transporter PstS may have at least 70%, 80%, 90%, 95%, 99%, or 100% sequence identity with SEQ ID NO:19. Additionally or alternatively, the gene encoding phosphate ABC transporter PstS may encode a phosphate ABC transporter PstS that has at least 70%, 80%, 90%, 95%, 99%, or 100% sequence identity with SEQ ID NQ:20. The function of the gene phosphate ABC transporter PstS can be seen in the transport of phosphate (across the cell membrane). The gene encoding Phosphate ABC transporter PstC may have at least 70%, 80%, 90%, 95%, 99%, or 100% sequence identity with SEQ ID NO:21. Additionally or alternatively, the gene encoding Phosphate ABC transporter PstC may encode a Phosphate ABC transporter PstC that has at least 70%, 80%, 90%, 95%, 99%, or 100% sequence identity with SEQ ID NO:22. The function of the gene Phosphate ABC transporter PstC can be seen in the transport of phosphate (across the cell membrane). The gene encoding Phosphate ABC transporter PstA may have at least 70%, 80%, 90%, 95%, 99%, or 100% sequence identity with SEQ ID NO:23. Additionally or alternatively, the gene encoding Phosphate ABC transporter PstA may encode a Phosphate ABC transporter PstA that has at least 70%, 80%, 90%, 95%, 99%, or 100% sequence identity with SEQ ID NO:24. The function of the gene Phosphate ABC transporter PstA can be seen in the transport of phosphate (across the cell membrane). The gene encoding Na+ / H+ antiporter NhaA type may have at least 70%, 80%, 90%, 95%, 99%, or 100% sequence identity with SEQ ID NO:25. Additionally or alternatively, the gene encoding Na+ / H+ antiporter NhaA type may encode a Na+ / H+ antiporter NhaA type that has at least 70%, 80%, 90%, 95%, 99%, or 100% sequence identity with SEQ ID NO:26. The function of the gene Na+ / H+ antiporter NhaA type can be seen in the transport of phosphate (across the cell membrane). The gene encoding phosphoglycerate mutase may have at least 70%, 80%, 90%, 95%, 99%, or 100% sequence identity with SEQ ID NO:27. Additionally or alternatively, the gene encoding phosphoglycerate mutase may encode a phosphoglycerate mutase that has at least 70%, 80%, 90%, 95%, 99%, or 100% sequence identity with SEQ ID NO:28. The gene encoding triosephosphate isomerase may have at least 70%, 80%, 90%, 95%, 99%, or 100% sequence identity with SEQ ID NO:29. Additionally or alternatively, the gene encoding triosephosphate isomerase may encode a triosephosphate isomerase that has at least 70%, 80%, 90%, 95%, 99%, or 100% sequence identity with SEQ ID NQ:30. The gene encoding enolase may have at least 70%, 80%, 90%, 95%, 99%, or 100% sequence identity with SEQ ID NO:31. Additionally or alternatively, the gene encoding enolase may encode an enolase that has at least 70%, 80%, 90%, 95%, 99%, or 100% sequence identity with SEQ ID NO:32. The gene encoding phosphoglycerate kinase may have at least 70%, 80%, 90%, 95%, 99%, or 100% sequence identity with SEQ ID NO:33. Additionally or alternatively, the gene encoding Phosphoglycerate kinase may encode a phosphoglycerate kinase that has at least 70%, 80%, 90%, 95%, 99%, or 100% sequence identity with SEQ ID NO:34. The gene encoding pyruvate kinase may have at least 70%, 80%, 90%, 95%, 99%, or 100% sequence identity with SEQ ID NO:35. Additionally or alternatively, the gene encoding pyruvate kinase may encode a pyruvate kinase that has at least 70%, 80%, 90%, 95%, 99%, or 100% sequence identity with SEQ ID NO:36. The gene encoding NAD-dependent glyceraldehyde-3-phosphate dehydrogenase may have at least 70%, 80%, 90%, 95%, 99%, or 100% sequence identity with SEQ ID NO:37. Additionally or alternatively, the gene NAD-dependent glyceraldehyde-3-phosphate dehydrogenase may encode a NAD-dependent glyceraldehyde-3-phosphate dehydrogenase that has at least 70%, 80%, 90%, 95%, 99%, or 100% sequence identity with SEQ ID NO:38. The function of the gene NAD-dependent glyceraldehyde-3-phosphate dehydrogenase can be seen in the conversion of glycerone phosphate to pyruvate. The gene encoding D-lactate dehydrogenase_may have at least 70%, 80%, 90%, 95%, 99%, or 100% sequence identity with SEQ ID NO:39. Additionally or alternatively, the gene D-lactate dehydrogenase_may encode a D-lactate dehydrogenase_that has at least 70%, 80%, 90%, 95%, 99%, or 100% sequence identity with SEQ ID NQ:40. The function of the gene D-lactate dehydrogenase_can be seen in the conversion of pyruvate to lactate. The gene encoding pyruvate-flavodoxin oxidoreductase may have at least 70%, 80%, 90%, 95%, 99%, or 100% sequence identity with SEQ ID NO:41. Additionally or alternatively, the gene pyruvate-flavodoxin oxidoreductase may encode an pyruvate-flavodoxin oxidoreductase that has at least 70%, 80%, 90%, 95%, 99%, or 100% sequence identity with SEQ ID NO:42. The function of the gene pyruvate-flavodoxin oxidoreductase can be seen in the conversion of pyruvate to acetyl-CoA. The gene encoding acetyl-CoA hydrolase may have at least 70%, 80%, 90%, 95%, 99%, or 100% sequence identity with SEQ ID NO:43. Additionally or alternatively, the gene acetyl-CoA hydrolase may encode an acetyl-CoA hydrolase that has at least 70%, 80%, 90%, 95%, 99%, or 100% sequence identity with SEQ ID NO:44. The function of the gene acetyl-CoA hydrolase can be seen in the conversion of acetyl-CoA to acetate. The gene encoding D-lactate dehydrogenase may have at least 70%, 80%, 90%, 95%, 99%, or 100% sequence identity with SEQ ID NO:45. Additionally or alternatively, the gene D-lactate dehydrogenase may encode an D-lactate dehydrogenase that has at least 70%, 80%, 90%, 95%, 99%, or 100% sequence identity with SEQ ID NO:46. The function of the gene D-lactate dehydrogenase can be seen in the conversion of pyruvate to lactate. The gene encoding pyruvate carboxylase may have at least 70%, 80%, 90%, 95%, 99%, or 100% sequence identity with SEQ ID NO:47. Additionally or alternatively, the gene pyruvate carboxylase may encode a pyruvate carboxylase that has at least 70%, 80%, 90%, 95%, 99%, or 100% sequence identity with SEQ ID NO:48. The function of the gene pyruvate carboxylase can be seen in the conversion of pyruvate to oxaloacetate. The gene encoding malate dehydrogenase may have at least 70%, 80%, 90%, 95%, 99%, or 100% sequence identity with SEQ ID NO:49. Additionally or alternatively, the gene malate dehydrogenase may encode a malate dehydrogenase that has at least 70%, 80%, 90%, 95%, 99%, or 100% sequence identity with SEQ ID NQ:50. The function of the gene malate dehydrogenase can be seen in the conversion of oxaloacetate to malate. The gene encoding NADP-dependent malic enzyme may have at least 70%, 80%, 90%, 95%, 99%, or 100% sequence identity with SEQ ID NO:51. Additionally or alternatively, the gene NADP-dependent malic enzyme may encode an NADP-dependent malic enzyme that has at least 70%, 80%, 90%, 95%, 99%, or 100% sequence identity with SEQ ID NO:52. The function of the gene NADP-dependent malic enzyme can be seen in the conversion of pyruvate to malate. The gene encoding fumarate hydratase alpha subunit may have at least 70%, 80%, 90%, 95%, 99%, or 100% sequence identity with SEQ ID NO:53. Additionally or alternatively, the gene fumarate hydratase alpha subunit may encode an fumarate hydratase alpha subunit that has at least 70%, 80%, 90%, 95%, 99%, or 100% sequence identity with SEQ ID NO:54. The function of the gene fumarate hydratase alpha subunit can be seen in the conversion of malate to fumarate. The gene encoding fumarate hydratase beta subunit may have at least 70%, 80%, 90%, 95%, 99%, or 100% sequence identity with SEQ ID NO:55. Additionally or alternatively, the gene fumarate hydratase beta subunit may encode an fumarate hydratase beta subunit that has at least 70%, 80%, 90%, 95%, 99%, or 100% sequence identity with SEQ ID NO:56. The function of the gene fumarate hydratase beta subunit can be seen in the conversion of malate to fumarate. The gene encoding succinate dehydrogenase cytochrome b558 subunit may have at least 70%, 80%, 90%, 95%, 99%, or 100% sequence identity with SEQ ID NO:57. Additionally or alternatively, the gene succinate dehydrogenase cytochrome b558 subunit may encode an succinate dehydrogenase cytochrome b558 subunit that has at least 70%, 80%, 90%, 95%, 99%, or 100% sequence identity with SEQ ID NO:58. The function of the gene succinate dehydrogenase cytochrome b558 subunit can be seen in the conversion of fumarate to succinate The gene encoding succinate dehydrogenase flavoprotein subunit may have at least 70%, 80%, 90%, 95%, 99%, or 100% sequence identity with SEQ ID NO:59. Additionally or alternatively, the gene succinate dehydrogenase flavoprotein subunit may encode an succinate dehydrogenase flavoprotein subunit that has at least 70%, 80%, 90%, 95%, 99%, or 100% sequence identity with SEQ ID NO:60. The function of the gene succinate dehydrogenase flavoprotein subunit can be seen in the conversion of fumarate to succinate The gene encoding succinate dehydrogenase iron-sulfur protein may have at least 70%, 80%, 90%, 95%, 99%, or 100% sequence identity with SEQ ID NO:61. Additionally or alternatively, the gene succinate dehydrogenase iron-sulfur protein may encode an succinate dehydrogenase iron-sulfur protein that has at least 70%, 80%, 90%, 95%, 99%, or 100% sequence identity with SEQ ID NO:62. The function of the gene succinate dehydrogenase iron-sulfur protein can be seen in the conversion of fumarate to succinate The gene encoding ATP synthase epsilon chain may have at least 70%, 80%, 90%, 95%, 99%, or 100% sequence identity with SEQ ID NO:63. Additionally or alternatively, the gene ATP synthase epsilon chain may encode an ATP synthase epsilon chain that has at least 70%, 80%, 90%, 95%, 99%, or 100% sequence identity with SEQ ID NO:64. The gene encoding ATP synthase beta chain may have at least 70%, 80%, 90%, 95%, 99%, or 100% sequence identity with SEQ ID NO:65. Additionally or alternatively, the gene ATP synthase beta chain may encode an ATP synthase beta chain that has at least 70%, 80%, 90%, 95%, 99%, or 100% sequence identity with SEQ ID NO:66. The gene encoding ATP synthase gamma chain may have at least 70%, 80%, 90%, 95%, 99%, or 100% sequence identity with SEQ ID NO:67. Additionally or alternatively, the gene ATP synthase gamma chain may encode an ATP synthase gamma chain that has at least 70%, 80%, 90%, 95%, 99%, or 100% sequence identity with SEQ ID NO:68. The gene encoding ATP synthase alpha chain may have at least 70%, 80%, 90%, 95%, 99%, or 100% sequence identity with SEQ ID NO:69. Additionally or alternatively, the gene ATP synthase alpha chain may encode an ATP synthase alpha chain that has at least 70%, 80%, 90%, 95%, 99%, or 100% sequence identity with SEQ ID NQ:70. The gene encoding ATP synthase delta chain may have at least 70%, 80%, 90%, 95%, 99%, or 100% sequence identity with SEQ ID NO:71. Additionally or alternatively, the gene ATP synthase delta chain may encode an ATP synthase delta chain that has at least 70%, 80%, 90%, 95%, 99%, or 100% sequence identity with SEQ ID NO:72. The gene encoding ATP synthase F0 sector subunit b may have at least 70%, 80%, 90%, 95%, 99%, or 100% sequence identity with SEQ ID NO:73. Additionally or alternatively, the gene ATP synthase F0 sector subunit b may encode an ATP synthase F0 sector subunit b that has at least 70%, 80%, 90%, 95%, 99%, or 100% sequence identity with SEQ ID NO:74. The gene encoding ATP synthase FO sector subunit c may have at least 70%, 80%, 90%, 95%, 99%, or 100% sequence identity with SEQ ID NO:75. Additionally or alternatively, the gene ATP synthase F0 sector subunit c may encode an ATP synthase F0 sector subunit c that has at least 70%, 80%, 90%, 95%, 99%, or 100% sequence identity with SEQ ID NO:76. The gene encoding ATP synthase F0 sector subunit a may have at least 70%, 80%, 90%, 95%, 99%, or 100% sequence identity with SEQ ID NO:77. Additionally or alternatively, the gene ATP synthase F0 sector subunit a may encode an ATP synthase F0 sector subunit a that has at least 70%, 80%, 90%, 95%, 99%, or 100% sequence identity with SEQ ID NO:78. The gene encoding ATP synthase protein I may have at least 70%, 80%, 90%, 95%, 99%, or 100% sequence identity with SEQ ID NO:79. Additionally or alternatively, the gene ATP synthase protein I may encode an ATP synthase protein I that has at least 70%, 80%, 90%, 95%, 99%, or 100% sequence identity with SEQ ID NQ:80. The 3-hydroxypropionate or a salt or ester thereof to propionate or a salt or ester thereof pathway gene set The gene encoding permease may have at least 70%, 80%, 90%, 95%, 99%, or 100% sequence identity with SEQ ID NO:81. Additionally or alternatively, the gene permease may encode a permease that has at least 70%, 80%, 90%, 95%, 99%, or 100% sequence identity with SEQ ID NO:82. The function of the gene permease can be seen in the transport of 3-hydroxypropionate (across the cell membrane). The gene encoding oxoacid CoA transferase may have at least 70%, 80%, 90%, 95%, 99%, or 100% sequence identity with SEQ ID NO:83. Additionally or alternatively, the gene oxoacid CoA transferase may encode an oxoacid CoA transferase that has at least 70%, 80%, 90%, 95%, 99%, or 100% sequence identity with SEQ ID NO:84. The function of the gene oxoacid CoA transferase can be seen in the conversion of 3-hydroxypropionate to 3-hydroxy propionyl-CoA. The gene encoding dehydratase may have at least 70%, 80%, 90%, 95%, 99%, or 100% sequence identity with SEQ ID NO:85. Additionally or alternatively, the gene dehydratase may encode an dehydratase that has at least 70%, 80%, 90%, 95%, 99%, or 100% sequence identity with SEQ ID NO:86. The function of the gene dehydratase can be seen in the conversion of 3-hydroxy propionyl-CoA to Acryloyl-CoA. The gene encoding electron transfer flavoprotein beta subunit may have at least 70%, 80%, 90%, 95%, 99%, or 100% sequence identity with SEQ ID NO:87. Additionally or alternatively, the gene electron transfer flavoprotein beta subunit may encode an electron transfer flavoprotein beta subunit that has at least 70%, 80%, 90%, 95%, 99%, or 100% sequence identity with SEQ ID NO:88. The function of the gene electron transfer flavoprotein beta subunit can be seen in the conversion of acryloyl-CoA to propionyl-Coa. The gene encoding electron transfer flavoprotein alpha subunit may have at least 70%, 80%, 90%, 95%, 99%, or 100% sequence identity with SEQ ID NO:86. Additionally or alternatively, the gene electron transfer flavoprotein alpha subunit may encode an electron transfer flavoprotein alpha subunit that has at least 70%, 80%, 90%, 95%, 99%, or 100% sequence identity with SEQ ID NO:90. The function of the gene electron transfer flavoprotein alpha subunit can be seen in the conversion of acryloyl-CoA to propionyl-Coa. The gene encoding acyl dehydrogenase may have at least 70%, 80%, 90%, 95%, 99%, or 100% sequence identity with SEQ ID NO:91. Additionally or alternatively, the gene acyl dehydrogenase may encode an acyl dehydrogenase that has at least 70%, 80%, 90%, 95%, 99%, or 100% sequence identity with SEQ ID NO:92. The function of the gene acyl dehydrogenase can be seen in the conversion of acryloyl-CoA to propionyl-Coa.. The gene encoding ATP synthase epsilon chain may have at least 70%, 80%, 90%, 95%, 99%, or 100% sequence identity with SEQ ID NO:63. Additionally or alternatively, the gene ATP synthase epsilon chain may encode an ATP synthase epsilon chain that has at least 70%, 80%, 90%, 95%, 99%, or 100% sequence identity with SEQ ID NO:64. The gene encoding ATP synthase beta chain may have at least 70%, 80%, 90%, 95%, 99%, or 100% sequence identity with SEQ ID NO:65. Additionally or alternatively, the gene ATP synthase beta chain may encode an ATP synthase beta chain that has at least 70%, 80%, 90%, 95%, 99%, or 100% sequence identity with SEQ ID NO:66. The gene encoding ATP synthase gamma chain may have at least 70%, 80%, 90%, 95%, 99%, or 100% sequence identity with SEQ ID NO:67. Additionally or alternatively, the gene ATP synthase gamma chain may encode an ATP synthase gamma chain that has at least 70%, 80%, 90%, 95%, 99%, or 100% sequence identity with SEQ ID NO:68. The gene encoding ATP synthase alpha chain may have at least 70%, 80%, 90%, 95%, 99%, or 100% sequence identity with SEQ ID NO:69. Additionally or alternatively, the gene ATP synthase alpha chain may encode an ATP synthase alpha chain that has at least 70%, 80%, 90%, 95%, 99%, or 100% sequence identity with SEQ ID NQ:70. The gene encoding ATP synthase delta chain may have at least 70%, 80%, 90%, 95%, 99%, or 100% sequence identity with SEQ ID NO:71. Additionally or alternatively, the gene ATP synthase delta chain may encode an ATP synthase delta chain that has at least 70%, 80%, 90%, 95%, 99%, or 100% sequence identity with SEQ ID NO:72. The gene encoding ATP synthase F0 sector subunit b may have at least 70%, 80%, 90%, 95%, 99%, or 100% sequence identity with SEQ ID NO:73. Additionally or alternatively, the gene ATP synthase F0 sector subunit b may encode an ATP synthase F0 sector subunit b that has at least 70%, 80%, 90%, 95%, 99%, or 100% sequence identity with SEQ ID NO:74. The gene encoding ATP synthase F0 sector subunit c may have at least 70%, 80%, 90%, 95%, 99%, or 100% sequence identity with SEQ ID NO:75. Additionally or alternatively, the 14 gene ATP synthase FO sector subunit c may encode an ATP synthase FO sector subunit c that has at least 70%, 80%, 90%, 95%, 99%, or 100% sequence identity with SEQ ID NO:76. The gene encoding ATP synthase FO sector subunit a may have at least 70%, 80%, 90%, 95%, 99%, or 100% sequence identity with SEQ ID NO:77. Additionally or alternatively, the gene ATP synthase F0 sector subunit a may encode an ATP synthase F0 sector subunit a that has at least 70%, 80%, 90%, 95%, 99%, or 100% sequence identity with SEQ ID NO:78. The gene encoding ATP synthase protein I may have at least 70%, 80%, 90%, 95%, 99%, or 100% sequence identity with SEQ ID NO:79. Additionally or alternatively, the gene ATP synthase protein I may encode an ATP synthase protein I that has at least 70%, 80%, 90%, 95%, 99%, or 100% sequence identity with SEQ ID NQ:80. Compositions The present disclosure provides a kit comprising a composition comprising the first bacterium and / or a composition comprising the second bacterium, wherein optionally the compositions comprise a physiologically acceptable carrier. The present disclosure also provides a composition comprising the first bacterium and / or second bacterium according to the present disclosure and optionally a physiologically acceptable carrier. The physiologically acceptable carrier may be any carrier that is suitable for keeping the bacterium / bacteria as taught herein viable until consumption by a subject (e.g. human or animal). Non-limiting examples of acceptable carriers that are suitable for this purpose include any well-known physiological or pharmaceutical carriers, buffers, and excipients. It will be appreciated that the choice of a suitable physiological or pharmaceutical carrier will depend upon the intended mode of administration of the composition as taught herein (e.g. oral) and the intended form of the composition (e.g. beverage, yogurt, powder, capsules, and the like). The skilled person knows how to select a physiological or pharmaceutical carrier, which is suitable for the compositions as taught herein. In an embodiment, the composition as taught herein may be in the form of a food composition, feed composition, feed supplement composition, food supplement composition or pharmaceutical composition. The composition is preferably suitable for consumption by a human being. In an embodiment, the composition is a food or food supplement composition. The food or food supplement composition may be selected from the group consisting of a liquid, liquid beverage (including dairy beverage and fermented beverage), yogurt, cheese, gel, gelatine, gelatine capsule, powder, paste, pressed tablet, and gel cap. In a suitable embodiment, the composition is a liquid, preferably a liquid beverage (e.g. dairy beverage). The food or food supplement composition may be a dairy product, preferably a fermented dairy product, such as yogurt or yogurt drink. In an embodiment, the composition as taught herein may be a probiotic composition. Such probiotic composition may comprise the first (isolated) bacterium and / or second (isolated) bacterium as taught herein, or a strain derived therefrom. In an embodiment, the composition as taught herein further comprises one or more additional beneficial isolated intestinal bacterial strain. In an embodiment, the composition may be a symbiotic composition. It may be advantageous to add one or more prebiotic ingredients to the composition as taught herein, for example, to supplement the effects (e.g. production of 3-hydroxypropionate / propionate) of the first bacterium and / or second bacterium as taught herein. In an embodiment, the one or more prebiotic ingredients may be any prebiotic ingredients, which are suitable to enhance the activity and / or stimulate the growth of the bacterium, or a strain derived therefrom, as taught herein. Non-limiting examples of suitable prebiotic ingredients include fibres such as inulin, pectin, and resistant starch, as well as cellobiose, maltose, mannose, salicine, trehalose, amygdalin, arabinose, melibiose, sorbitol, rhamnose and xylose. In an embodiment, the composition as taught herein comprises a phytate-rich source and / or phytate. For instance, it may be advantageous to add a phytate-rich source and / or phytate to the composition as taught herein to further promote the production of 3-hydroxypropionate / propionate or a derivative thereof in the Gl tract of a mammal (e.g. human being). In an embodiment, the composition as taught herein may comprise one or more ingredients which are suitable for promoting survival and / or viability of the bacterium or strain derived therefrom as taught herein during storage and / or during exposure to bile and / or during passage through the Gl tract of a mammal (e.g. a human being). Non-limiting examples of such ingredients include an enteric coating and controlled release agents allowing passage through the stomach. The skilled person knows how to select suitable ingredients for maintaining a bacterium as taught herein viable and functional, i.e. able to carry out intended function(s). In one embodiment, the compositions as taught herein may further comprise one or more ingredients, which further enhance the nutritional value and / or the therapeutic value the compositions as taught herein. For instance, it may be advantageous to add one or more ingredients (e.g. nutritional ingredients, veterinary, medicinal agents, etc.) selected from the group consisting of proteins, amino acids, enzymes, mineral salts, vitamins (e.g. thiamine HCI, riboflavin, pyridoxine HCI, niacin, inositol, choline chloride, calcium pantothenate, biotin, folic acid, ascorbic acid, vitamin B12, p-aminobenzoic acid, vitamin A acetate, vitamin K, vitamin D, vitamin E, and the like), sugars and complex carbohydrates (e.g. water-soluble and water-insoluble monosaccharides, disaccharides, and polysaccharides), medicinal compounds (e.g. antibiotics), antioxidants, and trace element ingredients (e.g. compounds of cobalt, copper, manganese, iron, zinc, tin, nickel, chromium, molybdenum, iodine, chlorine, silicon, vanadium, selenium, calcium, magnesium, sodium and potassium and the like). The skilled person is familiar with methods and ingredients that are suitable to enhance the nutritional and / or therapeutic / medicinal value of the compositions as taught herein. The first bacterium and / or second bacterium as taught herein may be incorporated into the composition in lyophilized form, microencapsulated form (reviewed by, for example, Solanki et al., BioMed Res. Int. 2013, Article ID 620719), or any other form preserving the activity and / or viability of the bacterial strain. The composition as taught herein may be a pharmaceutical composition. The pharmaceutical composition may be for use as a supplement. A pharmaceutical composition will usually comprise a pharmaceutical carrier, in addition to the first bacterium and / or second bacterium taught herein. The carrier is preferably an inert carrier. The preferred form depends on the intended mode of administration and (therapeutic) application. A pharmaceutical carrier can be any compatible, nontoxic substance suitable to deliver the bacterium taught herein to the Gl tract of a subject. For example, sterile water or inert solids may be used as a carrier, usually complemented with a pharmaceutically acceptable adjuvant, buffering agent, dispersing agent, and the like. A pharmaceutical composition as taught herein may be in liquid form, e.g. a stabilized suspension of bacteria of the bacterium taught herein, or in solid form, e.g., a powder of lyophilized bacteria taught herein. In case the bacterium taught herein is lyophilized, a cryoprotectant such as lactose, trehalose or glycogen can be employed. E.g., for oral administration, the first bacterium and / or second bacterium taught herein can be administered in (separate) solid dosage forms, such as capsules, tablets, and powders, comprising lyophilized bacteria, or in (separate) liquid dosage forms, such as elixirs, syrups, and suspensions. The first bacterium and / or second bacterium taught herein, e.g., in lyophilized form, can be encapsulated in capsules such as gelatin capsules, together with inactive ingredients and powdered carriers, such as e.g. glucose, lactose, sucrose, mannitol, starch, cellulose or cellulose derivatives, magnesium stearate, stearic acid, sodium saccharin, talcum, magnesium carbonate and the like. In an embodiment, the first bacterium and / or second bacterium as taught herein may be comprised in the composition as taught herein in an amount ranging from about 106 to about 1015 colony forming units (CFU). For instance, the intestinal bacteria may be comprised in the composition in an amount of about 107 CFU to about 1014CFU, preferably about 108 CFU to about 1013CFU, more preferably about 109 CFU to about 1012 CFU, even more preferably about 1010 CFU to about 1012 CFU, e.g. for each of the first bacterium and / or second bacterium. The present disclosure also provides for a composition obtainable by: a) growing the first bacterium as taught herein and optionally a second bacterium as taught herein in an aqueous medium suitable therefor (the aqueous medium may comprise phytate); b) after step a), separating the first bacterium and optionally the second bacterium from the aqueous medium to thereby obtain the composition (i.e. the aqueous medium separated from the first bacterium and optionally the second bacterium). The composition may comprise (3-hydroxy)propionate. In the present disclosure, it is preferred that the first bacterium and / or second bacterium, or composition taught herein, is not comprised in fecal matter. In this regard, the term ‘fecal matter’ includes feces or a fraction thereof, such as obtained by mixing feces with aqueous medium and subsequent filtering and / or centrifugation. Methods and uses The present disclosure is concerned with a first bacterium and / or second bacterium as taught herein or a composition as taught herein for use as a medicament, for use as a food or food supplement, or for use as a probiotic and / or symbiotic. In a preferred embodiment, the first bacterium and / or second bacterium for use according to the present disclosure may be administered separately, sequentially or simultaneously with phytate or with a phytate source, which may be present in the same composition as the first bacterium and / or second bacterium, or in a separate composition, for example, comprising in the range of from about 5 mM to about 100 mM, preferably from about 10 mM to about 50 mM, more preferably from about 15 mM to about 25 mM, and even more preferably about 20 mM phytate, or for example comprising from about 1 mg to about 1000 mg, preferably from about 10 mg to about 500 mg, more preferably from about 15 mg to about 50 mg. Alternatively, the amount of phytate and / or administration frequency may be chosen such that between 0.1 g and 100 grams is consumed per day, for example between 0.5 g and 10 g per day or between 0.1 g and 5 g per day. The present disclosure particularly pertains to the first bacterium and / or second bacterium as taught herein or (separate) composition comprising the same as taught herein for use in maintaining, restoring and / or improving Gl health in general, and / or for preventing and / or treating conditions or diseases such as obesity, metabolic diseases, such as metabolic syndrome and insulin resistance or insulin resistance-related complications, such as (metabolic) Adenylosuccinate lyase deficiency ((M)ASLD) I (metabolic) dysfunction-associated steatohepatitis ((M)ASH), dyslipidemia and type 2 diabetes mellitus as well as insulin-resistance in endocrine diseases (e.g., obese subjects with type 1 diabetes mellitus, Cushing's disease or lipodystrophy syndromes). In addition, foreseen is use for not gaining weight, such as after having lost weight e.g. following GLP1 agonist therapy. Furthermore, foreseen is use for maintaining weight (within 1, 2, 3, 4 or 5% margin with respect to said weight), such as during and / or after GLP1 agonist therapy. Without being bound by theory, the first and / or second bacterium according to the present disclosure (optionally administered together with phytate) may have satiety effects since in situ propionate is provided (see Int. Dairy J. 18, 945-950 (2008)). The present disclosure is also directed to a method for maintaining, restoring and / or improving Gl health in general, and / or for preventing and / or treating conditions or diseases such as obesity (i.e. a body mass index (BMI) over 25, 26, 27, 28, 29, preferably over 30), metabolic diseases, such as metabolic syndrome and insulin resistance or insulin resistance-related complications, such as dyslipidemia and type 2 diabetes mellitus as well as insulin-resistance in endocrine diseases (e.g., obese subjects with type 1 diabetes mellitus, Cushing's disease or lipodystrophy syndromes) in a subject in need thereof, said method comprising the step of increasing the level of the first bacterium and / or second bacterium as taught herein in said subject. It has also been found that the present disclosure, e.g. the first bacterium and / or second bacterium as taught herein, may be for use in enhancing (intestinal) epithelial barrier function. In this regard, see also Int. Dairy J. 18, 945-950 (2008); and Gut 2015;64:1744-1754. doi: 10.1136 / gutjnl-2014-307913. It has additionally been found that the present disclosure, e.g. the first bacterium and / or second bacterium as taught herein, may be for use in preventing or treating inflammatory disorders, such as rheumatoid arthritis, or inflammatory bowel disease. It has additionally been found that the present disclosure, e.g. the first bacterium and / or second bacterium as taught herein, may be for use in preventing or treating cancer such as colon cancer. The present disclosure also foresees use for enhancing satiety in a subject. The present disclosure shows in particular the increased propionate production in the gut that will increase satiety and as a consequence will reduce food intake and prevent weight gain (see Ruijschop et al. 2008 Chambers et al 2015). The level of the first bacterium and / or second bacterium as taught herein in said subject may be increased by administering an effective amount of said first bacterium and / or second bacterium to said subject, and / or by administering an effective amount of a compound capable of increasing the level of said first bacterium and / or second bacterium in (the Gl tract of) said subject. In an embodiment, the first bacterium and / or second bacterium as taught herein may be administered concomitant with phytate or a phytate source, such as fruits, beans, grains, and nuts. The skilled person can, without undue burden, readily identify phytate-rich sources. In addition or alternatively, the first bacterium and / or second bacterium as taught herein may be administered to a subject following a diet which includes phytate, such as a subject following a vegetarian diet, vegan diet, or Mediterranean diet. In a preferred embodiment, the level of the first bacterium and / or second bacterium as taught herein in the Gl tract of a subject may be increased by administering to the subject an 19 effective amount of the first bacterium and / or second bacterium as taught herein, preferably Mitsuokella jalaludinii or relative thereof having a 16S rRNA gene sequence with at least 97% sequence identity with SEQ ID NO:93 and / or Anaerostipes rhamnosivorans 1y2 or relative thereof having a 16S rRNA gene sequence with at least 97% sequence identity with SEQ ID NO:94 and / or a composition as taught herein comprising said. In an embodiment, the subject may be selected from the group consisting of human beings, (monogastric) animals such as non-human primates, mice, rats, cats, dogs, cows, and pigs. In a preferred embodiment, the subject is a human. The disclosure also relates to a method for producing 3-hydroxypropionate and / or propionate, comprising the step of contacting the first bacterium and / or second bacterium as taught herein with a suitable energy source, e.g. phytate and / or glucose / acetate, under conditions which allow the first bacterium and / or second bacterium as taught herein to convert the energy source to 3-hydroxypropionate and / or propionate. The methods taught herein may be in vitro methods. GENERAL DEFINITIONS The terms ‘probiotics’ and ‘probiotic products’ as used herein refer to microorganisms such as intestinal bacteria, which - when administered or ingested in effective amounts - confer health benefits to the host (e.g. mammals, such as humans). Preferably, probiotics should be alive or viable when administered to a subject so as to allow the probiotics to colonize the large intestine of the host. However, under certain conditions, probiotics may also be dead when administered provided that substances produced by the probiotics still exert probiotic, beneficial effects on the host. The terms ‘prebiotics’ and ‘prebiotic products’ as used herein generally refer to compounds that promote the growth and / or activity of Gl microorganisms that contribute to the well-being of their host. Prebiotics or prebiotic products consist mainly of fermentable fibres or non-digestible carbohydrates. The fermentation of these fibres by prebiotics promotes the production of beneficial end products, such as SCFAs, particularly butyrate. The skilled person is well-acquainted with the field of prebiotics and knows how to select ingredients endowed with prebiotic activity. The terms ‘symbiotics’ and ‘symbiotic products’ as used herein generally refer to compositions and / or nutritional supplements combining probiotics and one or more compounds that promote the growth and / or activity of Gl microorganisms, such as prebiotics, into one product. The symbiotic beneficially affects the host by improving the survival and colonization of the probiotic in the Gl tract, by selectively stimulating the growth and / or by activating the metabolism of the probiotic, thus improving host welfare. The skilled person is well-acquainted with symbiotics and knows how to select ingredients that may be combined into a symbiotic. The terms ‘propionate’ and ‘propionic acid’ as used herein refer to a carboxylic acid with chemical formula CH3CH2CO2H. The terms may include derivatives thereof, i.e. compounds derived from propionic acid and in particular salts of propionic acid (propionates) and esters of propionic acid ( propanoates). Propionic acid can be seen as a short-chain saturated fatty acid comprising ethane attached to the carbon of a carboxy group. Non-limiting examples of propionates are ammonium propionate, calcium propionate, magnesium propionate, potassium propionate and sodium propionate. A non-limiting example of a propanoate is ethyl propionate. The term ‘beneficial intestinal bacteria species’ as used herein refers to a bacterium species that inhabits (i.e. is innate) the mammalian (e.g. human) intestine and exerts beneficial effect(s) (e.g. protection against pathogenic bacteria species, production of butyric acid and / or butyrate and derivatives, etc.) on the Gl, metabolic and other health of a mammal in which it resides. Non-limiting examples of beneficial intestinal bacterial species include lactic acid bacteria from the genera Lactobacillus and Bifidobacterium. Other non-limiting examples of beneficial intestinal bacterial species include butyrate-producing bacterial species, which use the acetyl-CoA to produce butyric acid and / or butyrate and derivative thereof, such as the bacterial strains disclosed in US 2014 / 0242654, WO 2014 / 150094 or WO 2013 / 032328. The term ‘effective amount’ as used herein refers to an amount necessary to achieve an effect as taught herein. For instance, an effective amount of the first bacterium and / or second bacterium as taught herein is an amount which is effectively useful for maintaining, restoring, and / or improving Gl heath in a human being, for converting phytate into 3-hydroxypropionate / propionate or a derivative thereof and / or for preventing and / or treating conditions or diseases described herein in a subject, preferably a human being. These conditions or diseases include, without limitation, obesity, metabolic diseases, such as metabolic syndrome and insulin resistance or insulin resistance-related complications, such as dyslipidemia and type 2 diabetes mellitus as well as insulin-resistance in endocrine diseases (e.g., obese subjects with type 1 diabetes mellitus, Cushing's disease or lipodystrophy syndromes). The effective amount can be readily determined without undue experimentation by a person of ordinary skill in the art. The term ‘a strain that derives therefrom’ as used herein relates to strains obtained by using the deposited strain as taught herein as starting material. The strain that derives therefrom may be a mutant strain, which may be derived from a strain of the invention by means of, for instance, genetic engineering, radiation, UV light, chemical treatment. Alternatively, such derivative or mutant strain may be a strain derived from the deposited strain as taught herein that has been subjected to growth adaptation to particular conditions resulting in an additional benefit to the derivative strain, such as more rapid growth, better survival in the gut, enhanced phytate to propionate conversion, using methods that are well-known to the skilled person. It is preferred that the derivative or mutant is functionally equivalent to the deposited strain as taught herein. A preferred derivative or mutant as taught herein has substantially the same activity or function as the deposited strain as taught herein, i.e. has the ability to convert phytate to 3-hydroxypropionate / propionate and derivatives. The derivative or mutant advantageously provides substantially the same benefits to a mammal (e.g. humans or other mammals) administered with said derivative or mutant as would be the case upon administration of the deposited strain. The derivative or mutant strain may also be a spontaneous derivative or mutant strain having the same characteristics as described herein for the deposited strain. The term “isolated” may refer to being separated from its natural environment (which may be the gut or feces for example). The terms ‘suitable for consumption’ and ‘nutritionally acceptable’ refer to ingredients or substances, which are generally regarded as safe for human (as well as other mammals) consumption. The term ‘metabolic syndrome’ is well known by the skilled person. Within the present disclosure, the term encompasses all conditions diagnosed as “metabolic syndrome” by an (authorized) medical practitioner. For example, metabolic syndrome may be diagnosed if a patient has at least two or at least three of the following traits: - Large waist — A waistline that measures at least 35 inches (89 centimeters) for women and 40 inches (102 centimeters) for men; - High triglyceride level — 150 milligrams per deciliter (mg / dL), or 1.7 millimoles per liter (mmol / L), or higher of this type of fat found in blood; - Reduced "good" or HDL cholesterol — Less than 40 mg / dL (1.04 mmol / L) in men or less than 50 mg / dL (1.3 mmol / L) in women of high-density lipoprotein (HDL) cholesterol; -  Increased blood pressure — 130 / 85 millimeters of mercury (mm Hg) or higher; -  Elevated fasting blood sugar— 100 mg / dL (5.6 mmol / L) or higher. The term ‘insulin resistance’ is well known by the skilled person. Within the present disclosure, the term encompasses all conditions diagnosed as “insulin resistance" by an (authorized) medical practitioner. For example, insulin resistance may be diagnosed by the gold standard for determining and quantifying insulin resistance which is the "hyperinsulinemic euglycemic clamp" (DeFronzo RA, Tobin JD, Andres R (1979). The American Journal of Physiology. 237 (3): E214-23). This method measures the amount of glucose necessary to compensate for an increased insulin level without causing hypoglycemia. The procedure may take about two hours and typically involves the following steps. Through a peripheral vein, insulin is infused at 10-120 mil per m2 per minute. In order to compensate for the insulin infusion, glucose 20% is infused to maintain blood sugar levels between 5 mmol / L and 5.5 mmol / L. The rate of glucose infusion is determined by checking the blood sugar levels every five to ten minutes (Muniyappa R, Lee S, Chen H, Quon MJ (January 2008). American Journal of Physiology. Endocrinology and Metabolism. 294 (1): E15-26). The rate of glucose infusion during the last thirty minutes of the test determines insulin sensitivity. If high levels (7.5 mg / min or higher) are required, the patient is insulinsensitive. Low levels (4.0 mg / min or lower) indicate insulin resistance. Levels between 4.0 mg / min and 7.5 mg / min are not definitive and suggest "impaired glucose tolerance", an early sign of insulin resistance. Alternatively, the homeostatic model assessment (HOMA) is a method used to determine and quantify insulin resistance, as it correlates reasonably with the golden standard. See e.g. Matthews DR, Hosker JP, Rudenski AS, Naylor BA, Treacher DF, Turner RC (1985). Diabetologia. 28 (7): 412-9. doi:10.1007 / BF00280883. PMID 3899825; and / or A. S. Rudenski; D. R. Matthews; J. C. Levy; R. C. Turner (1991) Metabolism. 40 (9): 908-917. A HOMA(-IR) score that deviates from a reference range can indicate insulin resistance. Alternatively, a fasting serum insulin level greater than 25 mU / L or 174 pmol / L can be considered as indicating insulin resistance. The term “insulin resistance” as used herein refers to peripheral insulin resistance and / or hepatic insulin resistance. The term ‘insulin resistance-related conditions’ (or complications) may refer to dyslipidemia. Alternatively or additionally, the term may refer to type 2 diabetes mellitus. Further, the term ‘insulin resistance-related conditions’ (or complications) may refer to insulin-resistance in endocrine disease (e.g.,obese subjects with type 1 diabetes mellitus, Cushing's disease or lipodystrophy syndromes). As used herein, the term “identity" refers to a measure of the identity of nucleotide sequences or amino acid sequences. In general, the sequences are aligned so that the highest order match is obtained. "Identity" perse has an art-recognized meaning and can be calculated using published techniques. See, e.g.: (COMPUTATIONAL MOLECULAR BIOLOGY, Lesk, A. M., ed., Oxford University Press, New York, 1988; BIOCOMPUTING: INFORMATICS AND GENOME PROJECTS, Smith, D. W., ed., Academic Press, New York, 1993; COMPUTER ANALYSIS OF SEQUENCE DATA, PART I, Griffin, A. M., and Griffin, H. G., eds., Humana Press, New Jersey, 1994; SEQUENCE ANALYSIS IN MOLECULAR BIOLOGY, von Heinje, G., Academic Press, 1987; and SEQUENCE ANALYSIS PRIMER; Gribskov, M. and Devereux, J., eds., M Stockton Press, New York, 1991). While there exist a number of methods to measure identity between two polynucleotide or polypeptide sequences, the term "identity" is well known to skilled artisans (Carillo, H., and Lipton, D., SIAM J. Applied Math (1988) 48:1073). Methods commonly employed to determine identity or 23 similarity between two sequences include, but are not limited to, those disclosed in GUIDE TO HUGE COMPUTERS, Martin J. Bishop, ed., Academic Press, San Diego, 1994, and Carillo, H., and Lipton, D., SIAM J. Applied Math (1988) 48:1073. Methods to determine identity and similarity are codified in computer programs. For example NCBI Nucleotide Blast with standard settings (blastn, https: / / blast.ncbi.nlm.nih.gov / ). Preferred computer program methods to determine identity and similarity between two sequences include, but are not limited to, GCS program package (Devereux, J., et al., Nucleic Acids Research (1984) 12(1):387), BLASTP, BLASTN, FASTA (Atschul, S. F. et al., J. Molec. Biol. (1990) 215:403). As an illustration, by a nucleotide sequence or amino acid sequence having at least, for example, 95% "identity" to a reference sequence, it is intended that the nucleotide sequence or amino acid sequence is identical to the reference sequence except that there may be up to five-point mutations per each 100 nucleotides or amino acids of the reference sequence. In other words, to obtain a nucleotide sequence or amino acid sequence being at least 95% identical to a reference sequence, up to 5% of the nucleotides or amino acids in the reference sequence may be deleted and / or substituted with another nucleotide or amino acid, and / or a number of nucleotides or amino acids up to 5% of the total nucleotides or amino acids in the reference sequence may be inserted into the reference sequence. Preferably, the sequence identity refers to the sequence identity over the entire length of the sequence. It is further understood that, when referring to “sequences” herein, generally the actual physical molecules with a certain sequence of subunits (e.g. amino acids or nucleotides) are referred to. The term ‘about’ as used herein indicates a range of normal tolerance in the art, for example within 2 standard deviations of the mean. The term ‘about’ can be understood as encompassing values that deviate at most 10%, 9%, 8%, 7%, 6%, 5%, 4%, 3%, 2%, 1%, 0.5%, 0.1%, 0.05%, or 0.01% of the indicated value. The terms ‘comprising’ and ‘to comprise’ and their conjugations, as used herein, refer to a situation wherein said terms are used in their non-limiting sense to mean that items following the word are included, but items not specifically mentioned are not excluded. It also encompasses the more limiting verb ‘to consist essentially of’ and ‘to consist of’. Reference to an element by the indefinite article ’a’ or ‘an’ does not exclude the possibility that more than one of the elements is present, unless the context clearly requires that there be one and only one of the elements. The indefinite article ‘a’ or ‘an’ thus usually means ‘at least one’. The terms ‘to increase’ and ‘increased level’ and the terms ‘to decrease’ and ‘decreased level’ refer to the ability to significantly increase or significantly decrease or to a significantly increased level or significantly decreased level. Generally, a level is increased or decreased when it is at least 5%, such as 10%, 15%, 20%, 25%, 30%, 35%, 40%, 45%, or 50% higher 24 or lower, respectively, than the corresponding level in a control or reference. Alternatively, a level in a sample may be increased or decreased when it is statistically significantly increased or decreased compared to a level in a control or reference. Description of the figures Figure 1: Fecal phytate metabolism and identification of phytate-degrading Mitsuokella spp. a: 13C-NMR spectra of [13Ce]lnsP6 metabolism by fecal microbiome of donor A during 24h incubation. Dashed lines connect NMR signals of identified metabolites and CO2. For 3-hydroxypropionate dotted lines are used for better visibility. The final metabolic products derived from [13Ce]lnsP6 are [13C2]acetate, [13C3]propionate, and [13C4]butyrate. [13C3]3-hydroxypropionate accumulates transiently between 4.5 - 6.5 h. b: Microbial composition of fecal samples, the initial time points and end time points of phytate enrichment from donor A. Top 15 abundant taxonomic groups in the samples are shown in colors and the rest is shown as other in white, c: Changes of relative abundance of Mitsuokella jalaludinii and Mitsuokella spp. during phytate incubation and phytate consumption in fecal enrichments from donor A. Figure 2: Elucidation of phytate degradation pathway in Mitsuokella jalaludinii DSM13811T. a: Faster growth of M. jalaludinii in 10mM and 40mM phytate as compared to growth in 10mM and 40mM myo-inositol while similar metabolite production was observed, b: 13C-NMR analysis shows rapid [13Ce]phytate degradation with [13Ce]lns(2)P and [13C6]lnositol as intermediates and [13C3]3-hydroxypropionate, [13C3]lactate, [13C4]succinate, and [13C2]acetate as end metabolites, c: BIRD-{1H,13C}HMQC spectrum of the M. jalaludinii culture sample at 7.5 h. The region in which inositol polyphosphate signals are commonly found is shown. The mixture contains the starting material [13Ce]lnsP6 (purple arrows) but also the dephosphorylation products lns(2)P (blue arrows) and myo-inositol (grey arrows). Each detectable signal is annotated with the corresponding substance name and position of the inositol ring. Note that each of the detected substances exhibit four NMR signals each due to the Cs-symmetry of the six-membered inositol ring, and therefore, positions C1 and C3 are magnetically equivalent and so are positions C4 and C6. d: Log2fold change of differential expression of genes involved in phytate degradation; inositol and phosphate uptake and inositol metabolic genes comparing between phytate and inositol condition (Table S2). Predicted functional groups of these genes are indicated on the right, e: Reconstruction of the entire phytate degradation pathway based on genomic, transcriptomic and metabolomic analyses. The genes have been identified a genome from GenBank (BioProject PRJNA223472) of M. jalaludinii DSM13811T and re-annotating the genome in Rapid Annotation using Subsystem Technology (RAST). Figure 3: Mechanistic insight into the synergy between M. jalaludinii and A. rhamnosivorans in phytate degradation, a-b: Metabolite production and substrate consumption by monoculture of M. jalaludinii (a) and coculture of M. jalaludinii and A. rhamnosivorans (b) in phytate (n=2 biological replicates). Data are presented as mean values±SD. c: 13C-NMR spectra of [13Ce]lnsP6 metabolism by coculture of M. jalaludinii and A. rhamnosivorans during 48 h incubation. Dashed lines connect NMR signals of identified metabolites and CO2. Dotted lines are used for 3-hydroxypropionate to provide better visibility. The final metabolic products derived from [13Ce]lnsP6 are [13C2]acetate, [13C3]propionate, [13C3]lactate, [13C3]3-hydroxypropionate, [13C4]butyrate, and [13C4]succinate. [13C4]succinate is again formed as a mixture with partially or non-13C-labeled succinate. The same InsP intermediates can be observed between 2 - 7.5 h as for the monoculture (Fig. 3b). d: M. jalaludinii (MJ): Log2fold change of differential expression of genes involved in phytate degradation; inositol and phosphate uptake and inositol metabolic genes comparing between monoculture and coculture. Functions of these genes are indicated on the right. e: A. rhamnosivorans-. Log2fold change of differential expression of genes involved in inositol uptake, inositol metabolic genes, propionate production and 3-hydroxypropionate transport comparing between MA_I (coculture in myo-inositol) versus A_l (monoculture in myo-inositol); MA_P (coculture in phytate) versus A_l (monoculture in myo-inositol); MA_P (coculture in phytate) versus MA_I (coculture in myo-inositol). Predicted functional groups of these genes are indicated on the right. The transcriptomic analysis was performed in biological triplicate, f: Reconstruction of synergistic interaction between M. jalaludinii and A. rhamnosivorans in phyate. M. jalaludinii uses periplasmic phytase to dephosphorylate phytate rapidly to lns(2)P and inositol, which can subsequently be taken up and be used to produce succinate, acetate, lactate and 3-hydroxypropionate. The produced 3-hydroxypropionate is released into the medium and inhibits myo-inositol uptake by A. rhamnosivorans. A. rhamnosivorans, in turn, metabolizes 3-hydroxypropionate via a 3-hydroxypropionate scavenging pathway to produce propionate, conserving energy by coupling the electrochemical gradient generated via a membrane bound Rnf complex with ATP synthesis. Figure 4: In vivo phytate conversion by M. jalaludinii and A. rhamnosivorans in mice. a: experimental design of in vivo microbial phytate conversion. Three groups of 8 mice were treated with either phytate (0.1mg / g body weight) alone, or phytate (0.1mg / g body weight) together with M. jalaludinii (10A9 cells per dose) or phytate (0.1 mg / g body weight) with M. jalaludinii (MJ) and A. rhamnosivorans (A.rham) (10A9 cells per strain per dose) every second day for two weeks. After two weeks, a [13Ce]phytate oral challenge of the same bacterial dosage were performed for the respective group. A group of four mice was sacrificed after 3 h or 6 h. Cecum and plasma samples were harvested for inositol phosphate extraction and measurement while colon samples were used for quantification of M. jalaludinii 26 and A. rhamnosivorans via qPCR. Significant lower levels of cecal [13Ce] phytate in microbial treatment groups compared to control groups at 3 h (b) and 6 h (c) after oral challenge. Relative abundance of Mitsuokella jalaludinii at 6 h (d) and A. rhamnosivorans at 6 h (e) in murine colon samples quantified via qPCR in three groups: Phytate (purple); Phytate_A.rham_MJ (blue) and phytate_MJ (orange). Quantification of three [13Ce]lnsPs species: lnsPs[3OH] at 6 h (f), lns(1,2,5,6)P4 at 6 h (g); lnsPs[5OH] at 3 h (h) in the cecum samples by BIRD-{1H,13C}HMQC spectra at 6 h and 3 h after oral challenge. Relative abundance of A. rhamnosivorans (g) and Mitsuokella jalaludinii (h) in colon samples quantified via qPCR in three groups: Phytate (purple); Phytate_A.rham_MJ (blue) and phytate_MJ (orange), i: Postulated phytate degradation routes in mouse cecum. Black arrows indicate the route involved Mitsuokella jalaludinii and A. rhamnosivorans while grey arrows are routes by the mouse microbiome alone. Two arrows indicate conversion required more than one reaction. Shown values are means ± SEM (n=4) and statistical analysis was performed using one-way ANOVA. Only significantly different comparisons are shown. *P<0.05; **P<0.01; ***P<0.001. Figure 5: Propionate and phytate-derived bacterial metabolites improved epithelial barrier integrity via activating tight junction genes, a: 20mM propionate co-incubation increased TEER values as compared to the control, b: Increased activity of tight junction genes Claudin-1, Claudin-2 and E-cadherin upon propionate exposure. Increased barrier integrity when Caco-2 cells were incubated with 10% bacterial supernatant from a coculture (M. jalaludinii and A.rhamnosivorans) compared to 10% the medium control, d: Increased activity of tight junction genes Claudin-1 and E-cadherin upon bacterial supernatant exposure compared to the medium control. Shown values are means ± SD (n=4 biological replicates) and statistical analysis was performed by two-way ANOVA. Only significantly different comparisons are shown. *P<0.05; **P<0.01; ***P<0.001; ****P<0.0001. Figure 6: Concentration independent synergy between M. jalajudinii and A. rhamnosivorans for phytate breakdown, a: Growth curves of co-cultures (blue) of M. jalajudinii and A. rhamnosivorans and monocultures (pink) of M. jalajudinii in 10 mM, 20 mM, and 40 mM phytate during 24 h incubation, b: End metabolite production of the co-cultures and monocultures of cocultures (blue) of M. jalajudinii and A. rhamnosivorans and monocultures (pink) of M. jalajudinii in 10 mM, 20 mM, and 40 mM phytate after 24 h incubation. Shown values are means ± SD (n=3). Figure 7: 3-hydroxypropionate metabolism by A. rhamnosivorans. A. rhamnosivorans was found to co-metabolize 3-hydroxypropionate. Fermentation profiles are shown of A. rhamnosivorans incubated in glucose (a) (a); glucose and 3-hydroxypropionate (b); 3-hydroxypropionate (c) and myo-inositol plus 3-hydroxypropionate (HP) (d) by Anaerostipes rhamnosivorans. All experiment were performed in biological duplicate. Shown values are means ± SD (n=2). Figure 8.- Transcriptome analysis reveals synergy study M. jalaludinii and A. rhamnosivorans. Metabolite production and substrate consumption of phytate (a) and myo-inositol (b) by monocultures and co-cultures of M. jalaludinii and A. rhamnosivorans. Cell numbers of M. jalaludinii and A. rhamnosivorans quantified by qPCR in the coculture on myo-inositol (c) and phytate (d). e: Principal coordination plot of the transcriptional profiles obtained by RNA-seq of M. jalaludinii when grown on phytate (green / purple) or myo-inositol (red / blue) in the presence (blue / purple) or absence (red / green) of A. rhamnosivorans (Table S2-7). Ordination was based on centered log transformed counts and Euclidean distance. The experiment was performed in biological triplicate. Shown values are means ± SD (n=3). Figure 9: Reconstruction of 3-hydroxypropionate conversion to propionate by A.rhamnosivorans. 3-hydroxypropionate is imported via a permease (AR1Y2_1114) and further converted to 3-hydroxy propionyl-CoA, Acryloyl_CoA, propionyl-CoA and eventually propionate via oxoacid CoA transferase (AR1Y2_1115), dehydratase (AR1 Y2_1116), acad-etf complex (AR1Y2_1112, 1113 and 1117). Acyl-CoA dehydrogenase / Etf complex (AR1 Y2_1112, 1113 and 1117) is predicted to be involved in energy conservation via by coupling the electrochemical gradient generated via a membrane bound Rnf complex with ATP synthesis. Figure 10: Enrichment of 13C-short chain fatty acids in mouse ceca upon bacterial oral challenge. Relative abundance of one 13C (ml); two 13C (m2); three 13C (m3) and four 13C (m4) of 13C-propionate (a); 13C-butyrate (b) and 13C-acetate (c) in mouse cecum in three treatment groups: Phytate (brown); Phytate_A.rham_MJ (blue) and phytate_MJ (green). Shown values are means ± SD (n=4 except Phytate_MJ at 3h (n=2) and Phytate_A.rham_MJ and Phytate_MJ at6h (n=3) due to technical issues during derivatization). Figure 11: Production of bacterial supernatant of the co-culture for epithelial barrier function test using a Caco-2 cell model. The experiment was performed in YCFA medium supplemented with phytate. Around 20 mM phytate was repeatedly added after adjusting the pH to neutral (~7). Bacterial supernatants was collected before and after substrate addition for 5 days. In the end of the growth, propionate, acetate and succinate were found as major end metabolites with nearly 90 mM propionate. Red arrows indicate the time of phytate addition. Sequence listing PTP-like phytase MJ_0021 Nucleotide sequence (SEQ ID NO:1) ttgctttatcatatcctgcacaaaaaaataaatttctctctgctgctggccgtctgtctgatactaataaatgcaccagccatcgctgc ggctgcagttcctgaggaacctgcctggcggctcgatgcggccatcggcagtgacgagccgattcatttccgccgcgatgcag atcttaaaatcgcgggcggcgggcagccgacaaaagaagtcctcgcccatctgcccgcacttctcggcgtcccgcccgatat gcctatctgggatattgacctgcggcaggaatcccacggctttctcaatcatgcggccgtgagctggcatggcccgcagaatgc ggcgaatcgcggccttgccgcaacagaagtcgaacaagacgaaacggcccgcctgcaggaggcccttggacaccttgtcc aagccctgccgatgggccgctacgatgaagaacatatcaaaacatcttttgctgaaccagtagagagctggtcaacggaacg cgaactggcgcgcagagccgggctcggctacaagcgctttgccgcgaccgatatggaatggccggggcctgcggtcatcga tgacttcgtcgacttttaccgcagcctgccaaagaatcacggctggctcttcttccactgccaggccggacagggccgtacgac gacgtttatggtactctatgagctgctggaacatccatccgtcaccgcagatgaggcaattgcgcatcagcgcagcctaggcgg tgccgacctttcaagcgggccgcgttatcatggcctgcagcttttcgcccattatgtcaaagaaaactgtgcgtcaaattttcagca aacatggagccagtggctggctgcccgacaaaattcttactaa Amino acid sequence (SEQ ID N0:2) MLYHILHKKINFSLLLAVCLILINAPAIAAAAVPEEPAWRLDAAIGSDEPIHFRRDADLKIAGG GQPTKEVLAHLPALLGVPPDMPIWDIDLRQESHGFLNHAAVSWHGPQNAANRGLAATEV EQDETARLQEALGHLVQALPMGRYDEEHIKTSFAEPVESWSTERELARRAGLGYKRFAAT DMEWPGPAVIDDFVDFYRSLPKNHGWLFFHCQAGQGRTTTFMVLYELLEHPSVTADEAIA HQRSLGGADLSSGPRYHGLQLFAHYVKENCASNFQQTWSQWLAARQNSY major myo-inositol transporter lolT_MJ_0380 Nucleotide sequence (SEQ ID N0:3) atggcggaatcatctcatcgcaaatacctcaagcgtgtcacagtcgtctcgacgttcggtggcttgctcttcggttatgacaccgg cgtcatcaacggcgcccttgccttcatggcccgtccggatcagttgaacctgactccggcagtggagggcttcgtggccagtgg cctgctcttcggtgcggccatcggttcgttcttcggcggccgtctttcggatgctgagggacgccgcaagatgctgctttgcctggc agtcatcttcttcttcgcagccatcggctgctcgctgtcaccgacggctggcatcctcatcgcctgccgcttcgtcctcggcctggc agtcggtggtgcttcggtcacggtacctgcttacctggcagagatggcaccggccgacaggcgcggccgcatggtcacccag aatgagctcatgatcgtcacgggccagctgctcgccttcatcctcaacgctatcctcggcgtcaccttcggtgaggtcggccaca tctggcgttacatgctcgcactcgcatccatcccggctgtcgtgctctggttcggcatgctcgtgatgccggagagcccgcgctgg ctgctgctgcagggccgtgtcagcgatgcgatgcaggtactcaagaagatccgcgatgagcgcatggccatcgccgagctca acgagatccaggacagcatcgattcggagaagcatctcgacaaggctggttacaaggacctggcaacgccttggatccgcc gcatcgtcttcatcggcatgggcgtctccatctgccagcagatttctggcgtcaactccatcatgtattacggcacgcagatcttga cgcaggccggcttctcgacggaagccgcactgatcggcaacatcgccaacggcacgatctccgttgctgccacaatctttggc atgtggctcatgacgcgtcacggccgtcgtccgctcatcatgacgggccagatcggcacgatggcctgcctctgcgcgatcgg cgttctctcgaatctgcttgccggcaccgagatcctgccgttcgtcgtcctttcgctgaccgtcaccttcctgttcttccagcagggttt cctttccccggtcacctggctgctgctctcggagctcttcccgctgcgcatccgcggcatgggcatgggctgcgccgtcctctgcc tctggctgacgaacttctgcatcggctcggccttcccgtcgctgctctactcgttcggcctctcggctacgttcttcatcttcgcggcc atcggccttctcggcctcgccttcgtctacaagttcgtgccggagacgcgtggccgcacgctcgagcagatcgagcatgacttc cgccatcacggtgagaagagcgttcactgcgaagagaaagcttga Amino acid sequence (SEQ ID N0:4) MAESSHRKYLKRVTWSTFGGLLFGYDTGVINGALAFMARPDQLNLTPAVEGFVASGLLF GAAIGSFFGGRLSDAEGRRKMLLCLAVIFFFAAIGCSLSPTAGILIACRFVLGLAVGGASVTV PAYLAEMAPADRRGRMVTQNELMIVTGQLLAFILNAILGVTFGEVGHIWRYMLALASIPAVV LWFGMLVMPESPRWLLLQGRVSDAMQVLKKIRDERMAIAELNEIQDSIDSEKHLDKAGYK DLATPWIRRIVFIGMGVSICQQISGVNSIMYYGTQILTQAGFSTEAALIGNIANGTISVAATIF GMWLMTRHGRRPLIMTGQIGTMACLCAIGVLSNLLAGTEILPFVVLSLTVTFLFFQQGFLSP VTWLLLSELFPLRIRGMGMGCAVLCLWLTNFCIGSAFPSLLYSFGLSATFFIFAAIGLLGLAF VYKFVPETRGRTLEQIEHDFRHHGEKSVHCEEKA myo-inositol 2-dehydrogenase Nucleotide sequence (SEQ ID NO:45) atgattaaagttggtattatcggtgcaggccgtatcggtcatgtacatggcgagagcatctcgaagttcgtcaagaacgcaacg gtcaagacgattgctgatccgttcatgaacgagaagacggaagcttgggcaaagtccctcggcatcgagaagacgacgaaa gattaccatgagatcctcaacgatcctgaaattgaagccgtcctgatctgcgcttccacggaccagcattccccgctctccatcg aagcactgcgcgccggcaagcacgtcttctgtgagaaaccgattgaccatgatgtcaataagatcaaggaagttctcgacgtc gtcaaagagacgggcaagaaataccaggtcggcttcaaccgccgctttgaccacaacttcaaggctatccgcgatgctgtcgt cgccggaaaagtcggcaagcagcagatcatcaagatcacgtcccgtgatccggaaccgccttccatcgattacgtaaagattt ccggcggtatcttcctcgacatgacgattcatgatttcgatatggtccgctatctctccggcgcagaagtcgaggaagtatatgca gagggctctgtcaccgtcgatccggaaatcggcaaggctggcgacatcgatacggccatcatcacgctgaagctcgacaatg gcgctacggctgtcatcgacaactgccgtgccgcttgctatggctatgaccagcgcgctgaagtcttcggcacaaagggctgc gtcgccatctccaacgattcggattccaatgcagtctacagctgcaaggacggcgtcatcgccgagaagccgatgttcttctttct cgagcgctacatgatggcttatgcaaacgaagtcaatcagttcgtcgaagcgatcgtcaacgacacgccgaccccggtcaat gcaaacgacggcctgcagccggtcctcattggcctcgctgccaagaagtcggtcgaagagcatcgcccggtcaagattgca gagatccgcgcccagtacggcctctga Amino acid sequence (SEQ ID NO:46) MIKVGIIGAGRIGHVHGESISKFVKNATVKTIADPFMNEKTEAWAKSLGIEKTTKDYHEILND PEIEAVLICASTDQHSPLSIEALRAGKHVFCEKPIDHDVNKIKEVLDVVKETGKKYQVGFNR RFDHNFKAIRDAVVAGKVGKQQIIKITSRDPEPPSIDYVKISGGIFLDMTIHDFDMVRYLSGA EVEEVYAEGSVTVDPEIGKAGDIDTAIITLKLDNGATAVIDNCRAACYGYDQRAEVFGTKGC VAISNDSDSNAVYSCKDGVIAEKPMFFFLERYMMAYANEVNQFVEAIVNDTPTPVNANDG LQPVLIGLAAKKSVEEHRPVKIAEIRAQYGL Inosose dehydratase_MJ_0910 Nucleotide sequence (SEQ ID N0:5) atggctaatatcaaacttggtatcgctccgattgcttggacgaacgacgacatgccggatctcggcaaagagaatacgtttgaa cagtgcgtcagtgagatggcactggctggcttcacgggctgcgagatcggcaacaagtacccgaaagatccggctgtcctca agaaagcactcgaccttcgcggactccagatcgccagcgcatggttcagctcctacctcctcacgcagccgtacgagcaggt cgagaaggacttcatcaagcactgcgaattcctcaaggccatgggcgcgaagttctgcaacgtcgcagagcagggcacga gcgttcagggcaagctcgacaaggctgtcttccgcgacaagccgcacaacacggaagagcagtggaagacgctcgctgag ggcctcaacaagctcggtgctgtcgccaagaagattggcctgacgatgacgtaccatcatcacatgggcacctgtgtccagac gacggaagagattgaccgcctcatggagatgacggatccagacctcgtcttcctgctctacgatacgggccatctcgtctgctc cggtgaggacccgatctacatcctcaagaagtacctgccgcgcatccgtcacgtacatctcaaggacatccgcatggacatcc gcaacaaagtcaaggaagagaacatgagcttcctcgcaggcgtccgcgcaggcatgttcacggtcccgggcgatggcgact tcgacttcggtccggtcttcgacatcatcaatgacagcgactacgatggctggttcatcgtcgaagctgagcaggatccggcca aagccaacccgctcgagtacgcgatcaaagctcgcaagtacatcaaggaaaaagcacatatctga Amino acid sequence (SEQ ID N0:6) MANIKLGIAPIAWTNDDMPDLGKENTFEQCVSEMALAGFTGCEIGNKYPKDPAVLKKALDL RGLQIASAWFSSYLLTQPYEQVEKDFIKHCEFLKAMGAKFCNVAEQGTSVQGKLDKAVFR DKPHNTEEQWKTLAEGLNKLGAVAKKIGLTMTYHHHMGTCVQTTEEIDRLMEMTDPDLVF LLYDTGHLVCSGEDPIYILKKYLPRIRHVHLKDIRMDIRNKVKEENMSFLAGVRAGMFTVPG DGDFDFGPVFDIINDSDYDGWFIVEAEQDPAKANPLEYAIKARKYIKEKAHI 3D-(3,5 / 4)-trihydroxycyclohexane-1,2-dione hydrolase_MJ_0909 Nucleotide sequence (SEQ ID N0:7) atggctaagacaatcagactcacggtagcacaggctctcgtgaagttcctcaataatcagtatgtagaatttgacggcaagga agtgccgatgttcgaaggcatcttcggcatcttcggccacggcaatgtcatcggcatcggccaggctctcgaagaggatccgg gccatctgatcatgcgcatgggccgcaatgagcagggcatggcacacgcagcgatgggctttgccaagcagaagcgccgc aagcagatgtacgcctgcacgtcttccgtcggcccgggcgctgccaacatggtcacggcagctgctacggctacggcaaact gcatcccagtcctgttcctgccgggtgacacgtacgccgaccgccagccggatccggtactccagcagatggagcagacggt aagcctgacgacgacgacgaacgacgccttccgcgctgtctgcaaatactgggaccgcgtcacgcgtcctgaaatcctcatg acggcctgcatcaatgcgatgcgcgtcctgacggatccggctgagacgggtgctgtctgcatcgctctgccgcaggatgtcga aggcgaggcctgggattacccagattacttcttccagaagcgcgttcatcacatcgaccgcgtaaaaccgacggagcgcgcc attgaagaggctgtcaaggccatcgcgaaggctgagcgcccgctgatgatcttcggcggcggcgtcaagtattccgaggcag aggctgtcttccagaaattcgctgagaagtacggcatcccgttcggcgagacgcaggccggcaagggcacgattacgtggg agcatgagctcaacatgggcggcgtcggcgagacgggcggccttgcagccaacacgcttgcaaaagatgcagatgtcgtc atcggcgtcggcacgcgatacacggacttcacgacgtcctctaagtggatcttccagaacccgaacgtccagtacgtcaacat caacgtctcccgcttccatgcctacaagctcgatggcatccaggttgtcggcgatgccggcgcagcactcgagatgctcgatga ggccctcggcaagacgggctaccatgtgtcggatgcctatgctgcggacatcaaggcagccaaggaagcctatacgaagg aagtcgagcgtgtcttccacatccagttcggcgacaacttcgtgccggaagtcgacgatgatttcgattacaaggctgcagaga aagcctataaagaggcagtcggcgagacgctgccgcagacgcgcgtcctcggtctgctcgaagagcacatggatccgaac ggcatcatcgtcggtgcatcgggctccctgccgggcgacctgcagcgcgtatggcgtccgaagacggttggcagctaccatgt cgagtacggcttctcctgcatgggttatgaagtcaacgcagcactcggcgtcaagctcgctgagccgcagcgcgaagtctatg cgctcgttggcgactacgcttacatgatgctccattcggaactgccgacgtccatcgctgagggcaagaagatcaacgtcatcc tgttcgacaacatgcagggcggctgcatcaacaacctcgagatcggccatggccagggcagctacggcacggagttccgctt ccgcaacgagaagacgggccagctcgacggtgcctatgtaccggttgacttcgccatgaacgccgcttcctacggctgcaag agctacacggctcataccgaggaagagctcatcgcggccatcgaagatgctaagaagcagaaagtctcgacgctcatcgac tgcaaggtcatgccgaagacgatggttcacggctacggtgactggtggcgtgtcggcgtcgcgcaggtctccaagagcaaga agatccacgactgctacgagaatctcatgaagccgcattacgatgcagctcgcaagtattga Amino acid sequence (SEQ ID N0:8) MAKTIRLTVAQALVKFLNNQYVEFDGKEVPMFEGIFGIFGHGNVIGIGQALEEDPGHLIMRM GRNEQGMAHAAMGFAKQKRRKQMYACTSSVGPGAANMVTAAATATANCIPVLFLPGDT YADRQPDPVLQQMEQTVSLTTTTNDAFRAVCKYWDRVTRPEILMTACINAMRVLTDPAET GAVCIALPQDVEGEAWDYPDYFFQKRVHHIDRVKPTERAIEEAVKAIAKAERPLMIFGGGV KYSEAEAVFQKFAEKYGIPFGETQAGKGTITWEHELNMGGVGETGGLAANTLAKDADVVI GVGTRYTDFTTSSKWIFQNPNVQYVNINVSRFHAYKLDGIQVVGDAGAALEMLDEALGKT GYHVSDAYAADIKAAKEAYTKEVERVFHIQFGDNFVPEVDDDFDYKAAEKAYKEAVGETL PQTRVLGLLEEHMDPNGIIVGASGSLPGDLQRVWRPKTVGSYHVEYGFSCMGYEVNAAL GVKLAEPQREVYALVGDYAYMMLHSELPTSIAEGKKINVILFDNMQGGCINNLEIGHGQGS YGTEFRFRN EKTGQLDGAYVPVDFAM NAASYGCKSYTAHTEEELIAAIEDAKKQKVSTLID CKVM PKTMVHGYGDWWRVGVAQVSKSKKIH DCYEN LM KPHYDAARKY 5-deoxy-glucuronate isomerase_MJ_0908 Nucleotide sequence (SEQ ID N0:9) atgagattcggtcgcttaggtcagctcaagcacggctacaatgcaatgacgacgcgcgagagcgatatgctcatggatatcgg ttaccaggagatggatgagaacgagatcgtcgagttcgaagatccccttcaggagacggccttcgtcatcacgacgggtgatg tggagatctgctggaatggcaagaaagagctcatgcatcgcgagtcgctgctcgacgagaacccgtactgcctgcacgtgcc gcacggcgtcaaggtcgtcgtcaaggccctgaagaaatcggagctcctgatccagaagacgctcaacgaccgcgactttga gccggtcttctaccgtccgaaagatgtccaggctgacgttttcggcggcggcgtatggcagggcacggcagagcgcacggtc cgcacgatcttcgattacgacaatgcgccgtactccaacatggtcaacggcgaagtcatcatgacgccgggctgctggacgg gctacacgccgcacaatcatccgcagccggaagtctacacctacaaagtcgaccgtccgcagggctttggctgtgcgttcatc ggcgacaacgtcttcaagatcgaggacaacacttggtcggagatctcgggcggctacatgcatccgcagtgcgcagctcctg gctacgccatctggtacagctggatgattcgtcatctcgacggcgatccgtggaagaagacgcgcaatgacctgccggagca cacctggctgctcgagccggatgccgattcgaagatctggcagccgcacaagaagtga Amino acid sequence (SEQ ID NO: 10) MRFGRLGQLKHGYNAMTTRESDMLMDIGYQEMDENEIVEFEDPLQETAFVITTGDVEICW NGKKELMHRESLLDENPYCLHVPHGVKVWKALKKSELLIQKTLNDRDFEPVFYRPKDVQ ADVFGGGVWQGTAERTVRTIFDYDNAPYSNMVNGEVIMTPGCWTGYTPHNHPQPEVYT YKVDRPQGFGCAFIGDNVFKIEDNTWSEISGGYMHPQCAAPGYAIWYSWMIRHLDGDPW KKTRNDLPEHTWLLEPDADSKIWQPHKK 5-keto-2-deoxygluconokinase_MJ_0907 Nucleotide sequence (SEQ ID NO:11) atggcactcattagctttgatgaaaacaagaaacgcgatgtcgtcctgattggccgcgtcacgctggatttcaatccgaatgaac tgaaccgcacgctggacaaggtcaagactttctccatgtacctcggcggttcgccgggaaacatggctgtcggcatcaacaag ttgggcaagaacgtcggtttcatcggctgtgtatctgacgaccagttcggcgacttcgtcctcaattacttcaatgagcgtggcatt gacacgtcccagatgacgcgcgccaagaacggcgagcgcatgggtctgacgttcacggagatcaagagcccgacggagt cgagcatcctgatgtaccgcgaccaggtcgctgacctcgagattgcgccggaagatgtcgatgagcagtacatcgctgacag caagatcctgattgtctccggtacggcgctctcgaagagcccgtcgcgtgaggcatgcctgctggctgtccagtatgccaagaa acatggcacgcgcgtcatcttcgatatcgactatcgcccgtacagctggcgcagcaagaaggacatccagatctactactcgtt gcttgcgagcatggccgatgtcatcatcggttcgcgcgatgaggtcaacctcacggaaggtctcgatgaggaggcaacggag ccggcagatcacgtcatcgctgagaagtacatcgagcagggtgccaagattgtcatcatcaagcacggcaagaagggctcg atcgcttacacggccgacaagaaggcctacaaggttgagtcgtaccacatcaagctgctgaagtcgttcggcggcggcgatg cgtatggcagcgcctttgtctatggcctgctcgcaggctggacggtgccgcaggctctgcagcacggcacggcacacgccgct atggtcgtcgcaagccacagctgctcagatgccatgcagacggtcgagcagattgatgctttcatgcaggaacataaagacg agaaagtcatcacggaattggattgggaggcagcattatga Amino acid sequence (SEQ ID N0:12) MALISFDENKKRDWLIGRVTLDFNPNELNRTLDKVKTFSMYLGGSPGNMAVGINKLGKNV GFIGCVSDDQFGDFVLNYFNERGIDTSQMTRAKNGERMGLTFTEIKSPTESSILMYRDQVA DLEIAPEDVDEQYIADSKILIVSGTALSKSPSREACLLAVQYAKKHGTRVIFDIDYRPYSWRS KKDIQIYYSLLASMADVIIGSRDEVNLTEGLDEEATEPADHVIAEKYIEQGAKIVIIKHGKKGSI AYTADKKAYKVESYHIKLLKSFGGGDAYGSAFVYGLLAGWTVPQALQHGTAHAAMVVAS HSCSDAMQTVEQIDAFMQEHKDEKVITELDWEAAL 5-keto-2-deoxy-D-gluconate-6 phosphate aldolase_MJ_0906 Nucleotide sequence (SEQ ID NO:13) atgccactcgtacatttgacagacctcataagcaagccagacaacacatatgcaattggcgcgttcaatgtctcggatatggag atggccatgggtgccatcaaggcggcagaagagctccatgctccgctgatcctgcagattgcagaaggccgcctgcgctact cgccgctcgacctgcttggccccgtgatgatcgcggccgccaagaagtgctcgatgccgacggccgttcatctcgaccacgg cagcacgatggagacgatcaagcttgcgctcgacctcggcttcacgtccgtcatgttcgacggttcgaaatatccgctcgatga gaacatcgcccgcacgcaggaagtcgtcaagcttgcgaggagctacggcgctgacgtcgaaggtgagatcggccgcgtcg gcggcgcggagggcgactacaagagcgtggatgtcctcgtcacgagcgtcgaggaagccaagcgctttgccgaggaatcc ggcatcgatgcgatggccgtcgcaatcggaacggcacatggcaactacaaggagaagccgcagctccgcatcgaccgcct caaggaaatccatgcggccgtcaagacgccgctcgtcctgcacggcggcacgggcctgacggaagaggatttccggacttg ccttgccaacggcatccagaagatcaacatcgccacggcgtcgtacgacgcttcggcagcgaagataaaggaagtcgctgc agcgaacccgcaggcaaagtacttcgatttcagcgatgccatcgtacagggcacctacgagaatgtaaagaaacacatgca catcttcgggctcgaacagaaggcatga Amino acid sequence (SEQ ID N0:14) MPLVHLTDLISKPDNTYAIGAFNVSDMEMAMGAIKAAEELHAPLILQIAEGRLRYSPLDLLG PVMIAAAKKCSMPTAVHLDHGSTMETIKLALDLGFTSVMFDGSKYPLDENIARTQEWKLA RSYGADVEGEIGRVGGAEGDYKSVDVLVTSVEEAKRFAEESGIDAMAVAIGTAHGNYKEK PQLRIDRLKEIHAAVKTPLVLHGGTGLTEEDFRTCLANGIQKINIATASYDASAAKIKEVAAA NPQAKYFDFSDAIVQGTYENVKKHMHIFGLEQKA 2-hydroxy-3-oxopropionate reductase_MJ_1291 Nucleotide sequence (SEQ ID N0:15) atgaagaagattggttttgtaggactgggcatcatgggcaaaccgatggttcgcaatctcttgaaagcaggctttgctgtgactgt ctacgatatcgtggaggatgcagtcaaggcactggtagaagagggggcaaagggtgcttcttcagcaaaggaagttgcagc ggatcaagacgtcgtcatcacgatggtaccgagtggtccgattgtccgctcgttgctcaagggcgatgacggcatcctggctgg tgtcaaggaaggcacggtcatcgtggatatgagctccgtcacgccggtggaatcgaaggaatttgctgaactggcagcagag aagggatgcgcgttcctcgatgcaccggtcagcggcggtgagccgggtgcagttgcaggttcgctggccattatggtcggcgg tgaagaagctgtcctcaatcaggttcgcgatgtctttgaagcgatgggatcttccatcacactggtcggaccgacgggcagcgg ctcggtgacgaaactggccaatcaggtcatcgtcaacctcaatatcgcagcggtagccgaagcgctcatcctttcgaccaagg ccggcgcggatccgaagaaagtctacgaggcaatccgcggcggtctggctggcagcacggtgctggatgctaaggcaccg atgatgttccgccgcaatttcaaaccgggcggaccgatcaagattaacctcaaggacatcacgaatgtcatggatacggcca agaaactcgacctgccactcgtcatgacgggggtgctggagcagatcatgcacagcttgaaggcgacgggccatctgatgg atgatcacagtggcattgtccagttctatgagaatatttccggtgtcgtagtcaagacgcatgaagagtga Amino acid sequence (SEQ ID N0:16) MKKIGFVGLGIMGKPMVRNLLKAGFAVTVYDIVEDAVKALVEEGAKGASSAKEVAADQDV VITMVPSGPIVRSLLKGDDGILAGVKEGTVIVDMSSVTPVESKEFAELAAEKGCAFLDAPVS GGEPGAVAGSLAIMVGGEEAVLNQVRDVFEAMGSSITLVGPTGSGSVTKLANQVIVNLNIA AVAEALILSTKAGADPKKVYEAIRGGLAGSTVLDAKAPMMFRRNFKPGGPIKINLKDITNVM DTAKKLDLPLVMTGVLEQIMHSLKATGHLMDDHSGIVQFYENISGVWKTHEE D-beta-hydroxypropionate permease_MJ_0911 Nucleotide sequence (SEQ ID N0:17) atgggcatcagcatgattgtcttcagcctgatacttttgatgttcttcgcgtatcgtggctattccatcatcttcatcgcaccgattttcgc cgtcgtcgccgccatcggcagcggccacgcctccatgccggtctacagtgagatctatatgacgaaagccgcggagtacatc aagacgtattaccccgtcttcctgctcggcgccgtcttcgccaagatcatggagcagggcgggctcgcggcggccgtggccga caagatcgtctcggcgctgggccgcgacaaggccattctggccgtactgctcggatgcggcgtcctgacgtacggcggtctctc tgtcttcgtcgtcgcctttgtcatgtacccatttgctgccatcctcttcaagcaggctgatatcccgaagcgtctgttgccggggctgct ctggatgggtatcttcacctacagcatggtggccatcccgggcacaccgcagatccagaacatcattccgacgtcgttctttggc acttcgacctggtcggctccggtgctcggcctcatcggtgccgtgctctacttcggactggcctggggctggatcagctatcgcca caagaaactcaaggcaaagggtgagggatacggtcaccatgtgctcaatgagccggaggagtcgcgggaggctctgccgg actggcgcctgtcctcactgccgctgcttctcgtcatcgtgctgaatctcctgatcagcaatccgttccactgggattgggcgtacc actgggatccggaaagcctcgacagtttcatcccactgcacctctccctgctcgcgggcggcgtcgacaaggtacaggccatc tggtccatcaatgcggctcttatcgtgagctccatcgtcgcggccatcatcggccgcagacggctgagactcaagggcggtctc tcaaagcccatcaacacgggagccatcggctcgacgacggccatcctcaacgtagcttcaggctatgcctacggctgtgtcat cgcagccttgccagccttcacgatcatcaaggaagcattgctcggcctgcacctcggcgacggcccgctgatgtctgccatcgt gacgacgggcatcatgacgggcgtcacgggctcttcctcgggcggcatgacgattgccctcggcatgctcggacaggagtgg ctggcctgggcgcagcagatcggcatgagtgcagatgtcctgcaccgcatcatctgcatggcctctgagtgcatcgacaccgt gccgcagtcgggcgcactcgtcacactgctcgccgtctgcggcctgacgcatcgcgagtcgtattacgacgttgtgatcctgac gctcctgaagacgcttgtcgtcttcgcctgcctgggcgtctacctgatgacaggtattgaatga Amino acid sequence (SEQ ID NO: 18) MGISMIVFSLILLM FFAYRGYSII Fl API FAVVAAIGSGHASM PVYSEIYMTKAAEYIKTYYPVF LLGAVFAKIMEQGGLAAAVADKIVSALGRDKAILAVLLGCGVLTYGGLSVFWAFVMYPFAA ILFKQADIPKRLLPGLLWMGIFTYSMVAIPGTPQIQNIIPTSFFGTSTWSAPVLGLIGAVLYFG LAWGWISYRHKKLKAKGEGYGHHVLNEPEESREALPDWRLSSLPLLLVIVLNLLISNPFHW DWAYHWDPESLDSFIPLHLSLLAGGVDKVQAIWSINAALIVSSIVAAIIGRRRLRLKGGLSKP INTGAIGSTTAILNVASGYAYGCVIAALPAFTIIKEALLGLHLGDGPLMSAIVTTGIMTGVTGS SSGGMTIALGMLGQEWLAWAQQIGMSADVLHRIICMASECIDTVPQSGALVTLLAVCGLT H RESYYDVVILTLLKTLVVFACLGVYLMTGIE phosphate ABC transporter PstS_MJ_0658 Nucleotide sequence (SEQ ID NO:19) atgaagggagccgaagggctccagggttccaatcagcaagtgatttggggaggaaataatatgttcaacaagatgaagaaa cttctttccgtcggtgctgttgtcgcgagtgcggcagtgctgctggcgggctgcggcggtggcagccagcaggcttccagctcttc tggcagcgcagcacaggaaatctccggcaagatctcagcgtcgggctcgacggcactcctgccgctcttgaagccggcaca ggaagccttccaggacaagtacgataaggtgacggtcaacatcgcaggcggcggttcgttcacgggtatgaaccaggtcgc agagggatcggtccagatcggcaactcggatgtcaacctgccggatgagtacaaggacaagggcctcgtcgaccacaagg tcgtcgttgagccgttcgtcttcatcgtcgacaagaacaacaaggtcgacaacatcacgaagcagcaggtcatcgacatcctg acgggcaagatcacgaactggaaggaagtcggcggcgatgaccagccgatcacgctgatccaccgtgcaaagtcctcggg ttcccgtgcgacgatcagcgatgtcgtcctcaagggcgcagccttcacggataacgcagtcatccaggattccaatggtgcagt tcgcgccgctatcgccagcacgccgggctccatcggctatgtcgatgcaccgtatgccgatgattccgtcaagatcctgaagttc gatggcgttgagtattctccggagaacatcatcgccggcaagtatccgatctatggctatggccacatgtacacgaaaggtgag ccgactggcgcggtcaaggcattcatcgactacatcctcagcgatgagttccagaacacgcaggtcgagaagctcggcttcat ccctgtcaacaagatgaagaagtaa Amino acid sequence (SEQ ID NO:20) MKGAEGLQGSNQQVIWGGNNMFNKMKKLLSVGAVVASAAVLLAGCGGGSQQASSSSG SAAQEISGKISASGSTALLPLLKPAQEAFQDKYDKVTVNIAGGGSFTGMNQVAEGSVQIGN SDVNLPDEYKDKGLVDHKVVVEPFVFIVDKNNKVDNITKQQVIDILTGKITNWKEVGGDDQ PITLIHRAKSSGSRATISDVVLKGAAFTDNAVIQDSNGAVRAAIASTPGSIGYVDAPYADDS VKILKFDGVEYSPENIIAGKYPIYGYGHMYTKGEPTGAVKAFIDYILSDEFQNTQVEKLGFIP VNKMKK Phosphate ABC transporter PstC_MJ_0657 Nucleotide sequence (SEQ ID NO:21) atggaacgggcagcaacaatcggccgccttgacggcaagcagtcaggcggaggtcatgagcgcaggctattctacgacaa gtgcgggcggtatctcttcattgcggctgcctttctcatgaccatcatcatcttttccatcatcttcttcgtcggtcgccagggcctcatg acgttcgcagcggtcagtccgctggagttcttcttcagtgcgagctgggatccgtcgctcggcaagttcggcgcgctctcgttcat cgtgggctcgctggtgacgacactcctttcggttgccatcggcgcgccgctaggcctgctcggcgccatcttcctcgcgaaggtc gctccggcctggctcaagaacatcatgcgcccggcgacggatctctacgtcgccatcccttcggtcgtctacggctacatcggc ctgatgctgctcgtgccgtacatgcgcgatgcgttcggcacgacgacgggcttcggcgtgctcgcggcgtcgctcgtgctcgcc atcatgatcatgccgacaatcctctccatcagcacggatgcgctcaatgctgtgccgaagccgctggaggaggcgagcctcg cgctcggcgcgacgtggtggcagacgatggtccacgtcatcgtgcccgctgcagcgcctggcatcctgacggctgtcgtgctc gcgatggcgcgcgccgtcggcgagacgatggccgtgcagatgctcatcggcaacacgccgcagctcatcacctcgctgttct ctccgacggcaacgctgacgagtgacatcgtcgtcgagatgggcaatacgccgttcggctcggtctggggcaatgcgctcttc ctcatggctttcgtgctgctcatcctgtcgctggccatgattcttgtcatccgccgtttcggcacgaggagggtataa Amino acid sequence (SEQ ID NO:22) MERAATIGRLDGKQSGGGHERRLFYDKCGRYLFIAAAFLMTIIIFSIIFFVGRQGLMTFAAVS PLEFFFSASWDPSLGKFGALSFIVGSLVTTLLSVAIGAPLGLLGAIFLAKVAPAWLKNIMRPA TDLYVAIPSVVYGYIGLMLLVPYMRDAFGTTTGFGVLAASLVLAIMIMPTILSISTDALNAVPK PLEEASLALGATWWQTMVHVIVPAAAPGILTAVVLAMARAVGETMAVQMLIGNTPQLITSL FSPTATLTSDIWEMGNTPFGSVWGNALFLMAFVLLILSLAMILVIRRFGTRRV Phosphate ABC transporter PstA_MJ_0656 Nucleotide sequence (SEQ ID NO:23) atgaatgcaaaagtacagaatcaggtggcacgggcgggcctctggtgtacgggattcttcatcctcgccctgcttgcggctttcct cggctacatcctctacaagggattgccggtgctctcgccgcacttcattctcggcaaatcgagcgacatgatggctggcggcgg cgtcggttcacagcttttcaactcgttctacatgctcttcctctcgatggccatttccattccaatcgcgctcggcgcgggcatctacc tcgcggagtacgcgcgtgagaacaagctgacgaagtgcatccgcctttccgtcgagagcctcgcgacggtgccgtccatcgt actcggcctgttcggcatgatcgtcttcgtcaacatgatgaacatgggcttttccattctcggcggctcgctgacactcgtcctgctg aatctgccgatgctcgtgcgcgtgacggaggaatccatccgcaccgtgccgaggtcgtatgaagaagcgagccttgcgctcg gcgcgacgaagctccagacgatcttcaaggtcgtgctgccgagcgcgatgccgggcatcatcacgggcatcacgctgacgg cgggccgtgcactcggcgagacggccatcctgatcttcacggccggcacgacggtatcgcgtcacatgttcgacacggatgtc atggcgggcggcgagacgctggcggttcacctctggtacctcatgagcacgggcctcgtgccggaccgcgaggccatcgcc aacggcatcggcgcactgctgatcctgacgatcctcgtcttcaacttcgtcctgctgctgccgatcaagctgctggggcgcaaga caaaagcatga Amino acid sequence (SEQ ID NO:24) MNAKVQNQVARAGLWCTGFFILALLAAFLGYILYKGLPVLSPHFILGKSSDMMAGGGVGS QLFNSFYMLFLSMAISIPIALGAGIYLAEYARENKLTKCIRLSVESLATVPSIVLGLFGMIVFV NMMNMGFSILGGSLTLVLLNLPMLVRVTEESIRTVPRSYEEASLALGATKLQTIFKVVLPSA MPGIITGITLTAGRALGETAILIFTAGTTVSRHMFDTDVMAGGETLAVHLWYLMSTGLVPDR EAIANGIGALLILTILVFNFVLLLPIKLLGRKTKA Na+ / H+ antiporter NhaA type_MJ_0655 Nucleotide sequence (SEQ ID NO:25) atgaaagagacaatcaaatccatgcaggcaatcgcggagccgttcttggcattcctgcgctgggaggcgagcagcggtgtca tcctgctcgcctgcgccatcctcgcactcatcgtggcgaattcaccgctggccgaatcgtacgagcatctgctgcattatcccatc gctgtcggagcgggggagtacgtgctggagatgggcctgctgcactggatcaacgacggcctcatggcggtgttcttctttgtca tcggccttgagatcaagcgcgagttcctctacggcgagctgcgcacgtattcggcgatgctgctgcccgtcggcgcggcactcg gcggcatgctcgtgccggccgccatctatgcggcgatcaacttagggctgccgacattcggcggctggggcatcccgatggc gaccgacatcgcctttgcgctcggcatcatgaccatcgccgcgcgccaggcaccgctcggcctcgtcgtcttcctgacagcact cgccatcgtcgatgacctcggcgccatcgtcgtcatcgcgctgttctacaacacggacctcactgtatcggccttgctgctgggg ctcgtggccgtggctgccgctttcctgctcggccgtttccgcgtgcgcttcctgccggcctacatggcgctcggcttcgtcgcctgg ctggccttcctgaaggcgggcatccacccgacgattgcgggcgtgctgctcggcctctccatcccggcagcggcggatccgg agaactcgctcctgcacaagctcgagcacgcactcgagccgtggtcggcctatgccatcatgccgatcttcgccttggccaac gctggcgtcgcgatctctctggcgacgtttgacatggcctcgccgatcttcctcggcatcctcgcgggcctctgcctcggcaagcc catcggcatcttcggcgcggtattcgtgctctgcaaggtctttggcctgcagctgccgggcaatgcgacgaagagccagctcgc ggcgacgggcatgctcggcggcatcggattcacgatgtctatcttcatcgcctcgctggccttcacggacagcgcgatgctcga ccttgcgaagatcagcatcctctcggcgtcaatcctctcgggcatcctcggtacggctttcttcaagctgcagtcgctcttcggcgg gggagaaacggcgcaacagtaa Amino acid sequence (SEQ ID NO:26) MKETIKSMQAIAEPFLAFLRWEASSGVILLACAILALIVANSPLAESYEHLLHYPIAVGAGEY VLEMGLLHWINDGLMAVFFFVIGLEIKREFLYGELRTYSAMLLPVGAALGGMLVPAAIYAAI NLGLPTFGGWGIPMATDIAFALGIMTIAARQAPLGLWFLTALAIVDDLGAIVVIALFYNTDLT VSALLLGLVAVAAAFLLGRFRVRFLPAYMALGFVAWLAFLKAGIHPTIAGVLLGLSIPAAADP ENSLLHKLEHALEPWSAYAIMPIFALANAGVAISLATFDMASPIFLGILAGLCLGKPIGIFGAV FVLCKVFGLQLPGNATKSQLAATGMLGGIGFTMSIFIASLAFTDSAMLDLAKISILSASILSGI LGTAFFKLQSLFGGGETAQQ Phosphoglycerate mutase_MJ_1633 Nucleotide sequence (SEQ ID NO:27) atgacaaagatcatttttgtgcgccatggccagaccgagtggaatgtgctcggccgctaccagggccagacggacatcgcact ctcgccgctcggcatcgagcaggctgagaagcttgcggcacatttccccgtggacaaggtggaggctgtctactcgagcgac ctcgtgcgcgccatgatgacggcctgctgcgtcgccgaccgcttcggcctgacagtcgaggcgcgccccgagttgcgcgagc tcaacttcggcgactgggagggcctgacgtacgacgaaatcgtcgccaagtggcccgatgccctcaataatttcttccagcatc ccgacgtcctcgagatcccgcacggtgagagcttcccgaagctgcgcgagcgtgcgctcgatgccgtcgagaagatcgtgg cctgccaccctgagcagaccgttgccgtctttgcgcacggcgccattctgcgcaccatcctgacggccgccctgcacatggac ctcaagtacgtctggaccatccgccagttcaacacggccgtcaacatcgtgacgtacaccgagcacggcacgacagtcgaa ctgctcaatggcacaggacatctgaagtatgcacaggggactgtggattaa Amino acid sequence (SEQ ID NO:28) MTKIIFVRHGQTEWNVLGRYQGQTDIALSPLGIEQAEKLAAHFPVDKVEAVYSSDLVRAMM TACCVADRFGLTVEARPELRELNFGDWEGLTYDEIVAKWPDALNNFFQHPDVLEIPHGES FPKLRERALDAVEKIVACH PEQTVAVFAHGAILRTILTAALHM DLKYVWTIRQFNTAVNIVTY TEHGTTVELLNGTGH LKYAQGTVD Triosephosphate isomerase_MJ_0883 Nucleotide sequence (SEQ ID NO:29) atggcaagaactccaatcattgcaggcaactggaagatgaacaacacgatcgtcgagggcaagaacctcgtccgcggcct ggctccgctcgtcaaggatgccaaggtgacggtcgtcgtctgcccgacggctacggctctcgcagctgtcgcagatgcagcac tcggcacgaacatccacgtcggcgcacagaacgttcattgggaagatcacggcgcgttcacgggcgagatctccacgggca tgctcaatgagatcggcgtagattactgcgtcctcggccacagcgagcgccgcggttacttcggcgagacggatgagggcgtc aacaagcgcgctcatgctgctttcgctgcaggcatcacgccgatcatctgctgcggtgagtccctcgagcagcgcgaagctgg tgtatacctcgacttcgtcgctggtcaggtcaaggctgccctcgctggcttccagccggaagaagtagcaaagatcgtcatcgct tacgagccgatctgggctatcggcacgggcaagacggcttccttcgagcaggctgaggaagtctgcgcgcacatccgcaag acggttgccgcagaattcggccaggaagcagctgacggcatccgcatccagtacggcggcagcgtcaagccggctacgat caaagacctcatgaagcagccgaatgtcgatggcgccctcgtcggcggtgcatcgctcaaggctaaggacttcagcgagatc gtaaacttctga Amino acid sequence (SEQ ID NQ:30) MARTPIIAGNWKMNNTIVEGKNLVRGLAPLVKDAKVTVWCPTATALAAVADAALGTNIHV GAQNVHWEDHGAFTGEISTGMLNEIGVDYCVLGHSERRGYFGETDEGVNKRAHAAFAAG ITPIICCGESLEQREAGVYLDFVAGQVKAALAGFQPEEVAKIVIAYEPIWAIGTGKTASFEQA EEVCAHIRKTVAAEFGQEAADGIRIQYGGSVKPATIKDLMKQPNVDGALVGGASLKAKDFS EIVNF Enolase_M J_1725 Nucleotide sequence (SEQ ID N0:31) atgaaagcatacttacagatcatgcaggtcatcggccgtgaaatcatcgattcgcgcggcaatccgacggtcgaggcggaag tcacgctcgaggacggctccgtcggccgcgcatctgctccgtcgggcgcttcgacgggcgagttcgaggcgctcgagctccg cgacggcgacaaggcgaagttcggcggcaagggcgtctcgaaagctgtcgcgaacatcaatgagaagatcgccccggctc tcatcggtgcggatgcgtcggacatctatgcagtcgatgccatcatgctcaaactcgacggcacggaagacaagtcgaacctc ggcgcgaacgccatcctcgccgtctcgctcgcagcggcaaaggccgcggccgtatcgctcgacctcccgctctaccgcttcct cggcggcatcagcggcaatcacctgccggtgccgatgatgaacatcttgaacggcggcgcgcatgcgacgaactcggtcga cacgcaggagttcatgatcatgccggccggcgcaccgtccttccgcgagggactgcgctgggcgacggaggtcttccatgcg ctgcaggcgctgctcaagaaggaagggcagacgacggctgtcggcgatgagggcggctttgctccgaacctcaagagcga cgaggacacgatcgagcacatcctgacggccatccgcaatgcgggttacgagccgggccgcgacttcgtgctggcgatgga tgcggcttcgtcggagtggaagagcgagaagggcaagggcttctacaagcagccgaagtcgggcaaggagttcacgtcgg atgagctcatcgcgcactggaagagcctcatcgagaagtacccgatctactccattgaggacggcctcgatgaggaggactg ggaaggctggcagaagatgacgaaggagctcggcgacaaggtacagctcgtcggcgatgacctctttgtcacgaacacga agcgcctgaagaagggcatcgagctcggctgcggcaacagcatcctcatcaagctcaaccagatcggcacgctgtcggag acgctggaggccatcaagatggcacatgaggcgggctacacggccatcgtctcgcaccgttcgggcgagacggaggacac gacgatcgcggacctcgctgtcgcgctcaacacgaaccagatcaagacgggcgccccgtcccgctcggagcgcgtcgcca agtacaaccagctgctgcgcatcgaggaagagctcggcgcaagcgcggtctatccgggcaaagcagcttttagattccaga agtaa Amino acid sequence (SEQ ID NO:32) MKAYLQIMQVIGREIIDSRGNPTVEAEVTLEDGSVGRASAPSGASTGEFEALELRDGDKAK FGGKGVSKAVANINEKIAPALIGADASDIYAVDAIMLKLDGTEDKSNLGANAILAVSLAAAKA AAVSLDLPLYRFLGGISGNHLPVPMMNILNGGAHATNSVDTQEFMIMPAGAPSFREGLRW ATEVFHALQALLKKEGQTTAVGDEGGFAPNLKSDEDTIEHILTAIRNAGYEPGRDFVLAMD AASSEWKSEKGKGFYKQPKSGKEFTSDELIAHWKSLIEKYPIYSIEDGLDEEDWEGWQKM TKELGDKVQLVGDDLFVTNTKRLKKGIELGCGNSILIKLNQIGTLSETLEAIKMAHEAGYTAI VSHRSGETEDTTIADLAVALNTNQIKTGAPSRSERVAKYNQLLRIEEELGASAVYPGKAAF RFQK Phosphoglycerate kinase_MJ_0882 Nucleotide sequence (SEQ ID NO:33) atgaacaagaaaaccatcaaagacgttgacgtaaacggcaagaaagtattcgtccgcgtcgactacaatgtcccgttcgacg acaagatgaacatcacgaacgacacgcgcatggtccgcacgctgccgaccctgaactacctgctcgaccacggtgcagctc tcgtcatcgcctgccacatcggccgtccgaccgaggcgcgcgaggacaagttctccacaaagtacctcgtcaagcacctctcc gagctgctcggccgcgatgtcaagtgggcctccgactgcgtcggcgctgaggcagatgccgcaaaggctgcgctgaagccg ggcgaagtcctgctgcttgagaacctccgttaccacaaggaagagaagaagaacgatcccgagttcgcgaagcagctcgct tccggttgcgatctcgcagtcgacgatgctttcggtgtttcccaccgcgctcatgcttcgaacgcaggcgttccgaagtacatcga gacggttgctggcttcctgatggaaaaggaaatcaactacatcggcaagacgctcgagaacccgcagcatccgttcgtcgcc attatcggcggtgcaaaggtctccgataagatcggcgtcatcagcaacatgatcgacaaggttgacacgatcatcatcggcgg cggcatggctcatacgtttgatgcagccaagggcctgccgattggcgattccctctgcgagccggacaagtacgatctcgctcg tgagctgctcaagaaagcagaagacaagggcgtcaaggtcgtcctgccggtcgacctcgtcattgccgacaagttcgctgcc gatgccaacacgaagacggttgacgtcgacaaagtaccggatggctggcaggcactcgattccggcgagaagacgtcgga agagtacacgaaggctcttgaaggcgctaagacggtcatctggaacggaccgatgggcgtattcgagtttgatgcttttgcaaa aggcacgctcgctgttgctaaggctgtcgccaaggctacggaaaatggcgctatctccatcgtcggcggcggcgactccgttg cagccctcaagaagacgggcctgacggacaagatctcgcacgtctccacgggcggcggcgctacgctcgagttcctcgaag gcaaagagatgccgggcatcgcagcactggctgacaaataa Amino acid sequence (SEQ ID NO:34) MNKKTIKDVDVNGKKVFVRVDYNVPFDDKMNITNDTRMVRTLPTLNYLLDHGAALVIACHI GRPTEAREDKFSTKYLVKHLSELLGRDVKWASDCVGAEADAAKAALKPGEVLLLENLRYH KEEKKNDPEFAKQLASGCDLAVDDAFGVSHRAHASNAGVPKYIETVAGFLMEKEINYIGKT LENPQHPFVAIIGGAKVSDKIGVISNMIDKVDTIIIGGGMAHTFDAAKGLPIGDSLCEPDKYD LARELLKKAEDKGVKVVLPVDLVIADKFAADANTKTVDVDKVPDGWQALDSGEKTSEEYT KALEGAKTVIWNGPMGVFEFDAFAKGTLAVAKAVAKATENGAISIVGGGDSVAALKKTGLT DKISHVSTGGGATLEFLEGKEMPGIAALADK Pyruvate kinase_MJ_0374 Nucleotide sequence (SEQ ID NO:35) atgttaaagaagacgaaaattatctgcacgcagggtcctgctacggagagaccgggcgtagtcgatgcactgattgcaaacg gcatgaactgtgcacgctttaacttctcccatggtgaccacgcagagcacctcaaccgcatcaacatggtgcgcgaggctgcc aagaaggccggcaaggtcatttccctgattctcgatacgaagggaccggagatgcgcctcggcgagttcaaggacggcaag gtcatgctcgagaagggcaatcagttcacgctgacgtatgaggacatcccgggcgatgagacgcatgtctccgtcaaccaca agggcctctacacggaagtcaagccgggtgacacgctgctcctctctgatggcctcgtagcactcaaggtcgatgagatccgc ggcaaggacatcatcacgacgatccagaacagcggcaagatgagcacgaagaagcgcgtcgctgctccgggcgtatccct cggcctgccgccgatctcggagcaggatgcgaaggacatcatcttcggctgcgagcaggacctcgatttcgtcgctgcttccttt atccagcgtccggaggacgtcctggccatccgcaagctcatcgaggagcacaatggccacatggagatcatgccgaagatc gagaacctcgaaggcgtcaagaacttcgatgcgattctcgaagtctccgacggcatcatggtcgctcgcggtgacctcggcgtt gaggttccggccgaggacgttccgctgatccagaaagagatcatccgcaagtgcaacaaggctggcaagccggtcatcgtc gctacgcagatgctcgactccatggagcgcaacccgcgcccgacgcgcgctgaggtctccgatgtcggcaacgccatcctc gatggtacggatgccatcatgctctccggcgagacggcttccggcgattacccggtcgaggctgtttccacgatgaaccgcatc gcttgccgcatcgaggagtccctcgagtacaagaatctcttcgttgagcgcggcttcgagcacagccagagccgcacgcgcg ccgtcgcacatgctacggtacagatggcttacgagctcgatgtcccggctatcatcacgccgaccgacagcggctacacgac gaagatcgtatcccgttaccgtccgaaagcagctatcgttgcctacacgccgcatgagaaggtcgtccgccagctcaacctcc gttggggcgtatacccgatcctcggcacgcagtggaaggacgtcgacgagatgattgcgaacgctgtttccgcagctgtcaag gacggcttcgtgaagcgcggcgacacgacgatcatcacgtccggcatcaagctccagagcaagacgagcgtcggcaaca acacgaacatgatccgcgtctacaagatctga Amino acid sequence (SEQ ID NO:36) MLKKTKIICTQGPATERPGWDALIANGMNCARFNFSHGDHAEHLNRINMVREAAKKAGK VISLILDTKGPEMRLGEFKDGKVMLEKGNQFTLTYEDIPGDETHVSVNHKGLYTEVKPGDT LLLSDGLVALKVDEIRGKDIITTIQNSGKMSTKKRVAAPGVSLGLPPISEQDAKDIIFGCEQD LDFVAASFIQRPEDVLAIRKLIEEHNGHMEIMPKIENLEGVKNFDAILEVSDGIMVARGDLGV EVPAEDVPLIQKEIIRKCNKAGKPVIVATQMLDSMERNPRPTRAEVSDVGNAILDGTDAIML SGETASGDYPVEAVSTMNRIACRIEESLEYKNLFVERGFEHSQSRTRAVAHATVQMAYEL DVPAIITPTDSGYTTKIVSRYRPKAAIVAYTPHEKVVRQLNLRWGVYPILGTQWKDVDEMIA NAVSAAVKDGFVKRGDTTIITSGIKLQSKTSVGNNTNMIRVYKI NAD-dependent glyceraldehyde-3-phosphate dehydrogenase_MJ_0881 Nucleotide sequence (SEQ ID NO:37) atggcagtaaaagttgctatcaatggttttggccgtatcggtcgtctcgcattccgtcagatgttcgatgctgagggttatgaagtcg ttgcaatcaacgatctcacgagcccgaaaatgctcgcttacctgctgaagtacgattcttcccagggcaagtacgagtatgctga cacggttgaggctggcgaagacagcatcacggtcaagggcaagacgattaaaatctatgccgagaaagatgcaaagaac atcccctgggcgaagcatgatgtagatgtcgttctcgagtgcacgggcttctacacgtccaaggaaaaggcttccgcacatctc gaagctggcgctaagaaagtcgtcatctccgctccggcaggcaaggacctcccgacgatcgtgttcaacacgaaccacaag tccatcccggcaggcacgaaaatcatctccgctgcatcctgcacgacgaactgcctcgcaccgatggcaaaggccctcaatg accttgctccgattcagagcggcatcatgcagacgatccacgctttcacgggcgaccagatgacgctcgatggcccgcagcg caagggtaacctccgccgcagccgtgctgcttccgagaacatcgttccgacgtcctccggcgcagctaaagctatcggcctcg ttcttccggaactcgatggcaagctcatcggtgctgcacagcgcgttccgaccccgacgggttccacgacgctcctctacgctgt tgtcaagggcaacgttacggttgacgaagtcaatgcacagatgaagaaggagtccacggagtccttcggctacaacacggat gacattgtatccaaggatgttgtcggtatgcgttatggctccctgttcgatgctacgcagacgatggtcagcccgatggctgatgg caacacgctcgttcaggttgtatcctggtacgacaacgagaactcctacacgagccagatggttcgcacgatcaagtacttcgc tgaggaagtcaagtaa Amino acid sequence (SEQ ID NO:38) MAVKVAINGFGRIGRLAFRQMFDAEGYEVVAINDLTSPKMLAYLLKYDSSQGKYEYADTVE AGEDSITVKGKTIKIYAEKDAKNIPWAKHDVDWLECTGFYTSKEKASAHLEAGAKKWISA PAGKDLPTIVFNTNHKSIPAGTKIISAASCTTNCLAPMAKALNDLAPIQSGIMQTIHAFTGDQ MTLDGPQRKGNLRRSRAASENIVPTSSGAAKAIGLVLPELDGKLIGAAQRVPTPTGSTTLL YAVVKGNVTVDEVNAQMKKESTESFGYNTDDIVSKDVVGMRYGSLFDATQTMVSPMADG NTLVQWSWYDNENSYTSQMVRTIKYFAEEVK D-lactate dehydrogenase_MJ_0056 Nucleotide sequence (SEQ ID NO:39) atgaaaaaattccaagtcgtcgtgaagtgctcactcggtatccatgcgcgtcccgcagctcagatcgcgcaggcatgcagcaa cctgcgggcggcggtgacgctcgaggtcgataatgagactgcccagggcaacaacgtgctggagatcttgaacctccacgct ccgaaaggcgcaacggtcaatgtcaccgtggacggccctgatgaggaagaggctgcacagcagatccaggctgttttcgat gccatgggcccgaaggagaagaagggctctgtcctcaaggtcgcctttttcggcacgaaagactatgaccgcctctatttcagc gagctcgcaaaggacaagggcgagggcacgtacaacgtcgaactcaagtatttctcgagccgcctgacggatgagacggc acatctcgccaacggctatgacgctgtctgcatcttcgtcaacgacgaggcaccgcgttctgtcatcgagcagctgcatgacgg cggcgtccgcctgatcctcctgcgctgcgccggcttcaacaatgtcgacaagaaggccgctgccgagtacggcatcacggtc ctgcgcgtaccggcttactccccgtacgcagtggcagagcatgccatggcgacgctgcaggctgcaaaccgccgcctgcac aaggcatacaacaaggtgcgcgacaacaacttcgacctcacgggcctgctcggcgtcgatctccacaacaaggtcgccggc atcctcggcacgggccgcatcggccagtgcatggcgcgcatctgcaagggctacggcatgacggtcatcggctgggatgcgt tcccgaacaagaagctcgaggaagaggggctgctcacctatgcttcgaaggaagaggtcctgaagcgctctgacctcatctc cattcacgcaccgctcatcatgggcgaaggcggcacgtatcatctcattgatgagaaggccatctccctcatgaaggacgatgt catgctcacgaatgctgcacgcggcggcctcatcgatacggaagcgctcattgccgcgctcaagaagggcaagttccatgcg gttgcgctcgacgtctacgagggcgaggatgccaatgtctacacggaccacagcttcgacgtcccgacggaggatgtcacgg gccgtctgctcatgttcccgcaggtcatcctcacgagccatcaggcattctttacgcgcgaggcactgcaggccatcgcgacgg tgacgatggagaacgcccgcaatttcaacgagggccgtccgttcggtgctgctgaggtgaaataa Amino acid sequence (SEQ ID NO:40) MKKFQVWKCSLGIHARPAAQIAQACSNLRAAVTLEVDNETAQGNNVLEILNLHAPKGATV NVTVDGPDEEEAAQQIQAVFDAMGPKEKKGSVLKVAFFGTKDYDRLYFSELAKDKGEGT YNVELKYFSSRLTDETAHLANGYDAVCIFVNDEAPRSVIEQLHDGGVRLILLRCAGFNNVD KKAAAEYGITVLRVPAYSPYAVAEHAMATLQAANRRLHKAYNKVRDNNFDLTGLLGVDLH NKVAGILGTGRIGQCMARICKGYGMTVIGWDAFPNKKLEEEGLLTYASKEEVLKRSDLISIH APLIMGEGGTYHLIDEKAISLMKDDVMLTNAARGGLIDTEALIAALKKGKFHAVALDVYEGE DANVYTDHSFDVPTEDVTGRLLMFPQVILTSHQAFFTREALQAIATVTMENARNFNEGRPF GAAEVK Pyruvate-flavodoxin oxidoreductase _MJ_0614 Nucleotide sequence (SEQ ID N0:41) atgagcaaaaagatgaaaaccatggacggcaacacagctgccgcctacatctcctatgctttcaccgacgtcgcggcgatct acccgattacgccgtcctcgccgatggctgagcatgtagatgaaatggctgccaagggagcgaagaatctcttcggccagaa ggtcaaggtcatcgagctgcagtctgaggccggcgctgccggcgctgtgcacggctcgctgcaggccggtgcactgacgac gacgtacacggcttcccagggcttcttgctgatgatcccgaatctctacaaggtagccggcgagctgttgccgggcgtcttccac gtctccgcgcgcgcactcgctgccaactccctgaacatcttcggcgaccaccaggatgtcatggccgcacgccagacgggtt gcgccatgctcgccgaggcgagcgtccaggaggtcatggacctctcggccgtcgcacacctcgtcgccatcaagggccgcg tgccgttcatcaacttcttcgacggcttccgcacgtcgcacgagatccagaagatcgagacgattgactacgaagacctcgca aagctgctcgactgggatgccgtcaaggccttccgccgccgcgctctgaacccggaccacccggtcctgcgcggctccgcga cgaacccggacatctacttccagtcgcgtgaagcagccaacagcttctacgatgcgctgccagagctcgtcgaggaggccat ggctgacctcgcgaaggtcacgggccgcgagcaccatctctttgactactatggcgccaaggatgccgaccgcatcatcatcg cgatgggctccgtctgccagacggtccaggagacggtcgactacctcaacgcgaagggggagaaggtcggcctgctgaac gtacacctctaccgtccgttctccatcgagcacttcttcaagttcctgccgaagaccatcgagaaagtcgccgtcctcgaccaca cgaaggagccgggttcgctcggcgagccgctctacctcgatgtcaaggcagccttctatcattccgacatgcacccgacgatc atcggcggccgcttcggcctcggcggcaaggacacgacgccggaccagatcttcgccgtctttgaagagctcaagaaagac gcgccgaaggacggtttcacgatcggcatcgacgacgatgtcacgcacacgagcctgacgccggcgctgacggatgtcga cctcacgccggaaggcacgacggcctgcaagttctggggcctcggctcggatggcacggtcggcgccaacaagagcgcca tcaagatcatcggcgacaagacggacatgtacgcccaggcgtacttcgcctatgactccaagaagtcgggcggcatcacgat gtcgcacctgcgcttcggcaagtccccgatcacgagcccgtacctcatcaacaaggccgacttcatctcctgctcgcagcagtc gtacgtctacaagtacgacctgctcgccggcctcaagaagggcggcacgttcctcctcaacacggtctggagcgacgagaa gctcacgaagcacctgccggcagccatgaagcgctacatcgccaagaacgagatccagttctacacggtcaacgctgtctcc atcgccaagggcctcggcctcggcggccgcttcaacatggtcatgcagtccgcgttcttcaagctcgcgaacatcatcccgatc gagacggccgtgacctacctcaaggaagccgtcgtcacctcgtacggccgcaaaggccagaacatcgtcgacatgaacaa cggcgccatcgaccagggcatcgaggccctgcacaaggtcgaggtgccggcatcgtgggctgatgctgaagacgagccgc aggagaagcgcgacctgccggagttcatcaccgaggtccaggaagtcatgaaccgccaggaaggcgacaagctgccggt ctcgaagttcgccggcgaccgcgccgacggcacgtacccgctcggcggcgccgcctacgagaagcgcggcacggccatc aacgtgccggtctggaacgcccagaagtgcatcggctgcaacaagtgctcctatgtctgcccgcacgcttcgatccgtccggtc ctcacgaccgacgaagagctcgctgcagcaccggagggcttcccgtccaaggaagtccgcgccgtcaaggactaccacttc acggtggctgtctccacgatggactgcctcggctgcggcaactgcgcgcaggtctgcccggtcaaggcgctcgacatgacgc cgcttgacgacgacctcaaggcaaagcaggcttacttcgactacggcgtcgacacggagaaagtcgcgccgaagaagaac ccgatgaagaaagagaccgtcatcggcagccagttcgagcagccgctcatcgagttctccggcgcctgcgccggctgcggc gagacgccgtacgccaagctcatcacgcagctcttcggcgaccgcatgatgattgccaacgccacgggctgcacctccatct ggggcggcagcgcaccggccatgccgtacacgacgaacgccaagggccacggcccggcttgggacaactccctgttcga ggacaacgcagagttcggcctcggcatgttcctcggcacgcagtccgtccgcaatggcctcgccgatgacgccaagaaggc catcgaagaaggtcttggcagcgaagacctccaggcagccctcaaggactgggtagagaacctcgacaacggcaacggc acgcgcgaccgcgccgaccgcctcgaagccctgctcgcagccgagaagggtgacaatgcgctgctcaacaagctctacga gaaccgcgactacttcgtcaagcgctcccagtggatcttcggcggcgacggctgggcctacgacatcggctacggcggcgtc gaccacgtcctcgcctccggcgcagacgtcaacgtcttcgtcttcgacaccgaagtctactccaacaccggcggccaggcctc caaggccacgccggcagcagcaatcgcacagttcgccgcaaccggtaagaagacccgcaagaaggatctcggcctcatg gccaagacctacggctacgtctacgtcgcccaggtcgccatgggcgcagaccagaaccagctgctcaaggccatcaccga ggccgaggcttatccgggcccgtccctcatcatcgcctacgcaccgtgcatcaaccacggcatccgcaagggcatgggctgc agccagctcgaggagaaactcgccgtagagtgcggctactgggcaaactaccgctacaacccgcagctcgtcggcaccga caagaacccgttcagcctcgactccaaagagccggacttctccaagttccaggacttcctcatgggcgagaaccgctacatca acctcaagcgcaccttcccagaagcagccgaagccctctttgagaagacccagcgcgacgccgagatccgctacaacaac tacaagaccctcgccggcaaataa Amino acid sequence (SEQ ID NO:42) MSKKMKTMDGNTAAAYISYAFTDVAAIYPITPSSPMAEHVDEMAAKGAKNLFGQKVKVIEL QSEAGAAGAVHGSLQAGALTTTYTASQGFLLMIPNLYKVAGELLPGVFHVSARALAANSL NIFGDHQDVMAARQTGCAMLAEASVQEVMDLSAVAHLVAIKGRVPFINFFDGFRTSHEIQ KIETIDYEDLAKLLDWDAVKAFRRRALNPDHPVLRGSATNPDIYFQSREAANSFYDALPEL VEEAMADLAKVTGREHHLFDYYGAKDADRIIIAMGSVCQTVQETVDYLNAKGEKVGLLNV HLYRPFSIEHFFKFLPKTIEKVAVLDHTKEPGSLGEPLYLDVKAAFYHSDMHPTIIGGRFGL GGKDTTPDQIFAVFEELKKDAPKDGFTIGIDDDVTHTSLTPALTDVDLTPEGTTACKFWGL GSDGTVGANKSAIKIIGDKTDMYAQAYFAYDSKKSGGITMSHLRFGKSPITSPYLINKADFIS CSQQSYVYKYDLLAGLKKGGTFLLNTVWSDEKLTKHLPAAMKRYIAKNEIQFYTVNAVSIA KGLGLGGRFNMVMQSAFFKLANIIPIETAVTYLKEAVVTSYGRKGQNIVDMNNGAIDQGIEA LHKVEVPASWADAEDEPQEKRDLPEFITEVQEVMNRQEGDKLPVSKFAGDRADGTYPLG GAAYEKRGTAINVPVWNAQKCIGCNKCSYVCPHASIRPVLTTDEELAAAPEGFPSKEVRA VKDYHFTVAVSTMDCLGCGNCAQVCPVKALDMTPLDDDLKAKQAYFDYGVDTEKVAPKK NPMKKETVIGSQFEQPLIEFSGACAGCGETPYAKLITQLFGDRMMIANATGCTSIWGGSAP AMPYTTNAKGHGPAWDNSLFEDNAEFGLGMFLGTQSVRNGLADDAKKAIEEGLGSEDLQ AALKDWVENLDNGNGTRDRADRLEALLAAEKGDNALLNKLYENRDYFVKRSQWIFGGDG WAYDIGYGGVDHVLASGADVNVFVFDTEVYSNTGGQASKATPAAAIAQFAATGKKTRKKD LGLMAKTYGYVYVAQVAMGADQNQLLKAITEAEAYPGPSLIIAYAPCINHGIRKGMGCSQL EEKLAVECGYWANYRYNPQLVGTDKNPFSLDSKEPDFSKFQDFLMGENRYINLKRTFPEA AEALFEKTQRDAEIRYNNYKTLAGK Acetyl-CoA hydrolase_MJ_0049 Nucleotide sequence (SEQ ID NO:43) atggtagatatcctcgatcgtgtgcgcaacaaggcgctgcagtccaagatcgtgacaccggaggaagcggcagacttcatca agccgggcatgacccttgcgacgagcggcttcacatcctcggcctacccgaaggcggtgccgctcgctctcgcggaccgcat gaagaaggacccgttcacggtcaacatcatgacgggcgcttcgacgggcccggagttcgatgaagcgctcgcctcggtcca cggcatcaagaaacgcctgccgttccagacggacaaggtgctgcgcagccagatcaacgacggcacggtcgattacatcg acatacatctgtcggaggtcgcgcagctctcgcgctgcggctacctcggccatctcgacgtcgccgtcatcgaggcctgcgcc atcacggaggagggcaacatcatcccgacgacggccgtcggcaactcggcctcgttcgtgcagacggccgacaccgtcatc atcgaggtcaacaacgcgcagccgctggagttcgagggcatgcacgatgtctacctgccgctcgacccgccgaaccgtctgc ccatcccgatcgtgcgcgtcgacgaccgcatcggcacgccgtacatcccgtgcccgcaggacaagatccgctacatcgtgcc gtgcgacatcgcggaccacacgcgctcgctcgcgccgctcgacgcgacggcgcagcagatggctgacctgacgattgactt cctcaagcgcgagataaaggctggccgcatgccgaagaacctgctgccgatacagtcgggcgtcggcaatgtcgccaatgc cgtcacggcgggctttgtccgctcggacttccgcgacctcacggtctacacggaggtcatccaggacggcatgctcgacctcat cgatgcgggcaagctcaacttcgcctcgggcacggccttctcgccgtctcctgagggcatggcgcgcttcttcaaggacattga gaagtacaagaagtacatgatcctgcgcccgcaggagatctcgaacagcgcggaggtcatccgccgcctcggcgtcattgc gatgaacacggccgtcgaagtcgacatctacggcaacgtcaactcgacgcacatcgcgggcacgcacatgatcaacggca tcggcggcagcggcgacttcgcgcgcaacgcctacctgaccatcttctacacgccgtcggtggccaagggcggcaagatctc ggccgtcgtgccattctgctcgcatgttgaccagccggagcacgacgtcgacgtcatcatcacggagcagggcgtggccgac ctgcgcggcaagtcgccgcgccagcgcgccaaggagatcatcgagaactgcgcgcaccccgacttccgcccaatgctgcg cgactatttccagcgcgccgacgcgaagacgaaccacgcgcacacgccgcacctcctcgatgaggccttctcgttccaccag cgctatctggagacaggcagcatgaagcgcgagagtcaggaagatacaggaaaggtgtga Amino acid sequence (SEQ ID NO:44) MVDILDRVRNKALQSKIVTPEEAADFIKPGMTLATSGFTSSAYPKAVPLALADRMKKDPFT VNIMTGASTGPEFDEALASVHGIKKRLPFQTDKVLRSQINDGTVDYIDIHLSEVAQLSRCGY LGHLDVAVIEACAITEEGNIIPTTAVGNSASFVQTADTVIIEVNNAQPLEFEGMHDVYLPLDP PNRLPIPIVRVDDRIGTPYIPCPQDKIRYIVPCDIADHTRSLAPLDATAQQMADLTIDFLKREI KAGRMPKNLLPIQSGVGNVANAVTAGFVRSDFRDLTVYTEVIQDGMLDLIDAGKLNFASGT AFSPSPEGMARFFKDIEKYKKYMILRPQEISNSAEVIRRLGVIAMNTAVEVDIYGNVNSTHIA GTHMINGIGGSGDFARNAYLTIFYTPSVAKGGKISAWPFCSHVDQPEHDVDVIITEQGVAD LRGKSPRQRAKEIIENCAHPDFRPMLRDYFQRADAKTNHAHTPHLLDEAFSFHQRYLETG SMKRESQEDTGKV Pyruvate carboxylase_MJ_0277 Nucleotide sequence (SEQ ID NO:47) atgaagaacattcgcaagatcttggtgccgaaccgcggcgagattgccatccgcattttccgcgcctgccacgagatgggcat ccgcacggtcgcggtctactcgaaagaagatgtcctgtcgctgcatcgcagccgcgccgatgaagcgtatctcgtcggcaag ggcaagaagccagtcgatgcctacctcgacatcgaggacatcatccgtatctgcaaagagcacgatgtcgatgccatccatc cgggctacggcttcctctccgagaacgcacagctggccaagcgctgcgaggatgagggcatcatcttcatcggcccgaaagt tgagcacctgcagatgttcggcgacaaggtcaacgcgcgcatccaggcagagcgcgccgacatcccgatgatcccgggca cgaacggtgccgtcaaggatttcgctgaggtcaaggccttcgctgagcgcgtcggcctgccgatcatgatcaaggccatcaac ggcggcggcgggcgcggcatgcgccgcgtcgaccgcatggaagacctcaaagaggcgtacgatgaggcgcgctcggag gccaagcgtgccttcggcgatgaggatgtctacgtcgagaagtgcatcctaaacccgaagcacatcgaagtgcagatcatgg gcgatgaacacggcaatgtcatccacctcaatgagcgcgactgctccatccagcgccgccaccagaaagtcatcgagatgg caccggcatggtcgctgccgaagaagctgcgccagaatatctgcgctgctgcgctgaagatcatgaagaatgtccactacgtc aacgccggcacagtcgaattcctcgccgaccaggatgaggagcacttctacttcatcgaagtcaacccgcgcgtccaggtcg agcacacggtcaccgaggccatcacggacatcgacatcgtcaagacgcagatcctcgtcgccgagggccatgcgctctccg acccagagatcggcatcaagagccaagaagacatcccctgcaacggcgtggccatccagtgccgcatcacgacggagga cccgcagaacaacttcatgccggacaccggcaagatcaacgactaccgcagcggcggcggccctggcatccgcctcgatg ccggcacggcctacacgggcgccgtcatcacgccgtactacgactccctgctcgtcaaggtcacggcgcatgccaacaacg ccccggagacaatctaccgcatgctgcgctgcctcgatgaattccgcatcggcggcgtcaagacgaacatctacttcctcaag aacatgctgctcgacaagaacttccaggctggcagctgcaacgtcaactacatcgaccaccatccggacctgctcaacgccc cgcaggtcatcgatgagccggcagccggcctgctcgcctacatcggtgaggtcacggtcaacggcttccacggcaacggctc aaacccgaagccgcgcttcgagacgccggtgaagctcaatgccgccgacgaagcctgcccgtccggcacgcgccagctcc tagaggagctcggccccgagaagttctccaagtggatccaggaccagaagcaggtcctgctgatggacacgacgtaccgcg atgcccatcagtccctgctcgccacgcgcatccgcacgcgcgacatcatgcaggccatccactacacggcctgcaaggtccc gcagatctacgcctttgaggactggggcggcgcgacgttcgatgtcgcctaccgtttcctcgacgaggacccgtgggagcgcc tgcgcaagatgcgcgaggctgcgccgaacatcctgttccagatgttgacgcgcggcgccaacaccgtcggctacacgaact atccgcctgaagtcgtgcgccagttcctcgccctcgcggccaagaacggcgtcgatgtcttccgcatcttcgactgcctgaacc agctcgaccacatgacgctgtcgattgacgaagtccgcaagcagggcaagctcgcggagacggccttctgctacacgggcg atatccttgacgacggccgccagaagtacacgctgaagtactacacgaatctcgccaaggagatggaaaaggccggtgcc aacatcatcgccatcaaggatatggccggcctcctgaagccagaagcggcctacaccctgatctcggccctcaaggatgctgt cgacctgccgattcacctgcacagccacgagggtggcggctgcacgctctacacctacgccaaggcggcagaggccggcg tcgacatcgtcgatgtcgccacgagcgccctctccaacggcacgagccagccgtccatgacggccttcatccaggcgctctcc aacaacccgcgccagccgcagatggacatcgaggaactcgagacgattgaccgctactggcaggtcgtccgcgcctactac gcgggtgtcgacggcaagatgacgagcccgaacacgacggtcttccagcacgagatgcctggcggccagtacacgaacct gcgccagcaggcgaagggcgtcggcctcggcgacagatggccggaagtctgccgcatgtacgccaaggtcaacgagatgt tcggcgatgtcatcaaggtcacgccgtcctcgaaagtcgtcggcgacatgacgctcttcatggtccagaacaacctgaccgag aaagatatctacgagcgcggcgagacgatggacttcccgaaatccgtcgtcgacttcttcgacggcaagctcggcgtccccta cggcggcttccccgagaagctccagaagatcatcctcaggggcgagcagccgcacctcgagacgccgcccgccccgatcg accaggagaaggtcacgcaggacatgaaggccctgcgcatgccggagacggaagaggcgcgctcgagctactgcatcta cccgaaggtctacaaggactacatccagcgctaccatcagtacggcgacctttccatcctcgacacgccgacgtacttcttcgg catgaagccgggcgaggagagctggctgcgcatcggcggcaagatggtcctcatccgcatgaactacatcacgccgccgtc ggatgatggcttccgcgagatccagttcgaggtcaacggcatgccgcgcgagatccgcgtgcgcgataaggcggcttcgga aggcgcggcgatcatccgccaggccgacccgactgtcccgggcgaagtagccgctacgctctctggctctgtcctgcgcctca tcgcagccaagggcgatgtcgtcaagaaaggcgacccgctgatggtcacggaggccatgaagatggagacgacgatcac cgcgccgattgccggcatcgtcaaggaggtctgtgtcgcagcaggcagccgcatcacttccggcgacctcctcgctgtcatcg aataa Amino acid sequence (SEQ ID NO:48) MKNIRKILVPNRGEIAIRIFRACHEMGIRTVAVYSKEDVLSLHRSRADEAYLVGKGKKPVDA YLDIEDIIRICKEHDVDAIHPGYGFLSENAQLAKRCEDEGIIFIGPKVEHLQMFGDKVNARIQ AERADIPMIPGTNGAVKDFAEVKAFAERVGLPIMIKAINGGGGRGMRRVDRMEDLKEAYD EARSEAKRAFGDEDVYVEKCILNPKHIEVQIMGDEHGNVIHLNERDCSIQRRHQKVIEMAP AWSLPKKLRQNICAAALKIMKNVHYVNAGTVEFLADQDEEHFYFIEVNPRVQVEHTVTEAI TDIDIVKTQILVAEGHALSDPEIGIKSQEDIPCNGVAIQCRITTEDPQNNFMPDTGKINDYRS GGGPGIRLDAGTAYTGAVITPYYDSLLVKVTAHANNAPETIYRMLRCLDEFRIGGVKTNIYF LKNMLLDKNFQAGSCNVNYIDHHPDLLNAPQVIDEPAAGLLAYIGEVTVNGFHGNGSNPK PRFETPVKLNAADEACPSGTRQLLEELGPEKFSKWIQDQKQVLLMDTTYRDAHQSLLATRI RTRDIMQAIHYTACKVPQIYAFEDWGGATFDVAYRFLDEDPWERLRKMREAAPNILFQML TRGANTVGYTNYPPEVVRQFLALAAKNGVDVFRIFDCLNQLDHMTLSIDEVRKQGKLAET AFCYTGDILDDGRQKYTLKYYTNLAKEMEKAGANIIAIKDMAGLLKPEAAYTLISALKDAVDL PIHLHSHEGGGCTLYTYAKAAEAGVDIVDVATSALSNGTSQPSMTAFIQALSNNPRQPQM DIEELETIDRYWQWRAYYAGVDGKMTSPNTTVFQHEMPGGQYTNLRQQAKGVGLGDR WPEVCRMYAKVNEMFGDVIKVTPSSKVVGDMTLFMVQNNLTEKDIYERGETMDFPKSW DFFDGKLGVPYGGFPEKLQKIILRGEQPHLETPPAPIDQEKVTQDMKALRMPETEEARSSY CIYPKVYKDYIQRYHQYGDLSILDTPTYFFGMKPGEESWLRIGGKMVLIRMNYITPPSDDG FREIQFEVNGMPREIRVRDKAASEGAAIIRQADPTVPGEVAATLSGSVLRLIAAKGDWKKG DPLMVTEAMKMETTITAPIAGIVKEVCVAAGSRITSGDLLAVIE Malate dehydrogenase_MJ_0025 Nucleotide sequence (SEQ ID NO:49) atgaaggtaacagttgttggtgcaggtaatgttggtgcaacggtcgcaaacgttcttgctacgaagaagttctgcagcgaggttgt tcttgttgatatcaaggaaggcgttccgcagggcaaggccatggatatcatgcagacggctcacatgctgaactttgacacgac ggtaacgggcgttacggctctgccgaacgatccggaaggctatgctccgacggctggttctgatgttgtcgttgtcacgtctggc atgccgcgcaaaccgggcatgagccgtgaggacctcatcggcgtcaacgctaagatcgtcaagagcgttgttgaccaggcc ctcaagtattccccgaatgcttacttcatcatcatctccaacccgatggacgctatgacgttcctgacgctcaaggacacgaagct cccgcgcaaccgcatcctcggccagggcggcatgctcgacagcagccgtttccgttatttcctcgcacaggctctgacgaagg ctggctatccggctacgccggctgacgttgatggcatggtcatcggcggccacagcgacaagacgatggttccgctcgtcagc tatgcaacgctgcgcggcatccctgtaacgcagctcctgagcaaggaagcactcgacgacgttgtcgctcagacgaaggtcg gcggcgctacgctgacgaagctcctcggcacgtccgcttggattgcaccgggcgctgcagctgctacgatggttgaagccatc gccctcgatgccaagaagctcatcccgtgctgcgtctacctcgaaggcgagtatggcgagaaggacctctgcatcggcgtac cgtgcatcctcggcaagaacggcctcgagaagatcgtcgagatcaagctcgatggcgacgagaaggctaaattcgaagag agcgttcaggctgctcgcaacacgaacgcaaaactcggcgatgccctcaaataa Amino acid sequence (SEQ ID NO:50) MKVTVVGAGNVGATVANVLATKKFCSEWLVDIKEGVPQGKAMDIMQTAHMLNFDTTVTG VTALPNDPEGYAPTAGSDVWVTSGMPRKPGMSREDLIGVNAKIVKSVVDQALKYSPNAY FIIISNPMDAMTFLTLKDTKLPRNRILGQGGMLDSSRFRYFLAQALTKAGYPATPADVDGM VIGGHSDKTMVPLVSYATLRGIPVTQLLSKEALDDWAQTKVGGATLTKLLGTSAWIAPGA AAATMVEAIALDAKKLIPCCVYLEGEYGEKDLCIGVPCILGKNGLEKIVEIKLDGDEKAKFEE SVQAARNTNAKLGDALK NADP-dependent malic enzyme_MJ_1705 Nucleotide sequence (SEQ ID N0:51) atgagcaaattgaacgaccaggcattggccctgcatagagaacaccacggcaagatcgagatgcacagcaaggtccccct ccagaaggcgaaggacctgacgctggcctactcgccgggcgtcgctgcgccgtgcttggagattcagaaggactacaacaa gatctatgactacaccaacaagggcaacacggtcgccgtcgtgacgaacggcagcgctgtactcggcctcggcaacatcgg cgctggcgccggcctgccggtcatggagggcaagtccatcctgttcaagggcttcgcaggcgtcgactccgtccccatctgcct cgacacgcaggacgtcgatgagattgtccgcgccgtcgagctcatggcgccgacattcggcggcatcaacctcgaggacat caaggcaccgcagtgctttgacatcgagaagcgcctgcagaaactcgatatcccggtcttccacgacgaccagcacggcac ggccatcgtcgtcgtctcggccctcatcaacgccttcaagctcacgggccgcaagttcgaggagtcgaagttcgtcctcaacgg cgcaggtgccgctggccaggccatcacgcacctcatttacagcatgggcggccgcaacatcatcctctgcgaccgcatgggt gccatctacgaaggccgcaaggaagacatgaacccctacaaggacgccatcgccaaaatcacgaacccgcagcatgag gcgggccagctcaaagacgtcatcaaggacgccgacgtcttcatcggtgtctccgtagccggtgcagtcacccaggacatgg tccgctccatgaagaaggacccgatcgtcatgggcatggccaacccgacgccggaaatcatgccggatgaggcctacgctg ccggtgcccgcatcgtctgcacgggccgcagcgactacccgaatcaggtcaacaacctgctggccttcccgggcatcttccgc ggcgctctcgacgtccgcgcgaaaaagatcaacgaagagatgaagatggctgccgccaaggccatcgccgacctcatcga cgagagcgaactcgatgagcagcacgtcatcacgagcccgttcgacccgcgcgtcgcaccgcacgtcgccgcagccgtag cagatgccgccatcaagactggcgtcgcccgcatcaccgacatcacgcccgacgaggtagccgagcacacccgccagctc ctcgccgccgagcacgccagcgaggcctga Amino acid sequence (SEQ ID NO:52) MSKLNDQALALHREHHGKIEMHSKVPLQKAKDLTLAYSPGVAAPCLEIQKDYNKIYDYTNK GNTVAVVTNGSAVLGLGNIGAGAGLPVMEGKSILFKGFAGVDSVPICLDTQDVDEIVRAVE LMAPTFGGINLEDIKAPQCFDIEKRLQKLDIPVFHDDQHGTAIWVSALINAFKLTGRKFEES KFVLNGAGAAGQAITHLIYSMGGRNIILCDRMGAIYEGRKEDMNPYKDAIAKITNPQHEAG QLKDVIKDADVFIGVSVAGAVTQDMVRSMKKDPIVMGMANPTPEIMPDEAYAAGARIVCT GRSDYPNQVNNLLAFPGIFRGALDVRAKKINEEMKMAAAKAIADLIDESELDEQHVITSPFD PRVAPHVAAAVADAAIKTGVARITDITPDEVAEHTRQLLAAEHASEA Fumarate hydratase alpha subunit_MJ_0315 Nucleotide sequence (SEQ ID NO:53) ttgcgagaactcgacgcaaaacaaatcacggaaaccgttgcacagctgtgcaaggaggcggcttattacctgccgaaagat gtctatgagggcctcaagaagggccgcgagacggagaagtccccggttggccaggctgtactcgaccagattatcaagaat gcggaaatcgcacgcgatgaggatcgcccgtactgccaggataccggcatgacgatcgtcttcctcgaggtaggccaggac ctccacatcgtcggcggcgacctcgaagaggcagtcaacgacggtatcgccaagggctacacggaaggctacctgagaaa atcggtcgttgcagagccaatcttcaaccgcgtcaacacccagaacaacacgccgggcgtcatctacacgaagatcgttccg ggcgacaagctcaagatcacggttgagccgaagggcttcggttccgagaacaagggcggcatcaagatgctcgtaccggct gacggccttgagggcgtcaagaaggctgtcatggagatcatcctgcatgccagcatgaacccgtgcccgccgatggtcgtcg gcatcggtatcggcggcacgatggaccgcgccgctgtcatgagcaagattgccctgacgcgttcgatcgactcgcataaccc gatgccagaatatgcgaaactcgaagacgatctcctcgagctcatcaatgaaacgggtattggaccgcagctcggcggcac gacgtcctgcctcggtgtcaacatcgagtggggcccgacgcacatcgccggcctgccggtcgctgtgacgatctgctgccatg catgccgtcatgcaaagcgcgttctttga Amino acid sequence (SEQ ID NO:54) MRELDAKQITETVAQLCKEAAYYLPKDVYEGLKKGRETEKSPVGQAVLDQIIKNAEIARDE DRPYCQDTGMTIVFLEVGQDLHIVGGDLEEAVNDGIAKGYTEGYLRKSWAEPIFNRVNTQ NNTPGVIYTKIVPGDKLKITVEPKGFGSENKGGIKMLVPADGLEGVKKAVMEIILHASMNPC PPMVVGIGIGGTMDRAAVMSKIALTRSIDSHNPMPEYAKLEDDLLELINETGIGPQLGGTTS CLGVNIEWGPTHIAGLPVAVTICCHACRHAKRVL Fumarate hydratase beta subunit_MJ_0314 Nucleotide sequence (SEQ ID NO:55) atggcagaacctattcgcatccataccccgttcacggaagaagattcccacaagctcaagatcggcgacagcgttctcatcac gggcgagatctacgctgcacgcgatgctgcgcacaagaagatgtgcgaggcactcgctaaaggcgagaagctgccgatcg actggcacaacaagatggtctattacctcggaccgactccggcaaaaccgggtgatccgatcggctcctgcggcccgacgac ttctggccgcatggatgcctacacgccgacgatgctcgagcagggcatcaagggcatgatcggcaagggctcccgttcgaag gaagtcgtcgattccatgaagaagaacggcgttacgtatttcgctgctgtcggcggtgccgcagcgctcatcgcgaagtccgtc aagaagtacgaagttctcgcttacccagaactcggcccggaggcacttgcccgcctgaccgttgaggatttcccagctattgttg tcatcgactgcgaaggcaataacctttacgatgtcaaccaggagaagtatcgtaccctgaagggttactga Amino acid sequence (SEQ ID NO:56) MAEPIRIHTPFTEEDSHKLKIGDSVLITGEIYAARDAAHKKMCEALAKGEKLPIDWHNKMVY YLGPTPAKPGDPIGSCGPTTSGRMDAYTPTMLEQGIKGMIGKGSRSKEVVDSMKKNGVT YFAAVGGAAALIAKSVKKYEVLAYPELGPEALARLTVEDFPAIVVIDCEGNNLYDVNQEKYR TLKGY Succinate dehydrogenase cytochrome b558 subunit MJ 0313 Nucleotide sequence (SEQ ID NO:57) atgttccatacaactttttatctgcgccgtctgcactcgttagtcggcctgctggcaatcggcattttcctcttcgagcatatcattacg aatgctcgtgcactcggcggtgctgagtccctcaacggtgctctggccatgatggagctcatcccgcatccgatcttcctcggcct ggagatcttcggtgtcgcactgccgatcctcttccatgccatctacggcatctacatcgcccttcaggcgaagaacaacccggg ccgctacggctacgtccgcaactggcagttcgctctgcagcgctggacggcatggttcctcgtcatcttcctcatctggcatgtgtt ctacctgcgcatcttcacgaaggccatcaacggcacgccgatctcgtatgagctgctgcatacgctcttcacgagcagcccgat cacgacgctgctctacacgatcggcatgttcgcagctatcttccatttctgcaatggtatcacgactttctgcatgacctggggcat cgccaagggcccgcgcatccagaacgtcatcaacgttctctcgatgtgcctctgcgcattcctctgccttgtcacgattgcgttcat ggcaagctactttgtcatgtaa Amino acid sequence (SEQ ID NO:58) MFHTTFYLRRLHSLVGLLAIGIFLFEHIITNARALGGAESLNGALAMMELIPHPIFLGLEIFGV ALPILFHAIYGIYIALQAKNNPGRYGYVRNWQFALQRWTAWFLVIFLIWHVFYLRIFTKAING TPISYELLHTLFTSSPITTLLYTIGMFAAIFHFCNGITTFCMTWGIAKGPRIQNVINVLSMCLC AFLCLVTIAFMASYFVM Succinate dehydrogenase flavoprotein subunit_MJ_0312 Nucleotide sequence (SEQ ID NO:59) atggctaagaaaccagaaaataagattattgtcgtaggcggcggcctctcgggcctcatggctacgctgaagatctgcgaagg cggcggcaaggttgacctcttctcttactgcccggtcaagcgttcccactccctctgtgcacagggcggcatcaacgcctgcatg gacacgaagggtgagcatgactcgatctacgagcatttcgatgatacggtctacggcggcgacttcctcgctgaccagctcgct gtcaagggcatggtcgaagctgcaccgaagctcatcaagatgttcgaccgcatgggcgtgccgttcacgcgcacggctgaag gtgttctcgacctccgtaacttcggcggccagaagaacaagcgcacggtcttcgctggctccacgacgggccagcagctcctc tacgctctcgacgagcaggttcgccgttgggaagtaaagggcggcgtcaagaagtatgagttctgggaattcatcaagatcat caagaacaaagagggcatctgccgcggtatcgtcgcgcagaacatgaactccaatgagatcgtctcgttcccggctgacgttg tcatcctcgcaacgggcggccctggccaggtatacggccgctgcacggcttcgacgatctgcaacggttcggctgtttccgctgt ttaccagcagggcgctgagctcggcaacccggagttcctccagatccatccgacggctatcccgggttccgacaagaaccgc ctgatgtccgaggcttgccgcggtgagggcggccgcgtctgggtttaccgcaagaacccgcagacgggcgaaaaagagcg ctggtacttcctcgaggatatgtacccggcatacggcaacctcgtaccgcgtgacgttgcatcgcgtgccatctacaaggtcgtc gtccacatgggcctcggcatgcacaacccgaaccgcgtctacctcgacctctcgcacatcccggctgattacctcgagcgcaa gctcggcggcatccttgagatgtacagcgacttcatgggccaggatccgcgcaaggtcccgatggagatcttcccgtcgatcc actactcgatgggcggcatctgggtcgatcgcgagcatcacacgaacatcccgggcctcctcgcttccggcgagtgcgattac cagtaccacggcgcaaaccgcctcggtgcaaactcgctgctgtcggcaacgtactcgggcacgatttctggcccagagtccct gcgcctcgcacgcagcggcaagctcggctctgccctgacggcagaagagctcgaggctgcccgccaggagtgcgtcgcag agttcgacaagatccgcaacatgaacggcacggagaatgcgcataagctccatcatgagctcggcgacatcatgtacaagt acgtctccatcgagcgcgacaacaacggcctcaaagaatgcgtcaaggaactcaaggaaatcctcaagcgctgggacaac atcggcgttacggaccacggcacttgggcaaaccaggaagcgatgttcgtccgccagctgcgcaacatgatcatctatgcgat ggccatcacgcagtccgctctgcagcgtgacgagagccgcggtgctcatgcgaagatcgtcctgaagtccgattacgataag atggacgaccagctcaaggaagccctcacgaagaagtacggcaagttccacttcgacgctgagacgggccgtggcacgac ggatgacggcaacgacgacctcgtattcttcgagcgcaacgataagaagttcatgcgcacgaccatcgttaccttcgaccagg agaaggaagagccggtcgtttcctaccgtgaattcgagcactctctcatcaagccgcgtctgcgcaactatgccgtagctaaga aagagtaa Amino acid sequence (SEQ ID NQ:60) MAKKPENKIIVVGGGLSGLMATLKICEGGGKVDLFSYCPVKRSHSLCAQGGINACMDTKG EHDSIYEHFDDTVYGGDFLADQLAVKGMVEAAPKLIKMFDRMGVPFTRTAEGVLDLRNFG GQKNKRTVFAGSTTGQQLLYALDEQVRRWEVKGGVKKYEFWEFIKIIKNKEGICRGIVAQN MNSNEIVSFPADVVILATGGPGQVYGRCTASTICNGSAVSAVYQQGAELGNPEFLQIHPTA IPGSDKNRLMSEACRGEGGRVWVYRKNPQTGEKERWYFLEDMYPAYGNLVPRDVASRA IYKWVHMGLGMHNPNRVYLDLSHIPADYLERKLGGILEMYSDFMGQDPRKVPMEIFPSIH YSMGGIWVDREHHTNIPGLLASGECDYQYHGANRLGANSLLSATYSGTISGPESLRLARS GKLGSALTAEELEAARQECVAEFDKIRNMNGTENAHKLHHELGDIMYKYVSIERDNNGLK ECVKELKEILKRWDNIGVTDHGTWANQEAMFVRQLRNMIIYAMAITQSALQRDESRGAHA KIVLKSDYDKMDDQLKEALTKKYGKFHFDAETGRGTTDDGNDDLVFFERNDKKFMRTTIV TFDQEKEEPWSYREFEHSLIKPRLRNYAVAKKE Succinate dehydrogenase iron-sulfur protein_MJ_0311 Nucleotide sequence (SEQ ID NO:61) atggcagaacagaaaaaagtcagaatcatcgtcgagcgccaggacggcccgaaagagaagccgtacaaccaggagttc gagatcgactatcgtccgggcctcaacatcgttgctgccctgatggaaatccagaagaacccggtaacggtcgacggcaaga aagtcccgccagtgacgtgggaatgcaactgcctcgagaaagtctgcggcgcctgcatgatggtcatcaacggcaaggctcg ccaggcttgctgcacgctcgttgatacgctcaagcagccaatccacctgcagccggcccgcacgttcccggtcatccgcgacc tgctcatcgaccgctccgtcatgttcgagagcctcaagcgcatccacggctgggtcgaagtcgacggcacgtgggaggtcaa ggatgctccgatccagaacccgtacacggcacagacggcctacgagatctcgcactgcatgacctgcggctgctgcctcgag gcctgcccgaacgtcggcccgcagtccgacttcatcggaccggctccgacggtacaggcttaccttttcaacctccatccgctc ggaaagttcgacgctccgaagcgcctgaacgcactgatggagaagggcggcatcacgagctgcggcaacagccagaact gtgtcgaagcttgcccgaagaacatcaagctgacgacgtatctcgcacagctcaaccgcgatgtcaacaagcaggccctga agaatatcttcaatcactga Amino acid sequence (SEQ ID NO:62) MAEQKKVRIIVERQDGPKEKPYNQEFEIDYRPGLNIVAALMEIQKNPVTVDGKKVPPVTWE CNCLEKVCGACMM VINGKARQACCTLVDTLKQPIH LQPARTFPVIRDLLIDRSVM FESLKRI HGWVEVDGTWEVKDAPIQNPYTAQTAYEISHCMTCGCCLEACPNVGPQSDFIGPAPTVQ AYLFNLHPLGKFDAPKRLNALMEKGGITSCGNSQNCVEACPKNIKLTTYLAQLNRDVNKQ ALKNIFNH ATP synthase epsilon chain_MJ_0869 Nucleotide sequence (SEQ ID NO:63) atggcgactatcaagctggagattgtctcaccggataaagtggtctacgagaatgacatcagcatgctgatcgtccgctcgacg ggcggtgagctcggcatcctgccgcaccatgccccgctcgtcgcgggtctcgtgccgcatgccatgcgcatccgcctcggcgc agaccgcgatgagcagctcatcgcggttgcgggcggcttcatggaagtcacgccggagaagatcacggtcctcgcgacggc tgctgagcagccaatcgacattgacatcaaccgcgcgaaggaggccatggcccgcgccaaggcccgcatcgccgccttcc atcagggcacgcctgagggcaaggacgtcgatatcgaccgcgccgaactcgcactgcgccgctcgagtgcgcgtctgcgcg cactcggctcgcaattcgaagaataa Amino acid sequence (SEQ ID NO:64) MATIKLEIVSPDKVVYENDISMLIVRSTGGELGILPHHAPLVAGLVPHAMRIRLGADRDEQLI AVAGGFMEVTPEKITVLATAAEQPIDIDINRAKEAMARAKARIAAFHQGTPEGKDVDIDRAE LALRRSSARLRALGSQFEE ATP synthase beta chain MJ 0868 Nucleotide sequence (SEQ ID NO:65) ttggcaaaaggtaaagtcgtacaggtcatcggacctgtcgtagatattgaattcccggcgggcgagctgccggcaatcctcaat gccgtcaccatcaagggcaagacgagcattgacatcgacctcgtcgtcgaggtcatgcagcatcttggcgacagcgtcacgc gctgcatcgccatgagctcgacggacggtctgacgcgcggcatggaagcagtcgacacgggcaacccgatcatggtcccg gttggcacggagtgcctcggccgcgtcttcaacgtactcggtcagacggttgaccacaacccggctcctgtcggcaacaagg agtcctggccgatccatcgcccggctccgaagttcgacgagcaggagacgagcgcgcaggtcctcgagacgggcatcaag gtcgtcgacctcatcgctccgtactccaagggcggcaagacgggcctcttcggcggcgcaggcgtcggcaagacggtcctca tcatggagctcatccacaacatcgcgacggagcacggcggttactccgtcttcgccggcgtcggcgagcgcacccgtgaggg caacgacctctggggcgagatgactgagtcgggcgtcatcgacaagacggcactcgtctacggccagatgaacgagccgc caggagcacgtatgcgcgtcgccctgacgggcctgacgatggcagagtacttccgcgatgtccagcatcaggacgtgctgct cttcatcgacaacatcttccgcttcatccaggctggttctgaggtttcggcactgctcggccgcatgccgtcggccgtcggttatca gccgacgctgtccacggatatcggtgctctgcaggagcgcatcacctcgacgaagaatggttccatcacgtcggttcaggcag tctatgtcccggccgatgacctgacggacccggcaccggctggtacgttcacgcacctcgatgccacgacggtcctctcgcgtc agatcgccgagctcggcatctacccggccgtcgatccgctcgattcgacgagccgcatcctcaacgccgaagtcctcggcga ggagcattacgaagttgcccgcggtgtccaggccgtgctccagaagtacaaggagctccaggacatcatcgccatcctcggc atggaagagctctccgatgaggataagctgactgtctcgcgtgcgcgcaagatccagcgctttctctcgcagcccttcttcgtcg cagaggtgttcacgggttcgccgggcaagtacgtgccgctcaaggagacggtacgcggcttcaaggagatcctcgagggca agtacgatgacctgccggagaatgccttctacatggtcggcacgatcgatgaggcagtggagaaagcacggaagatcaaa gaagaggagggataa___________________________________________________________ Amino acid sequence (SEQ ID NO:66) MAKGKWQVIGPVVDIEFPAGELPAILNAVTIKGKTSIDIDLVVEVMQHLGDSVTRCIAMSST DGLTRGMEAVDTGNPIMVPVGTECLGRVFNVLGQTVDHNPAPVGNKESWPIHRPAPKFD EQETSAQVLETGIKVVDLIAPYSKGGKTGLFGGAGVGKTVLIMELIHNIATEHGGYSVFAGV GERTREGNDLWGEMTESGVIDKTALVYGQMNEPPGARMRVALTGLTMAEYFRDVQHQD VLLFIDNIFRFIQAGSEVSALLGRMPSAVGYQPTLSTDIGALQERITSTKNGSITSVQAVYVP ADDLTDPAPAGTFTHLDATTVLSRQIAELGIYPAVDPLDSTSRILNAEVLGEEHYEVARGVQ AVLQKYKELQDIIAILGMEELSDEDKLTVSRARKIQRFLSQPFFVAEVFTGSPGKYVPLKET VRGFKEILEGKYDDLPENAFYMVGTIDEAVEKARKIKEEEG ATP synthase gamma chain _MJ_0867 Nucleotide sequence (SEQ ID NO:67) ttggctagtttacaggatattcgccatcgcatcaagagcgtaaagagtaccaagcagatcacgagtgccatgaacatggtcgct acgagccgtctgcgccatgccaaagaggctgcaaccgcgaaccgtccctatgcacagaaggtcagcgaggtcgtccacgc catcgccaagaatgcaggcatggacttctcgcacccactgctcgagaagcacgaggatggcaggaagctcgtcttcctgatc acctcggacaagggattggcaggtgcgtattcgtcgaatgcctgcaaggcggcagagaccctcatcgagaaagcggacgat acggacttcgtcatcgtcggccgcaagggcgtgggccacttcaagacccgcggccacaaggtcatcaaggagttcatcggc atcagcgagcacccgtcttctgaggcggcgcgggacatcgctctcgagctcatccagctctacaagacgggcgagtaccgcg aggtcgacatggtctacacgaagttcgtctcggccatcagctgcgagccgaaatcgggggcgctgctcccgttcgccccgctg aaggcagaggaccaggacgacctgaacgtcgagtacatctatgagccagatgccgctacggtgctcggtttcatgctgccgc agtatctcttcacggtcgtttatgcagcgcttctgcagtcggcagccagcgagctctcctcgcgcatgaacgcgatgagcaacg cgacggacaacgcagaagacctcatggataaactcaatctgcattacaacaaggtacgtcaggctggcattacccgtgagat cactgagattgtcggcggcgccgaagcccttaagtga Amino acid sequence (SEQ ID NO:68) MASLQDIRHRIKSVKSTKQITSAMNMVATSRLRHAKEAATANRPYAQKVSEWHAIAKNAG MDFSHPLLEKHEDGRKLVFLITSDKGLAGAYSSNACKAAETLIEKADDTDFVIVGRKGVGH FKTRGHKVIKEFIGISEHPSSEAARDIALELIQLYKTGEYREVDMVYTKFVSAISCEPKSGAL LPFAPLKAEDQDDLNVEYIYEPDAATVLGFMLPQYLFTVVYAALLQSAASELSSRMNAMSN ATDNAEDLMDKLNLHYNKVRQAGITREITEIVGGAEALK ATP synthase alpha chain _MJ_0866 Nucleotide sequence (SEQ ID NO:69) atgaaaatgaatccggaagaaataacggccatcatcaaggaccagatcaagaattacgatgtggacctcaatgttgatgatgt tggttccgttatcgagatcggtgacggcatcgcacacatccatggcctcgacaaggctatggcgggcgagctgctcgatttcgg caatgatatttatggtctggtcctgaaccttgagcaggacaacgtcggtgccgttatcttaggcggcgagacgaaaatcaaaga gggctcgcaggtcaagcgcacgggccgcatcatgcaggttcctgtcggtgaggccatgatcggccgcgtcgtcgatgccctc ggccgtccaatcgacggcaagggcaagatcgagacgacggagacgcgtccggtcgagtacccggcaccgggcatcgca gaccgcaagccggtcaaggagccgctgcagacgggcatcaaggccatcgacgccctcgtaccgatcggccgcggccagc gcgagctcatcatcggtgaccgcggcatcggcaagacggccatcgccatcgacacgatcctcaaccagcacgaccagaac tgcatctgcgtctacgtcgccatcggccagaaggcctcgacggtcgcgcgcgtcgtcaagacgctcgaagagcgcggcgcc atggactacacgatcgtcgtcgctgctacggctgctgacagctcgccgctgcagtacctcgcaccgtatgccggtgtcgctatgg ctgagcacttcatgtatcagggcaaggcctgcctctgcgtctacgatgacctcacgaagcacgcagctgcttaccgcgccatgt ccctgctgctccgcagaccgccaggacgtgaagcatatccgggcgatgtcttctacttgcattcccgcctgctcgagcgcgcag cgaagctcaacgatgagctcggcggcggctccatcacggctctgccgatcatcgagacgcaggccggcgacctctcggcct acatcccg acg aacgtcatctccatcacg gacg g ccag atcatg ctcg ag acgg actccttctattctg gtatccg cccg gcca tcaacgtcggcctctccgtatcgcgtgtcggcggctcggctcagatcaaggccatgaagcaggtagcaggtaccctgcgcctc gacctcgcgcagtaccgcgagctcgcagcgttctcgcagttcgcctcggacctcgacaaggagacgaaggcacagctcgac cgcggtatccgcatggtcgagacgctgaagcagccgcagtacagcccgctgctcgtccaggaacaggtcatggtcatctaca cggccgccaagggctatcttgttgatatcccggtcgagaaggtcgtcgagttccagacggacttcctgaagttcatgcgcacgc agcatccggaagtcgcacagaagatcattgaccagaagaaactcgatgatgctctggagacggagctcaagaacgcgatc gtggagttcaaggaaactgtaccgtataaaatggcgtaa Amino acid sequence (SEQ ID NO:70) MKMNPEEITAIIKDQIKNYDVDLNVDDVGSVIEIGDGIAHIHGLDKAMAGELLDFGNDIYGLV LNLEQDNVGAVILGGETKIKEGSQVKRTGRIMQVPVGEAMIGRWDALGRPIDGKGKIETT ETRPVEYPAPGIADRKPVKEPLQTGIKAIDALVPIGRGQRELIIGDRGIGKTAIAIDTILNQHD QNCICVYVAIGQKASTVARVVKTLEERGAMDYTIVVAATAADSSPLQYLAPYAGVAMAEHF MYQGKACLCVYDDLTKHAAAYRAMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLNDEL GGGSITALPIIETQAGDLSAYIPTNVISITDGQIMLETDSFYSGIRPAINVGLSVSRVGGSAQI KAMKQVAGTLRLDLAQYRELAAFSQFASDLDKETKAQLDRGIRMVETLKQPQYSPLLVQE QVMVIYTAAKGYLVDIPVEKVVEFQTDFLKFMRTQHPEVAQKIIDQKKLDDALETELKNAIV EFKETVPYKMA ATP synthase delta chain _MJ_0865 Nucleotide sequence (SEQ ID N0:71) atgctaaacttacagcttgtacggaaatacgccaaggcaatcttcgagattgcgcaggaagaggaaaagctcgtggagtatg gcgatgaactcaaggctgcgcgcgagggcatcgagtccgtgccgcaggcgatggagttcttctccaatccgcaggttgatccg aagcagaagaaggagctcctgcagaaatgcttcaagaaagagctctcgaagaacgtgtaccatttcctgctgctgctggtcga caagcaccgcttcgtgctgttcccggcaatagtggatgagtaccgcgtgctctcgaatgaagccaggggcatcctgatcgcgg acgtgacgacggtcgcgcctgcctcgaagaagcagcagaaggccatcgcagacaaattggaacagataacgggcaaga aagtggagctccgcctccacgaggacaagtcccttatcggcggcgtcgtcgtcaagatcggtgaccgccgcatcgatggcag tgtcgctggccgtctcgagacgatgaagagaaaattactggctaacgagtga Amino acid sequence (SEQ ID NO:72) MLNLQLVRKYAKAIFEIAQEEEKLVEYGDELKAAREGIESVPQAMEFFSNPQVDPKQKKEL LQKCFKKELSKNVYHFLLLLVDKHRFVLFPAIVDEYRVLSNEARGILIADVTTVAPASKKQQ KAIADKLEQITGKKVELRLHEDKSLIGGVVVKIGDRRIDGSVAGRLETMKRKLLANE ATP synthase FO sector subunit b_MJ_0864 Nucleotide sequence (SEQ ID NO:73) ttgatagatatcaatgccacattgatcgctcagatcttgaacttcttgatcttggctggtctccttcgcgctgttgcctataaaccggtc gtgcggatgctcaaagctcgtcaggaccgcatccaggaaagcctcgacaaggcggatgcagatgctgaggaagcggaca agctcctggctgagtacaaggcaaaacttgcggaggcgaacgtcaaggcggagaacatcgtcctgatggccgagaagcgt gcaagtgaggagcgcgaggcaaagcgcgctgaagtcaagcgcgagattgaacagatgcgcaaggcagcaaaggctga gatcgaccgtgagcgcgagcatgcggtccagcagctgcgcaccgagatgattacgctgtccatggcagccgccggtaagat cgttgctaagaacatggacaagtccgagaacgaagcgctgatctcggatttcgtcaaggaactcgacaaggacaagattggt gatctgccatgctaa Amino acid sequence (SEQ ID NO:74) MIDINATLIAQILNFLILAGLLRAVAYKPWRMLKARQDRIQESLDKADADAEEADKLLAEYK AKLAEANVKAENIVLMAEKRASEEREAKRAEVKREIEQMRKAAKAEIDREREHAVQQLRTE MITLSMAAAGKIVAKNMDKSENEALISDFVKELDKDKIGDLPC ATP synthase FO sector subunit c_MJ_0863 Nucleotide sequence (SEQ ID NO:75) atggaaaacgcaatcatggtcgcagcagctctcgtaggtgcaggtctttgcatgggtttggctgcagtcggcgctggcctcggtg atggtcttgtcacgagccgctttatcgaaggtatcacgcgtcagccggaagcacagagcaagctcttcacgaatacgctgatct ccgtcggcctcatcgagtccatggcaatcatcgcaacggtcgttgccctgatcatgctctatgcgaacccgctcatcaaataa Amino acid sequence (SEQ ID NO:76) MENAIMVAAALVGAGLCMGLAAVGAGLGDGLVTSRFIEGITRQPEAQSKLFTNTLISVGLIE SMAIIATVVALIM LYAN PLIK ATP synthase FO sector subunit a_MJ_0862 Nucleotide sequence (SEQ ID NO:77) atgcatgaaattggtgttcgcgaagtagtgcatttcgccgggttgacattcaactgggagaccctttgcatgacttggctcacgatg gcgatcgtcatcctgatctcatggctggcaacgcggaacctcaagatgattccgacgggctggcagaatgtggtggagatcct cgtctcgtggctcgacacgcaggtgagctccatgatgggcaagcggggactgttcctggcgccgttcatcatgtcgctgttcatgt tcctgctgacgtcaaactggctgggactcatcccgacgttgtcttcgccgacgaatgacttgaacaccaccttggggctggcgct gctcgtcgtcgtactggtacacgtactgggtgtccacatgaagggcggtcattatatcgcgcatttcttcaagccgacgccggtatt tgtcatcatcaacgcgatcgaagagattgccaagccaatcacgctgtcgttccgtctattcggcaacatcctagcaggtgagatc ttgatcatcatcctgctcaagctgatgccaatctggatgccgatcccgtcagtcatctggctggcattcagtatctttgtcggcggag tccaggcgttcatcttcacgatgctgtcgatggcttaccttgcgaatgcagtcaaggaagatgaagaagagtcgtga Amino acid sequence (SEQ ID NO:78) MHEIGVREVVHFAGLTFNWETLCMTWLTMAIVILISWLATRNLKMIPTGWQNVVEILVSWL DTQVSSMMGKRGLFLAPFIMSLFMFLLTSNWLGLIPTLSSPTNDLNTTLGLALLVVVLVHVL GVHMKGGHYIAHFFKPTPVFVIINAIEEIAKPITLSFRLFGNILAGEILIIILLKLMPIWMPIPSVI WLAFSIFVGGVQAFIFTM LSM AYLANAVKEDEEES ATP synthase protein l_MJ_0861 Nucleotide sequence (SEQ ID NO:79) atgaaacagattttatcggtcttcatgaagcgtctcgcgattgcccttgggcttgcggcgctgatgatcggcagccttctgctcgcg agaggagaagggcagctcatcggcgcactcttcctcggctatttcgcggcgctggtatttgtctggaacatggcctggcgcctct ggcgcctgacgtacatgcagagtggcggcaagaggcagatgctctggggcatggtgctccggatgctcgtgctcttcctcgtcc tgctcgtcgcggtgacgatctccgtaccggtattcctcgtcacggcgctcggttttctcgtctgctatggactcgccctgttcctgctg atccacatgaacctcggtaaaaaataa Amino acid sequence (SEQ ID NQ:80) MKQILSVFMKRLAIALGLAALMIGSLLLARGEGQLIGALFLGYFAALVFVWNMAWRLWRLT YMQSGGKRQMLWGMVLRMLVLFLVLLVAVTISVPVFLVTALGFLVCYGLALFLLIHMNLGK K ATP synthase protein l MJ 0860 - may be used in addition or alternatively to 0860 above Nucleotide sequence (SEQ ID NO:95) atggacgagaaaaacaaggacacgacgcatgagatgctgcgcacgggcctgcgccaggccatcaaggctttcgctgtcttg agtggcgtcggcatctacctcgccgtcttcgtcggcatctgtctgttcctcgggaatctggcggacacgtatctcttgggcggcgg ctatgcaggcaagctcacgggcatcctcgtcggcttccccggcgccttctacaccctgttccgtcagctcaagcagaacgggat tgtctga__________________________________________________________________________________________ Amino acid sequence (SEQ ID NO:96) MDEKNKDTTHEMLRTGLRQAIKAFAVLSGVGIYLAVFVGICLFLGNLADTYLLGGGYAGKL TGILVGFPGAFYTLFRQLKQNGIV Permease (AR1Y2_1114)_____________________________________________________ Nucleotide sequence (SEQ ID N0:81) gtgaatttacaaatcttagtcttagtcctggcgattgtcctgtttggagttctggcatttaaacagatgagcgctttgatcctggctccg cttgtcacgatctttgttgtcatctgctcgaaactcccaattctggactcgttaaaaaatgcgttcatgcctgcagcgtccgactacgt gacaaagtatttccttgtcttctttgtcggcgcactgtttggttctgtttaccagtatactggagccgcagaatccattgccagagcca tcgcaggtctctgccgcggaaagttcgtggcaccgatcatcatgatcatcaccggtcttttgacctttggaggagtcagtggctttg ttgtattctttgttatctatccgatcgctctgaacttatttaaagaggcgaaccttacgagaaggcttatcccggctgcaatctctgcc ggatgctggacctggtccatgagcggccctggttctccttccattcagaacgttattgctatggataaccttggtacaccggcaact gccgcatttgttccatctctgatcacaacggttgctatgtttttaatgatctttgtatggctggaaatgcgcgcaagaaagtttacaaa aaagggataccgctttattgacaaatctttaaagtatcaattaagtgaagaggagacggcaattgatgaaaacaaagatcttcc tcatgttgccatcgctatccttccgatcattgtaatcctggtactctttaacattgtaaagctgccggtagagacatccgtatttgcag gcgtggctctggctacagttctgatgttcaagagagtcaaaggcatcaacgaatggatcaatgtctttaacaaaggggcatctg attccggtgtcgctatcctgaatactgccattgtcgtaggattcggcggcgttgtgcagaaaacacaggggtttacagatctggtc gctgctctcaaagatatgagcatgccgcctctggtatttgtaatgatcactgtggctgtctgtgcaggagcctgcggttccgcttccg gcgggatgggcgttgccttcaatgcactgaagtctacctatatcaagatgggaattcctctgccttatgtacataggatttccgcaa ttgccgctggtacattggatacccttcctcaccagggagcgcagatcactctgctcggcatttgtaaaatgacccataaggaagc ctactgggatattgcggttacgcagattatcataccatttatatcctgcggaatctttatcgttttagcttcttttggactataa Amino acid sequence (SEQ ID NO:82) MNLQILVLVLAIVLFGVLAFKQMSALILAPLVTIFVVICSKLPILDSLKNAFMPAASDYVTKYFL VFFVGALFGSVYQYTGAAESIARAIAGLCRGKFVAPIIMIITGLLTFGGVSGFVVFFVIYPIAL NLFKEANLTRRLIPAAISAGCWTWSMSGPGSPSIQNVIAMDNLGTPATAAFVPSLITTVAMF LMIFVWLEM RARKFTKKGYRFIDKSLKYQLSEEETAI DEN KDLPH VAI Al LPIIVILVLFNIVKL PVETSVFAGVALATVLMFKRVKGINEWINVFNKGASDSGVAILNTAIVVGFGGVVQKTQGF TDLVAALKDMSMPPLVFVMITVAVCAGACGSASGGMGVAFNALKSTYIKMGIPLPYVHRIS AIAAGTLDTLPHQGAQITLLGICKMTHKEAYWDIAVTQIIIPFISCGIFIVLASFGL Oxoacid CoA transferase (AR1Y2_1115) Nucleotide sequence (SEQ ID NO:83) atgggaaaagttaaaattatcacagcagatcaggctgctgccctggtggaggatcatacaacgatcacaaccagcggatttgt tgccagcggaatgccggaagctctcacaaaagctttggaaaaaagattcaaagaaaccggatcccccaaaaacctgacttt gttttatgctgccgcccagggaaaccgtgacggaagcggcgcggatcattttgcccatgaaggtatgacaaaacgtgtcatag gcggacattggaacatggttcctgcactgggacagatggttctggacaataaaatcgaaggctataatctgcctcagggaaca ctggcacagttataccgtgccatcgcaggtcacaaacccggcgttatcagtcatgtaggattaaatacatttgctgacccacgca ttgagggcggtaaattaaatgacattacaaccgaagatatcgtcgatgtagttgaaatcctgggagaagagaaattattgtaca aatcgttcccgatcaacatcggatttatccgcggtacatatgcagatgaacacggcaacgtaactctgtctcacgaatgtgccac cacagaggtcacaaccatggctcaggccgtaaagaacagcggcggaaaggtcgttgtacaggtagaaaaggtcgtttcag acggcaccttagatccaaaattagtcaagatccctggaatttatgtggatgccgttgtggaagtagaagacatgaaggatcacg aacaatgcgtgggctgtgattatgatggttccatgaccggagacttccgggttccgttaagcagtcttgagtacccgcctctttccg ccaagaagatcattggacgcagagcagccatggaactgacagaaaacacggttgtaaatctaggcattggtattccagagta catctccatggtagccaacgaagaaggcattggagattacatgactctgactgtagaggccggaccaatcggcggtgtacctc agggaggagctaaattcggaggcgctgtcaatgctgaatgtatcctagatcagccgtaccagtttgatttctatgacggcggcg gagttgactatgcattcttaggactcgcacaggcagataaagacggtaatatcaacgtaagcaagttcggtccaaggattgcg ggctgcggcggtttcgtcaatatcacccagaacgcaaaacgctgctacttctgcggaacttttactgcaggaggtctgaagaca tccgtaaaagacgggaaacttatcattgaccaggaaggaaaatcaaacaaattcctggataccgtagaacagatcaccttca gcggtgaatacgcaaataaagtcggccagccggttctctatatcacagaacgtgctgtattcgaactcagaaaggacggcgtc tatctgacagaggttgcccctggtatcgatatccagacacagatcatcgatcatatgggatttgctccaaagatggaaggaacg ccaaagttcatggatgaaagaatcttcaaagatgagctgatgggcctgaagcacgattaa Amino acid sequence (SEQ ID NO:84) MGKVKIITADQAAALVEDHTTITTSGFVASGMPEALTKALEKRFKETGSPKNLTLFYAAAQG NRDGSGADHFAHEGMTKRVIGGHWNMVPALGQMVLDNKIEGYNLPQGTLAQLYRAIAGH KPGVISHVGLNTFADPRIEGGKLNDITTEDIVDVVEILGEEKLLYKSFPINIGFIRGTYADEHG NVTLSHECATTEVTTMAQAVKNSGGKVVVQVEKWSDGTLDPKLVKIPGIYVDAVVEVED MKDHEQCVGCDYDGSMTGDFRVPLSSLEYPPLSAKKIIGRRAAMELTENTWNLGIGIPEY ISMVANEEGIGDYMTLTVEAGPIGGVPQGGAKFGGAVNAECILDQPYQFDFYDGGGVDYA FLGLAQADKDGNINVSKFGPRIAGCGGFVNITQNAKRCYFCGTFTAGGLKTSVKDGKLIID QEGKSNKFLDTVEQITFSGEYANKVGQPVLYITERAVFELRKDGVYLTEVAPGIDIQTQIIDH MGFAPKM EGTPKFM DERI FKDELMGLKH D Dehydratase (AR1Y2_1116)_______________________________________________________ Nucleotide sequence (SEQ ID NO:85) atgaacaatttattaatggaagtagaaaacgaagtcgcagttgtaacaatcaacagaccaaaatcattaaacgctttaaacagt gaaactttagctgagttagaccagtgctttacagagatttcaggacgcaaggacatcagagtggtgatcctcacaggatcagg cgaaaaatcctttgtagctggtgctgatatctctgaaatggtcaatgcaactcctgcagaaggaagacagatgggtcttttggca aaagaagcatttcttaagttagagacaatgcctcaggtaaccatcgctgccgtcaacggttacgctctgggaggcggatgcga gatctccatggcatgtgatatccgtgtagctgcggaaaacgcaaaattcgcacagccagaaacaggacttggaattcttccgg gattcggcggaacacagcgtctctcccgtttagtaggaaaaggacgcgcaaaggaattgatctttacatgtgaccagatcgatg ccgaagaagcttacagaattggtcttgcaaacaaagtagtgcctcaggcggagctgatcgattactgtaagaagatggctgca aagatcatgtccaaaggaagctacgcaatttcccttgcaaaagaagcgatcaacacaggaatggacacagacttaagcagc ggtcttacattagaagctgacttattcggacttgcattctccactgctgacaaaaaagagggtatgacagcattccttgaaaaacg taaagctgatttaaaagatttctag Amino acid sequence (SEQ ID NO:86) MNNLLMEVENEVAVVTINRPKSLNALNSETLAELDQCFTEISGRKDIRVVILTGSGEKSFVA GADISEMVNATPAEGRQMGLLAKEAFLKLETMPQVTIAAVNGYALGGGCEISMACDIRVAA ENAKFAQPETGLGILPGFGGTQRLSRLVGKGRAKELIFTCDQIDAEEAYRIGLANKWPQA ELIDYCKKMAAKIMSKGSYAISLAKEAINTGMDTDLSSGLTLEADLFGLAFSTADKKEGMTA FLEKRKADLKDF Electron transfer flavoprotein, beta subunit (AR1Y2_1112) Nucleotide sequence (SEQ ID NO:87) atgagaattttggtttatttaaaagaaataccgccggaagaagaacgggatctgtaccaggatacagaggggatcaatgaca gtgatcagaatgtcttaatggaggcactgaatctgagggacaaggaaggcggaactgtgacggtcatggtcatcgggccgtc cacaggagagaagacagcaagggaggcgctgacctggggagttgacaggtcagtcctggttttaaaggatggaaaggcta caggggatatcctggaaagtgcaagagtgctagcaaaagccatagaagcggaaggcacatttgatgtaattttgtgcggaag acaggcgatagatggagatgcggcccatatggcggctatgacggcgtcctttttaaatatcccgcttattgccttctccaaaaaa atggagatctcggacggaaagctgtacaactggtgtatgtccaaagatgggacagaacggacagagtgttgtatgccagcac tggtcctctcagtgaaggaagacaacaaacgaaggcaccccaatgtctgtgatattatgtcagcttatgccgggagcactgtga tcccggttataaaaccagagagaaatacaccggagaagatcattagacaggttgggcagtatacgcccggcaaaaaacac aagaagggaatgatgctggccggaaaagatgaacaggaactggcgggacaactccggcagatattaacgaagttcacgg cagcaaaatag Amino acid sequence (SEQ ID NO:88) MRILVYLKEIPPEEERDLYQDTEGINDSDQNVLMEALNLRDKEGGTVTVMVIGPSTGEKTA REALTWGVDRSVLVLKDGKATGDILESARVLAKAIEAEGTFDVILCGRQAIDGDAAHMAAM TASFLNIPLIAFSKKMEISDGKLYNWCMSKDGTERTECCMPALVLSVKEDNKRRHPNVCDI MSAYAGSTVIPVIKPERNTPEKIIRQVGQYTPGKKHKKGMMLAGKDEQELAGQLRQILTKF TAAK Electron transfer flavoprotein, alpha subunit (AR1Y2_1113) Nucleotide sequence (SEQ ID NO:89) atggaaagagtatcaaagattttgattattggagaaatacaaaatggacagccagccccggtaactctggaattattagggga gggagagaagatagcctcttctctgaacgcaaagcttttactggctgtagcgggcagcggtattcaggagatcttaagtgagctt ttgcagtatcctgtagacaggatcattgcagtggatcatcccaggatggaattggatcaaacggagacccacgccagagttttg gaggccgtgatccgggagcacgagccggatatgattctgggaggagcaacgttgtcaggaaaggtgctgctgccaatgctg gctgcggttcttggaacagaagtggtgacagacgcggctgacctggagattgacaaggaaacagggaaacttctgatcagc aagccggcgtttgacggaaaaagaatgtctatagtatcgatgccaaaggcccacgtacagatcgtttctgtaaagcccgggatt tttgagaaggcctgcaggacggaaagaaaaagaggcggtatcaccatggtggcggctgactggctggaagatatcaaaga gcggaaaaagatgctggagctgatcacagaagacggcaacaagatatctctggaagattcaaagatcatcgcagccggcg gacggggactgaaagggcctgaaggatttgaactccttacacggtttgcaagagaaatcggtgcccaggtgggctgcacaa gaccatgtgtggatgcaggatggacctcgccggagcagcagatcggccagaccggattcacaaccaaaccggatctctatct ggcttttgggatttccggtgcgatccagcatatgaccggagtccgggcaaagaccgtgatcgcagtcaataacaatccaaatg cggcaatttttaattattgcgactatgggatcgtcggggatgcccaaaaaatattgagagaactactaagagaatag Amino acid sequence (SEQ ID NQ:90) MERVSKILIIGEIQNGQPAPVTLELLGEGEKIASSLNAKLLLAVAGSGIQEILSELLQYPVDRII AVDHPRMELDQTETHARVLEAVIREHEPDMILGGATLSGKVLLPMLAAVLGTEVVTDAADL EIDKETGKLLISKPAFDGKRMSIVSMPKAHVQIVSVKPGIFEKACRTERKRGGITMVAADWL EDIKERKKMLELITEDGNKISLEDSKIIAAGGRGLKGPEGFELLTRFAREIGAQVGCTRPCV DAGWTSPEQQIGQTGFTTKPDLYLAFGISGAIQHMTGVRAKTVIAVNNNPNAAIFNYCDYG IVGDAQKILRELLRE Acyl dehydrogenase (AR1Y2_1117) Nucleotide sequence (SEQ ID N0:91) atgaattttgaattaacagagcagcaggcagccattcaggaaacagcaaggaactttgctcagacagaactgcagccaggt gtgctggagagagatgcaaacagtgagtttccggtagatctttataagaagatgggggatatgggcctgatcggtcttccatatc cgaaagaagtcggaggacagggagccgattatctttcttatgcactggcagtggaagagatctcaaaagtagatgcctctgtg ggtatttcctattctgtttccacctctctgtatggcggaagcattatgaactctgatgcttccgttgagaaaaagaatgaatttctagca ccggtactgtccggacagcatttcggatcctttggactcacagagcccaatgccggatcagacgcaggcggatgtgtcactgtg gctgaaaaagatggggacgaatacatattaaatggtatgaagtgttttaacaccaacggacctttggccgattatacagcggtat atgccctgacagaacctgagaagaaagcaaagggtctttcctgctttgtagtaaaaaaaggaactcctggattttctgtaggca aggtggaggataagatgggaatccgctctgcgcaggtctctgagatgatcctggaaaatgtcagagtacctgcagagaatatg gtcgttccatctggggacggatttaagctggccatgaagactttggatggaggacgcatcggcgttgccgcgcaggggcttggt atcgcggagggcgcatttgagatcgcaaaagaatacttaaagagcagagaacagttcggcaaaccattatataaaaaccag tatcttgcatttaagatggcggaacttgaaatggagatcgacgctgcaagatacatgctttacaaagcggctacagataaacac gagggaagatcttactcaatcccggcagcaaaggcaaaatacctttgtacagaggccgctatgcatgtgacaacagaagca gtacagatgttaggtggaaatgggtatatgaagggttaccatgtagaacgtatgatgagagatgcgaagatcactcagatctat gagggaaccaatgaaatccagaagctcgttgtaagcggagctatcttcagatag Amino acid sequence (SEQ ID NO:92) MNFELTEQQAAIQETARNFAQTELQPGVLERDANSEFPVDLYKKMGDMGLIGLPYPKEVG GQGADYLSYALAVEEISKVDASVGISYSVSTSLYGGSIMNSDASVEKKNEFLAPVLSGQHF GSFGLTEPNAGSDAGGCVTVAEKDGDEYILNGMKCFNTNGPLADYTAVYALTEPEKKAK GLSCFVVKKGTPGFSVGKVEDKMGIRSAQVSEMILENVRVPAENMVVPSGDGFKLAMKTL DGGRIGVAAQGLGIAEGAFEIAKEYLKSREQFGKPLYKNQYLAFKMAELEMEIDAARYMLY KAATDKH EGRSYSIPAAKAKYLCTEAAM H VTTEAVQM LGGNGYM KGYH VERM M RDAKIT QIYEGTNEIQKLVVSGAIFR Mitsuokella jalaludinii - 16S rRNA Nucleotide sequence (SEQ ID NO:93) tttgagagtcgagtggcaaacgggtgagtaacgcgtagacacctgccgtaaagatggggacaacagttcgaaaggactgct aataccgaatgttgtagagtttccgcatgggaatcctactaaaggtggcctctacttgtaagctatcgctttacgatgggtctgcgtc tgattagctagttggtggggtaacggcctaccaaggcgacgatcagtagccggtctgagaggatgaacggccacattggaac tgagacacggtccagactcctacgggaggcagcagtggggaatcttccgcaatgggcgcaagcctgacggagcaacgccg cgtgagtgaagaagggtttcgactcgtaaagctctgttgtcggggacgaatgtggagatggtgaataaccattttcaatgacggt acctgacgaggaagccacggctaactacgtgccagcagccgcggtaatacgtaggtggcgagcgttgtccggaattattggg cgtaaagggagcgcaggcgggaaggtaagtctatcttaaaagtgcggggctcaaccccgtgaggggatggaaactatctttc ttgagtgcaggagaggaaagcggaattcctagtgtagcggtgaaatgcgtagatattaggaggaacaccagtggcgaaggc ggctttctggactgtaactgacgctgaggctcgaaagcgtggggagcgaacaggattagataccctggtagtccacgccgtaa acgatgaatgctaggtgtaggaggtatcgacccctcctgtgccggagttaacgcaataagcattccgcctggggagtacggcc gcaaggctgaaactcagaggaattgacgggggcccgcacaagcggtggagtatgtggtttaattcgacgcaacgcgaaga accttaccagggcttgacattgagtgaaaggactagagatagtcccctctcttcggagacacgaaaacaggtggtgcatggct gtcgtcagctcgtgtcgtgagatgttgggttaagtcccgcaacgagcgcaacccctatcctttgttgccagcacgcaatggtggg aactcaaaggagactgccgcggacaacgcggaggaaggcggggatgacgtcaagtcatcatgccccttatgtcctgggcta cacacgtactacaatgggatggacagagagcagcgaagccgcgaggccaagcgaaccccataaaccatctcccagttcg gattgcaggctgcaacccgcctgcatgaagttggaatcgctagtaatcgcaggtcagcatactgcggtgaatacgttcccggg ccttgtacacaccgcccgtcacaccacggaag Anaerostipes rhamnosivorans - 16S rRNA Nucleotide sequence (SEQ ID NO:94) tattttggattgaagttttcggatggatctccttaatgactgagtggcggacgggtgagtaacgcgtggggaacctgccctataca gggggataacagctggaaacggctgctaataccgcataagcgcacagaatcgcatgattcagtgtgaaaagccctggcagt ataggatggtcccgcgtctgattagctggttggcggggtaacggcccaccaaggcgacgatcagtagccggcttgagagagt ggacggccacattgggactgagacacggcccaaactcctacgggaggcagcagtggggaatattgcacaatgggggaaa ccctgatgcagcgacgccgcgtgagtgaagaagtatttcggtatgtaaagctctatcagcagggaagaaataagacggtacc tgactaagaagccccggctaactacgtgccagcagccgcggtaatacgtagggggcaagcgttatccggaattactgggtgt aaagggtgcgtaggtggcatgataagtcagaagtgaaagcccggggcttaaccccgggactgcttttgaaactgtaatgctag agtgcaggagaggtaagcggaattcctagtgtagcggtgaaatgcgtagatattaggaggaacaccagtggcgaaggcgg cttactggactgtcactgacactgaggcacgaaagcgtggggagcaaacaggattagataccctggtagtcnacgccgtaaa cgatgaatactaggtgtcggggccgtagaggcttcggtgccgcagcaaacgcagtaagtattccacctggggagtacgttcgc aagaatgaaactcaaaggaattgacggggacccgcacaagcggtggagcatgtggtttaattcgaagcaacgcgaagaac cttacctggtcttgacatccttctgaccggttnnnaaccgaacctttccttcgggacagaagtgacaggtggtgcatggttgtcgtc agctcgtgtcgtgagatgttgggttaagtcccgcaacgagcgcaacccctatctttagtagccagcatataaggtgggcactcta gagagactgccagggataacctggaggaaggtggggacgacgtcaaatcatcatgccccttatggccagggctacacacgt gctacaatggcgtaaacaaagggaagcgaccccgcgagggcaagcaaatcccagaaataacgtctcagttcggattgtagt ctgcaactcgactacatgaagctggaatcgctagtaatcgtgaatcagaatgtcacggtgaatacgttcccgggtcttgtacaca ccgcccgtcacaccatgggagtcagtaacgcccgaagtcagtgacccaaccgcaaggaggaga Should there be an inconsistency between the sequences disclosed in the description and the sequences disclosed in the sequence listing, the sequences disclosed in the description are preferred. Alternatively, the sequences of the sequence listing may be used. EXPERIMENTAL SUPPORT EXAMPLE 1 - Identification of microbial phytate metabolism in the human gut and its relation with host health This Example shows that Misuokella jalaludinii or another bacterium comprising the identified phytate degradation pathway of Misuokella jalaludinii is able to convert phytate into the antimicrobial 3-hydroxypropionate. The Example also shows the synergy of M. jalaludinii with A. rhamnosivorans in phytate breakdown to beneficial SCFAs (i.e. propionate, acetate, succinate). This also supports that the beneficial effects of dietary phytate on host health may derive from the modulation of the microbiome. Methods Phytate degradation by fecal microbiome using stable isotope labeling. Fresh stools were collected from a healthy donor of whom informed consent was obtained following Good Clinical Practice. The inventors have complied with all relevant ethical regulations for work with human participants. Fresh stool samples from donor A were collected in falcon tubes and quickly brought to an anaerobic chamber to prepare fecal suspension for inoculation. 0.2 ml of fecal suspension was added into 10ml bicarbonate buffered medium containing either 10mM non-labelled phytate or [13Ce]phytate as sole energy and carbon source. [13Ce]phytate was synthesized and purified. Samples of [13Ce]phytate enrichments were taken at several time points during a first few days after inoculation. The supernatants of these samples were used for 13C-NMR analysis to monitor substrate consumption and end metabolite production. [13Ce]phytate was synthesized and purified. The first none-labeled phytate enrichments were subsequently transferred to a fresh medium with none labelled phytate as a sole substrate to further enrich for phytate-degrading microbes. At the 3rd transfer, phytate degradation capacity and metabolite production were assessed by HPLC analysis on the bacterial supernatant over 5 days while the pellets were harvested for gDNA extraction and followed by 16S rRNA sequencing analysis to determine changes of the microbial composition during phytate incubation. Stool of donor A was used to extract gDNA and inositol phosphates to further determine the microbial composition by 16S rRNA sequencing analysis and inositol phosphate profiles by 1D- and 2D-NMR analyses (see below for detailed protocol). ID- and 2D-NMR measurements. All chemicals were used without further purification unless specified. Deuterated solutions (deuterium oxide (D2O), sodium deuteroxide (NaOD) and deuterium chloride (DCI)) were obtained from Eurisotop, perchloric acid (HCIO4) from Supelco, potassium hydroxide (KOH) from Carl Roth, ammonia solution from Sigma Aldrich, tetramethyl phosphonium bromide (TMPBr) from Alfa Aesar, titanium oxide particles (Titanosphere 5 pm) from GL Sciences. For NMR measurements and NMR data analysis, TopSpin 3.5 was used. For formatting, the processed spectra were loaded into MestreNova 10.0 and exported into Adobe Illustrator where lines tracing accumulation of metabolites in stacked spectra were manually added. Measurements were conducted on a Bruker AV-HI spectrometer (Bruker Biospin, Rheinstetten, Germany) operating at 600 MHz for 1H and 151 MHz for 13C nuclei equipped with a cryo-QCI probe. The pulse sequence for BIRD-{1H,13C}HMQC is based on the hmqcbiph pulse program from Bruker. Measurement parameters are adapted depending on sample composition. Typically, HMQC measurements of lyophilized bacterial culture samples were recorded with TD(13C) = 512, 64 scans, spectral width (13C) limited to 50 - 90 ppm. HMQC measurements of cecal and plasma extracts were recorded with 128 scans, and P1 pulses determined for every single sample, and otherwise identical parameters. For the measurement of 13C-NMR spectra of bacterial culture samples TD = 131072, 2048 scans, and a spectral width of 220-20 ppm were used. All samples were recorded at 310 K. BIRD-{1H,13C}HMQC-NMR spectra were processed without digital water suppression with manual phasing and automatic baseline correction. 13C-NMR spectra were processed with SI = 16384, manual phasing and segment-wise automatic baseline correction. Quantification of NMR data were conducted as follows: For cecal extracts InsPs were quantified against a known concentration of tetramethylphosphonium bromide (TMPBr). A standard curve for lnsP6 against TMPBr was recorded earlier. For other InsP species, the standard curve for lnsP6 was used as an approximation as there are no fully 13C-labeled standards available. As the signals of the 2-positions are the sharpest and best resolved (due to the reduced coupling to the neighboring CH groups), the 2-position signals were used for quantification. For the analysis of metabolites produced in bacterial cultures, capped NMR tubes were roughly sterilized by rubbing with 70 % ethanol and radiation with UV light for 20 min in an aseptic laminar flow hood. Thawn aliquots of bacterial culture samples were centrifuged (5 min, 5000 g, 4 °C) and 500 pL of the supernatant were transferred under aseptic conditions into a sterilized NMR tube and 55 pL of D2O (from a previously unopened bottle which was kept under aseptic conditions) were added for locking during NMR measurements. Samples were kept at 4 °C until the measurement of 13C-NMR spectra on the same day. NMR samples which contained multiple InsP species according to the 13C-NMR were lyophilized, redissolved in D2O, and lyophilized again. Finally, the samples are taken up in 500 pL of D2O and pH adjusted to 6.0 with NaOD and DCI and submitted for recording HMQC and HMQC-CLIP-COSY spectra. Microbiome profiling analysis. DNA from using from 1ml bacterial culture of fecal phytate enrichments using a repeated bead-beating protocol. For the enrichments, 16S V3V4 amplicon sequences were parsed using a vsearch (v2.15.2) based pipeline. Paired end reads were merged, with max differences set to 100 and allowing for staggered overlap. ASVs were inferred from reads with lower than 1.5 expected error rate using the cluster unoise with centroids algorithm with a minsize of 4, after which chimeras were removed using the uchime3 denovo method. For each sample, ASV abundances were determined by mapping the merged reads against the ASV sequences with identical matches sequence set using the usearch_global algorithm with a 0.97 distance cut off. Taxonomy was assigned using R (V4.0.5) and the dada2 assign taxonomy function using the silva (v132) reference database. Human cohort study. The HELI US study is a population-based multi-ethnic prospective cohort study, based in Amsterdam, The Netherlands. Baseline data collection took place between 2011 and 2015 among the six largest ethnic groups in Amsterdam (those of Turkish, Moroccan, African Surinamese, South-Asian Surinamese Ghanaian and Dutch origin). People in these groups who were aged 18-70 were randomly, stratified by ethnicity, recruited from the municipal registry. Data collection consisted of a questionnaire and a physical examination including the collection of biological samples. Fecal samples were collected from participants. Microbiome data from the HELIUS study was processed. ASV variants with an average abundance of more than 0.1% were selected as representatives. Sequences were placed phylogenetically placed in the tree from the Living tree project (LTP_06_2022) using MAFFT (V7.310) and Fastree (V2.1.11). The tree was subset to all members of the Selenomonadales order. Ordination of the microbiome was performed by principal coordinate analysis of the Bray-Curtis dissimilarity. Enterotypes were defined by pam-clustering of the Jensen-Shannon Distance and were labelled by their major representative clade. Association of the ASVs with the different principal coordinates was determined by calculating the weighted average scores using wascores from the vegan (V2.6.4) package. Differences in prevalence were tested with a chi-square test. Data were visualized using ggplot2. The HELI US study complies with all relevant ethical regulations, is in accordance with the Declaration of Helsinki (6th, 7th revisions), and is approved by the Academic Medical Center (AMC) Medical Ethics Committee. All participants provided written informed consent. Isolation of prevalent Mitsuokella strain. Stool sample of donor A was suspended in anaerobic PBS buffer in an anaerobic tent to make a serial dilution of fecal slurry from 10'1 to 10'5. An amount of 200 pl of these dilutions were smeared on a screening agar medium containing phytate as a sole energy and carbon source. The screening medium was prepared by saturating 20mM phytate with magnesium chloride (SIGMA) to produce milky agar plates. The agar plates were subsequently incubated in an anaerobic jar filled with N2 / CO2 at 37°C up to 5 days. Colonies surrounded with clear zones as indication of phytate degradation activities were picked up and streaked on new agar medium to confirm the degradation activity. This streaking was repeated a several times before being inoculated in a liquid medium containing phytate as a sole energy and carbon source. The identity of the isolate was determined via 16S rRNA sequencing at Macrogen, and a draft genome of the Mitsuokella isolate was sequenced by Illumina NovaSeq 6000 S4 PE150 XP and assembled using Genome de novo assembly pipeline at Eurofins. Phylogeny of phytases. A phytase phylogenetic tree was constructed from amino acid sequences of phytases and phosphatases from all hosts ranging from mammals to bacterial species that were retrieved from the NCBI database. This included previously reported phytase and phosphatase amino acid sequences from all hosts, E. coli phytase, Akkermansia phytase and Mitsuokella phytase. All amino acid sequences were aligned using the Clustal_X programme. A phylogenetic tree was constructed using the neighbour-joining algorithm by the MEGA 7 with 1000 bootstraps to obtain confidence levels for the branches. Bacterial culturing. Mitsuokella jalaludinii DSM13811T was obtained from DSMZ culture collection and Anaerostipes rhamnosivorans 1y-2T was isolated previously and is available as DSM26241T. These two bacteria were routinely maintained in a modified YCFA medium supplemented with myo-inositol (SIGMA) for A. rhamnosivorans or phytate (SIGMA) for M. jalaludinii. The growth experiments were performed in duplicate in 20 ml bicarbonate-buffered medium supplemented with 20 mM phytate filled with N2 / CO2 (80:20, v / v) gas in the head phase. Phytate and inositol were filter sterilized as stock solutions of 0.2 M and 0.5 M. respectively. The condition in which the bacteria were added to 20 ml bicarbonate-buffered medium without substrate was used as control. The growth was monitored via metabolite formation by HPLC and optical density measurement by a spectrophotometer at a wavelength of 600 nm. Monoculture and coculture studies of phytate degradation. The coculture study was performed in a bicarbonate buffered medium supplemented with phytate as sole energy and carbon source. Monoculture of M. jalaludinii or coculture of M. jalaludinii and A. rhamnosivorans were inoculated with 10 mM phytate. Bacterial supernatants were collected from both conditions at several time points for substrate consumption and metabolite production by HPLC. To identify the intermediates of phytate degradation by the monoculture and the coculture, the bacteria were inoculated with 5 mM [13Ce] phytate and bacterial supernatants were collected during the growth for NMR measurements. M. jalaludinii DSM13811T and A. rhamnosivorans 1y-2T were pre-cultured in YCFA medium supplemented with 20 mM phytate or 20 mM myo-inositol respectively. These precultures were added with 2.5 % to the media of the test conditions. To investigate the synergy between M. jalaludinii and A. rhamnosivorans, the bacteria were grown in monoculture and coculture in a medium containing 10 mM, 20 mM and 40 mM phytate or 10 mM, 20 mM or 40 mM myo-inositol in 96 well plate incubated in an anaerobic tent for growth monitoring for 48 h. At the end of the growth, the bacterial supernatants were collected to analyze the substrate consumption and metabolite production. The experiment was performed in biological triplicate. To study the growth rate of M. jalaludinii in phytate and myo-inositol; the bacteria were inoculated in YCFA medium supplemented with either 10 mM or 40 mM phytate or 10 mM or 40 mM myo-inositol. The experiment was performed in 96 well plate which was incubated at 37 °C in a plate reader in the anaerobic chamber to monitor the OD600 every 30 min for 24 h. To study the capacity of A. rhamnosivorans to use 3-hydroxypropionate, the bacterium was incubated in a bicarbonate buffered medium containing 10mM 3-hydroxypropionate or 15mM glucose or both. The cultures were collected during 48 h for OD600 and end metabolite measurements. The experiment was performed in biological duplicate. To study the influence of 3-hydroxypropionate on the growth on myo-inositol, A. rhamnosivorans was grown in 20mM myo-inositol supplemented with either 0 mM, 10 mM, 20 mM, 30 mM, 40 mM, or 50 mM of 3-hydroxypropionate, and the growth was monitored by OD600 measurement every 30 minutes in a plate reader placed in an anaerobic tent. The experiment was performed in biological triplicate. Analytical methods Phytate, myo-inositol, succinate, 3-hydroxypropionate and other short-chain fatty acids and alcohols were quantified on a Shimadzu HPLC system equipped with a Shodex sugar SH1821 6 pm, 8.0 x 300 mm column. The column was kept at 45 °C while running with 0.005 M H2SO4 as eluent under a flow of 1 ml / min. The detector was a refractive index detector. Chemicals at HPLC quality were used to prepare the standard curves. All analyses were performed in duplicate. Transcriptomics. To identify genes involved in phytate degradation by M. jalaludinii DSM13811T, the bacterium was grown in two conditions including a bicarbonate buffered medium supplemented with 20 mM phytate or 20 mM myo-inositol. The experiments were performed in triplicate. The bacteria were harvested after 17 h incubation. Bacterial supernatants were collected to perform HPLC measurement for substrate consumption and metabolite production while the cell pellets were used for RNA extraction. Cells were harvested from 100 ml bacterial cultures by centrifugation at 4700 g for 30 min at 4 °C in 50 ml-pre-cooled sterile falcon tubes. Pellets were washed with 20 ml, 20 mM TE-buffer (pH 7) at 58 4700 g for 30 min at 4 °C and re-suspended in 150 pl TE buffer. Cell suspension was incubated with Lysozyme at 37 °C for 10 min. Cell lysis and RNase inactivation was performed by addition of a mix containing 4 pl p-mercaptoethanol, 1 pl proteinase-K and 150 pl of Gram-positive lysis solution (Gram positive DNA extraction kit, Masterpure). Lysis was done at 65 °C for 15 min while vortexing every 5 min. After incubation, the mix was quickly cooled on ice for 5 min and proteins were precipitated by adding 175 pL of MPC protein precipitation reagent (Gram positive DNA extraction kit, Masterpure). Debris was removed via centrifugation at 4 °C 10 000 g. The sample was further cleaned and purified via the automated Maxwell LEV simply RNA extraction kit (Promega, Madison, USA), according to manufacturer’s instructions. Quality and quantity of the RNA extracts were checked by spectrophotometer DS-11 FX (DeNovix), according to manufacturer’s instructions. RNA was collected in RNase free water and stored at -80 °C till further analysis. Depletion of rRNA and sequencing was performed by Novogene (Hong Kong, China) using Illumina high throughput sequencing platform. To investigate the interaction between M. jalaludinii DSM13811Tand A. rhamnosivorans in phytate at molecular levels, M. jalaludinii and A. rhamnosivorans were grown either together or alone in a bicarbonate buffer medium supplemented with 20 mM phytate or 20 mM inositol. The experiments were performed in triplicate. The bacteria were harvested after 17 h incubation. 1 mL bacterial supernatants were collected to perform HPLC measurement for substrate consumption and metabolite production while the cell pellets were used for quantification of M. jalaludinii and A. rhamnosivorans. qPCR primers for M. jalaludinii were designed to quantify M. jalaludinii in the cocultures and murine microbiome using Primer3 and Blast based on 16S rRNA sequence of M. jalaludinii DSM13811T. The primers were validated using gDNA of M. jalaludinii, which resulted in an 83 bp amplicon. The 16S rRNA gene of M. jalaludinii was used to optimize temperature and make standard curves. The qPCR programme was 95 °C for 5 min and 35 cycles consisting of 95 °C for 30 s, 60 °C for 10 s and 72 °C for 40 s; 95 °C for 1 min and 60 °C for 1 min. DNA copies were calculated based on standard curves. qPCR primers for A. rhamnosivorans were used as previously designed and validated. 100 ml bacterial cultures were used for RNA extraction and sequencing as described above. Obtained reads were aligned against reference genomes (BioProject PRJNA223472) of M. jalaludinii and A. rhamnosivorans using bowtie2 (V2.5.1). Gene counts were gathered in R (V4.0.5) using feature counts function of the R subread package (V4.3). Differential expression analysis was performed using DESeq2 (V 1.38.3). For analysis were re-annotated using an available genome from GenBank (BioProject PRJNA223472) and re-annotating the genome in Rapid Annotation using Subsystem Technology (RAST). Animal studies using a stable isotope approach. All animal experiments were done in male C57BI / 6J mice (Charles River), which were housed in individually ventilated cages with 59 2 mice per cage. Mice were kept under constant temperature (19-21 °C); humidity of 40-70 % and a 12h light / dark cycle with free access to food and water. All animal experiments were conducted according to guidelines of the ‘Guide to the Care and Use of Experimental Animals’ approved by the Ethics Committee on Animal Care and Use in Academisch Medisch Centrum, The Netherlands. The inventors have complied with all relevant ethical regulations for animal testing and research. A stable-isotope approach was employed to study in vivo conversion of phytate by Mitsuokella jalaludinii (MJ) and Anaerostipes rhamnosivorans (AR). Mice were received at the age of 4 weeks and randomized and divided in 2 mice per cage. Acclimatization time was 2 weeks. To reduce the interference of endogenous murine microbiome, mice were treated with antibiotic cocktail of 1 mg ml-1 ampicillin, 5 mg ml-1 streptomycin and 1 mg ml-1 colistin via oral gavage one time in 1 week prior to the intervention as described previously. To test the in vivo degradation of phytate MJ and AR, 0.2 ml oral administration of 0.1 mg / g body weight phytate or 0.1 mg / g body weight phytate and 109 CFU of MJ or 0.1 mg / g body weight phytate and 109 CFU of MJ and 109 CFU of AR were given to a group of 8 mice every second day for 2 weeks. Bacterial suspension was prepared in 10 % trehalose. In week 3, [13Ce]phytate-AR-MJ, [13Ce]phytate-MJ or [13Ce]phytate challenge were given to a group of 8 mice in corresponding group. To estimate the time preference of in vivo conversion of [13Ce]phytate, a vial of bacterial suspension of MJ and AR was inoculated in a medium supplemented with 5 mM phytate. Phytate conversion by the bacteria was monitored during 24 h via metabolite measurement by HPLC. The experiment was performed in biological duplicate. Each 4 mice per group were sacrificed after 3 h or 6 h of the 13C challenge and cecum contents and blood were collected for targeted metabolomics analyses via NMR, CE-MS, GC-MS and UHPLC-MS / MS measurements. Detailed methods were described in following sections. Colon samples were collected for quantification of A. rhamnosivorans and M. jalaludinii by qPCR at 3 h and 6 h time points as described above. Extraction of InsPs from mouse cecal and plasma samples for metabolomics. The protocol for the extraction of InsPs from cecal samples was adapted from published procedures but scaled to match the higher mass and volume (between 20-120 mg). The cecum content is resuspended in ice-cold 1 M aq. perchloric acid (HCIO4, Supelco, 0.1 mL per 1 mg cecum content) in a 5 mL or 15 mL tube by pipetting up and down (using a 1 mL pipette tip with the tip slightly cut off to widen the opening) and vortexing for about 20 s until all major clumps have broken up. The suspension was then incubated for 20 min at 4 °C on a rotary shaker. The sample is then centrifuged (10 min, 21 000 g, 4 °C) in 2 mL tubes and the supernatant transferred into a separate 5 mL or 15 mL tube containing TiO2 beads (Titanosphere 5 pm, GL Sciences, 0.5 mg of TiO2 per 1 mg original cecum content material), which were already washed with 1 mL Milli-Q® water and 1 mL 1 M perchloric acid. The extract and TiO2 beads were mixed by briefly vortexing and on a rotary shaker for 20 min at 4 °C. After centrifugation (10 min, 18 000 g, 4 °C) in fresh 2 mL tubes the supernatant was discarded (note: for transferring the supernatant without disturbing the TiO2 beads a 2 pL Eppendorf tip attached to the tip of a 1 mL tip was used with slow pipetting) and the beads united in a single 1.5 mL tube by resuspending in 1 mL HCIO4 in total. After vortexing the suspension was again centrifuged (10 min, 18 000 g, 4 °C) and the supernatant discarded. To eluate InsPs from the TiO2 beads, the beads were incubated with 375 pL of 10 % ammonia solution for 5 min at room temperature on a rotary shaker. After centrifugation (IKA miniG, 6000 rpm, 1 min) the supernatant was collected in a separate tube. The elution step is repeated once more and the eluates are combined. The combined eluates are filtered through a 0.2 pm syringe filter (Sartorius Minisart RC4) which was subsequently rinsed with 150 pL of Milli-Q® water. The filtrate was collected in a new 1.5 mL tube and lyophilized. To reduce the water content for NMR analysis the lyophilized eluates were redissolved in 500 pL D2O and lyophilized again. The lyophilized samples were taken up in 500 pL D2O and defined volumes of NaOD and DCI were used to adjust the pH to 7.0. Afterwards, 2.86 pL of a TMPBr stock solution (20 mM in D2O) were added for quantification and submitted for NMR measurement. The extractions of InsPs from plasma samples were performed based on the procedures of TiO2 purification method. Briefly, 60-100 pL of plasma was thawed on ice and an equal amount of perchloric aid (2 M, 4 °C) was added. The sample was rotated for 30 min at 4 °C and then centrifuged (15.000 g, 10 min, 4 °C). Transfer the supernatant to pre-washed TiO2 beads (5 mg per sample, 5020-75000 GL Sciences) and incubate at 4 °C with rotation for 20 minutes. After that, the suspension was centrifuged (3.500 g, 1 min, 4 °C) and the supernatant was discarded. Wash the unbinding compounds with 0.5 mL perchloric acid (1 M) twice. For elution, NH4OH (200 pL, 3 % [v / v]) was used. The elution step was repeated and the eluents were combined. The combined eluents were centrifuged (17.000 g, 1 min, 4°C) to remove any insoluble residues. For subsequent CE-ESI-MS analysis, the supernatant was completely dried under vacuum evaporation (60 °C) and dissolved into 20 pL of ultrapure water before measurement. Extraction of myo-inositol from plasma samples for metabolomics. The extractions of inositol from plasma samples were performed. Briefly, plasma samples were thawed and vortexed before transferring 50 pL of sample to 250 pL of acetonitrile containing 1 % of formic acid for protein precipitation. After centrifuging, the supernatants were transferred into a HPLC vial for the UHPLC-MS analysis. CE-ESI-QQQ analysis of^Ce] InsPs in plasma samples. Known amounts of isotopic standards (2 pM [18O2] 5-lnsP?) were spiked into samples for quantitation of [13Ce] PP-lnsPs and [180i2] lnsP6 (2 pM) were spiked into samples for quantitation of [13Ce] InsPs. For plasma samples, 2 pM [18O2] 5-lnsP? and 2 pM [180i2] InsPe were spiked. For cecum samples, the samples were diluted 20-fold, then 4 pM [18O2] 5-lnsP7 and 20 pM [180i2] InsPe were spiked. A CE-ESI-QQQ system is used for the measurement. Set MS source parameters and MRM transitions as shown in table. The injection for each sample is 30 nL. MS Source Parameters Gas Temperature 150 °C Gas Flow 11 L / min Nebulizer 8 psi Sheath Gas Temperature 175 °C Sheath Gas Flow 8 L / min Capillary Voltage -2000 V Nozzle Voltage 2000 V High Pressure RF (Ion Funnel Parameters) 70 V Low Pressure RF (Ion Funnel Parameters) 40 V MRM transitions Molecular name Precurs or Ion Produ ct Ion dwell Fragmentor (V) Collision Energy (V) Cell Accelerate r Voltage Polarity [13C6] lnsP2 345 247 50 166 21 4 Negativ [13C6] lnsP3 424.9 326.8 50 166 17 4 e Negativ [13C6] lnsP4 252 424.9 50 166 5 1 e Negativ [13C6] lnsP5 292 504.9 50 166 9 3 e Negativ [13C6] lnsP6 331.9 486.9 50 166 13 4 e Negativ [,8O12] 340.9 494.9 50 166 17 4 e Negativ InsPe [13C6] lnsP7 371.9 322.9 50 166 9 3 e Negativ [18O2] lnsP7 370.9 319.9 50 166 9 3 e Negativ e [13C6] lnsP8 411.9     362.8   50    166          9          1            Negativ e 13C-Myo-lnositol measurement in plasma samples. Plasma [13C8]myo inositol was quantified using UHPLC-MS / MS. Analysis was performed on a LIHPLC (Agilent 1290 infinity II) coupled to a Q-TOF (Agilent 6546). Chromatographic separation was achieved using gradient elution on an LIHPLC Acquity BEH Amide column (1.7 pm, 2.1 mm x 150 mm) at 30 °C at a flow rate of 0.4 ml / min. Mobile phase consisted of 0.04 % NH4OH (mobile phase A) and 100 % acetonitrile (mobile phase B). Setting of instrument parameters and gradient elution as shown in table. The elution started with 13 % mobile phase A, increased to 17 % mobile phase A between 0 min and 16 min then to 19 % mobile phase A between 16 min to 19 min. Between 19 min to 21 min, mobile phase A was increased to 30 % then held for 2 min. Stock solution of myo-inositol (2 mg / mL) was prepared in ultrapure water, then was diluted in 87 % acetonitrile (starting mobile phase condition for analysis) to obtain five calibration levels (0.1 pg / mL, 0.5 pg / mL, 1 pg / mL, 5 pg / mL, 10 pg / mL) for quantification of myo-inositol in plasma. Each calibration levels have three replicates. Cecum SCFA measurement. SCFA concentration and 13C-enrichment in cecal sample were analyzed. Briefly, samples were thawed, diluted in 500 pL PBS and spiked with 50 pL of (0.5 mg / mL) 2-ethyl butyric acid as internal standard. After adding 10 pL of HCI (12M), samples were homogenized, and centrifuged (20 min, 15000 x g, 4 °C). The supernatant was transferred to a glass vial with a spatula tip of solid NaCI. SCFAs were extracted in 2 mL diethylether. For SCFA derivatization, an amount of 500 pL of diethyl ether was derivatized with 50 pL N-tert-butyldimethylsilyl-N-methyltrifluoroacetamide (MTBSTFA) at room temperature overnight. Mass spectrometry analysis was performed using an Agilent 5975C series gas chromatography / mass spectrometry (GC-MS) (Agilent Technologies, Santa Clara, USA) equipped with a ZB-1 column (Phenomenex, Torrance, USA). The mass isotopologue spectra of ([M-57]+) fragment of the derivatives of acetate (m / z 117-1119, mo-m2), propionate (m / z 131-134, mo-ms) and butyrate (m / z 173-149, mo-mu) were monitored. The standard curve were prepared in a range of 10 pM to 10 mM for acetate, 3 pM to 3 mM for propionate and butyrate. These ranges covered all measured points. Caco-2 cell testing. To investigate the effects of microbial metabolites on barrier integrity, TEER (Transepithelial electrical resistance) experiments in Caco-2 cells were performed. As propionate is the major metabolite from phytate break-down by the coculture, effect of propionate on barrier integrity was accessed in Caco-2 cell with transwell setting. To produce bacterial supernatants for Caco-2 cell work, a coculture of M. jalaludinii and A. rhamnosivorans was grown in YCFA containing 20mM phytate. The pH of the cultures was monitored every day and adjusted to neutral pH after addition of substrates. The pH adjustment and substrate addition were conducted every day for 5 days. Bacterial supernatants were collected at all time points for HPLC measurement. At 80 % of confluence of the Caco-2 cell culture, cells were treated with Trypsin-EDTA and seeded apically at 5x104 cells / well onto a 20-well, 12 mm ThinCert™ with 0.4 pm pore membrane, TC-treated (Coming, CLS3460). Growth media were renewed every 2 days with DMEM containing 10 % fetal bovine serum (FBS), 1 % Penicillin-Streptomycin and 1 % of non-essential amino acids. Caco-2 cells were incubated in an incubator maintained in a humidified atmosphere at 37 °C with 5 % CO2. Caco-2 cells were seeded on transwells for 21 days to obtain a monolayer for TEER measurement. TEER analyses were performed at day 7, 14, and 21 in culture. After 21 days, the medium in the apical compartment was replaced with medium containing either 20mM propionate; 10 % M. jalaludinii and A. rhamnosivorans supernatant or 10 % YCFA medium as control. TEER measurement was performed at TO; 4 h; 7 h; 24 h and 30 h. Cells with fresh medium was used as control condition. At the end of the experiment, the supernatant in the apical compartment was collected for HPLC analysis while Caco-2 cells were washed with 300 pL of PBS and collected in 300 pL of Trizol / Tripure®. These cells were then stored at -80°C freezer for RNA extraction and qPCR to quantify the activity of tight junction genes. The experiment was performed in biological triplicate. In order to assess the influence of propionate and bacterial metabolites on barrier integrity, total RNA was extracted from cells incubated with either water or 20 mM propionate, 10 % bacterial supernatant of the coculture of M. jalaludinii and A. rhamnosivorans, 10% bacterial medium using TriPure reagent according to manufacturer’s instruction. Quality and concentration of extracted RNA were determined by Nanodrop. The cDNA was amplified using SensiFAST SYBR Green PCR Kit (Meridian bioscience, USA), following the manufacturer’s instructions. Human tight junction genes (Claudin 1, Occludin, E-cadherin, Claudin 2 and ZO1) were amplified using specific primers, with expression being normalized to 18S and 36B4 genes. The qPCR programme was 10 minutes at 95°C, 39 cycles consisting of 15 seconds at 95 °C and 30 seconds at 60 °C and melting curves were obtained at between 65 °C to 95 °C with an increment of 0.5 °C every 5 seconds. Fold changes were calculated using 2'ACq. The qPCR was performed with technical duplicates. RESULTS Fecal phytate metabolism identifies human Mitsuokella spp. as efficient phytate degraders. To gain a better understanding which bacteria are involved in the rapid degradation of phytate, the inventors incubated fresh fecal samples from a healthy donor (A) in a medium supplemented with [13Ce]phytate as the sole carbon and energy source. The supernatants from [13Ce]phytate enrichments were collected over time and used for the analysis of 13C-labelled components by 13C-NMR. In parallel, non-labelled phytate fecal enrichments were repeatedly transferred to fresh phytate media to further enrich for phytate degrading microbes. The inventors observed that the fecal microbiome metabolized [13Ce]phytate within a few hours to [13C2]acetate and [13C3]3-hydroxypropionate, which was subsequently converted to [13C3]propionate after 24h (Fig. 1a). To identify the phytate-degrading microbes, genomic DNA was isolated from phytate enrichments after two transfers during which bacteria involved in phytate metabolism were highly enriched and subjected to 16S rRNA gene amplicon sequencing. The inventors observed a microbial community enriched from fecal microbiomes with Ruminococcaceae, Mitsuokella and Butyricicoccus as the most abundant taxa (Fig. 1 b). At the end of the phytate incubation, the relative abundance of most species decreased, whereas that of Mitsuokella spp. increased in both enrichments up to 10 % of total microbiome, with M. jalaludinii as the most dominant species (Fig. 1b-c). Of note, the relative abundance of Mitsuokella increased gradually during the first 48 h, which was in line with a rapid degradation of phytate within 30 h (Fig. 1c). Overall, these results suggest that M. jalaludinii is involved in phytate degradation in the human gut. Mitsuokella as prevalent taxon in the human Gi tract and its health relation. To further investigate the prevalence of Mitsuokella in the general population and determine its ecological niche, the inventors analyzed the microbiome of 6039 Amsterdam-located subjects in HELIUS cohort with different ethnicities. The inventors found three amplicon sequence variants (ASV) of Mitsuokella which represented 89 % of all Mitsuokella counts. These sequence variants were highly similar to those belonging to Mitsuokella multacida or Mitsuokella jalaludinii. A total of 1542 out of 6039 subjects were positive for one of these clades, indicating the high prevalence of Mitsuokella in the general population. All three clades had bimodal distributions with either absence or presence of which relative abundance were between 0.01 to 10 %. Mitsuokella is closely related to known fiber-degrading species, including ruminal Selenomonas spp., one of which has been reported to have an active periplasmic phytase. Mitsuokella spp. were also strongly associated with the Prevotella Enterotype, which has been linked with high fiber intake and health status. The prevalence of different clades of Mitsuokella spp. varied slightly among the ethnicities but most subjects harbored M. jalaludinii. To verify its functionality, the inventors isolated a dominant Mitsuokella strain from donor A and found it to grow fast on phytate and its genome sequence to be highly similar (an average nucleotide identity of 97.3 %) to that of the type-strain M. jalaludinii DSM13811T with greatly identical phytate degradation pathway genes. Hence, this confirms that M. jalaludinii is highly prevalent in human. Of note, M. jalaludinii remained as the most prevalent Mitsuokella species in both genders with higher prevalence in male. It was recently reported that the abundance of fecal Mitsuokella spp. was significantly lower in 65 cardiometabolic patients compared to the healthy population. This prompted the inventors to further study the role of M. jalaludinii in phytate degradation and its contribution to metabolic health. Complete phytate degradation pathway by Mitsuokella jalaludinii DSM13811T characterized via stable isotope and transcriptomic analyses. The inventors used M. jalaludinii DSM13811Tfor proof-of-concept experiments and cultured it in a medium containing phytate or myo-inositol as the sole energy and carbon source. M. jalaludinii grew rapidly in phytate with a doubling time of 3.4 h, while the doubling time with myo-inositol was 7 h (Fig. 2a). The metabolite production was similar between both conditions. Based on the observed stoichiometry of phytate conversion, the inventors propose the net theoretical fermentative equation as: 1 phytate + 6 H2O —> 1 3-hydroxypropionate + 0.4 lactate + 0.2 succinate + 0.2 acetate + 0.6 CO2 + 6 phosphate. Of note, the formation of CO2 was not determined due to the pre-existing bicarbonate in the medium but predicted based on carbon and redox recovery. To unambiguously identify the pathway, its intermediates and all end metabolites of phytate degradation, M. jalaludinii was grown in bicarbonate buffered medium containing either [13Ce]phytate or [13C6]myo-inositol as the sole energy and carbon source. As observed by 1D-NMR and 2D-NMR spectroscopy, M. jalaludinii converted [13Ce]phytate rapidly to various metabolites with [13C3]3-hydroxypropionate, [13C3]lactate and [13C4]succinate as major end metabolites (Fig. 2b). The inventors identified the accumulation of myo-inositol-2-monophosphate (lns(2)P) and myo-inositol during the first 7.5 h via 2D-NMR (Fig. 2c), suggesting that these are intermediates of phytate degradation. The capacity to use myo-inositol was confirmed by the growth of M. jalaludinii and conversion of [13C6]myo-inositol to [13C3]3-hydroxypropionate, [13C3]lactate and [13C4]succinate. The production of 3-hydroxypropionate from phytate assured our previous hypothesis that Mitsuokella spp. were responsible for the efficient fecal phytate degradation in which 3-hydroxypropionate was detected as intermediate (Fig. 1a). To further identify genes of M. jalaludinii involved in phytate metabolism, the inventors analyzed transcriptomic profiles of cells grown in either phytate or myo-inositol. The differential expression of the whole transcriptome between two conditions is shown in a volcano plot in which phytate metabolic genes are highlighted. The inventors found the gene for a periplasmic phytase (MJ_0021) constitutively expressed in both conditions (Fig. 2d). Evolutionary analysis showed that the encoded phytase was only distantly related to other microbial and human phytases, which may imply its unique capacity to readily dephosphorylate phytate to inositol (Fig. 2b-c). The expression of the genes for an inositol transporter (MJ_0380) and a high affinity phosphate transport system PstSCAB (MJ_0656-0658) were 8-fold increased during the growth on phytate as well as the electron 66 transport chain by a succinate dehydrogenase membrane complex (MJ_0311-0313) and ATP synthase (MJ_0861-0869). The inventors also identified induced expression of 2-hydroxy-3-oxopropionate reductase (MJ_1291) and a 3-hydroxypropionate permease (MJ_0911) involved in 3-hydoxypropionate production and transport, respectively. Genes involved in acetate, lactate and succinate, 3-hydroxypropionate production, glycolysis and ATP synthase were identified, all of which except a pyruvate carboxylase were expressed constitutively (Fig. 2d). The metabolomic and transcriptomic analyses imply that the faster growth of M. jalaludinii on phytate as compared to myo-inositol may likely be due to the increased activity of the inositol transporter. Based on the NMR and transcriptomic analyses, the entire metabolic phytate degradation pathway was reconstructed. The observation that a monoculture of M. jalaludinii mainly produced succinate and 3-hydroxypropionate and not the canonical short chain fatty acids from phytate, suggests that there are metabolic interactions between Mitsuokella with other commensal bacteria in the human colon. Mechanistic understanding of in vitro synergy between M. jalaludinii and A. rhamnosivorans in phytate. It has been shown that supplementation of A. rhamnosivorans in fecal phytate enrichment increased propionate formation. Hence, the inventors investigated the potential synergy between M. jalaludinii and A. rhamnosivorans in phytate degradation. The inventors observed that the cocultures reached higher cell density compared to monocultures of M. jalaludinii independent on phytate concentration (Fig. 6a). The inventors detected propionate and acetate in the cocultures while 3-hydroxypropionate and lactate were only accumulating in the M. jalaludinii monoculture with presence of succinate in both conditions (Fig. 6b). This indicates a potential synergy between these two bacteria leading to propionate production upon phytate degradation. To gain mechanistic insight into this interaction, the inventors monitored and compared phytate metabolism by monoculture of M. jalaludinii versus coculture of M. jalaludinii and A. rhamnosivorans using both non-labelled and 13Ce-isotopomer of phytate. The inventors observed that 3-hydroxypropionate was first produced and subsequently converted to propionate after 8 h in the coculture (Fig. 3b-c), while 3-hydroxypropionate accumulated in the monoculture of M. jalajudinnii (Fig. 3a), suggesting a trophic chain involving 3-hydroxypropionate as an intermediate. Interesting, the inventors found that A. rhamnosivorans was indeed able to convert 3-hydroxypropionate to propionate particularly in presence of glucose as carbon source, indicating a co-metabolic conversion (Fig. 7a-c). Of note, glucose consumption was reduced in the presence of 3-hydroxypropionate, suggesting inhibition of the glucose metabolism. This was further supported by a slower growth of A. rhamnosivorans on myoinositol in the presence of increased 3-hydroxypropionate levels (Fig. 7d). This 3-hydroxypropionate-mediated inhibition of A. rhamnosivorans metabolism may be so potent that most released inositol from phytate dephosphorylation might be taken up and used by M. jalaludinii. These results imply that the synergy between the two intestinal bacteria was mainly via 3-hydropropionate interspecies transfer. Furthermore, 13C-NMR analysis confirmed 13C-labelled propionate, succinate and acetate as end metabolites from [13Ce]phytate in the coculture (Fig. 3c), with [13Ce]lns(2)P and [13C6]lnositol as intermediates. The commonalities between the monocultures and cocultures indicates the limited influence of A rhamnosivorans on phytate dephosphorylation by M. jalaludinii (Fig. 3c). To further investigate the microbial interaction at the molecular level, the inventors assessed the differential expression of phytate degradation pathway genes of M. jalaludinii and myo-inositol degradation pathway genes of A. rhamnosivorans during growth in monocultures compared with cocultures on phytate and myo-inositol using transcriptomic analyses. The results of the metabolic time-course measurements showed high concentrations of 3-hydroxypropionate only in monocultures of M. jalaludinii at the expense of high propionate concentration in the cocultures in both phytate and myo-inositol (Fig. 8a-b). The inventors found that the number of cells of the two bacteria were similar when grown on phytate while the cell numbers of A. rhamnosivorans were 3-fold higher than that of M. jalaludinii with myo-inositol as a carbon source (Fig. 8c-d). A. rhamnosivorans had small effects on the overall transcription profiles of M. jalaludinii grown in phytate in contrast to strong influence on M. jalaludinii transcriptomic profile grown in myo-inositol (Fig. 8e). For M. jalaludinii, the expression of genes involved in phytate dephosphorylation, inositol uptake, inositol fermentation was highly similar between monoculture and coculture in phytate (Fig. 3d) while genes involved in myo-inositol uptake and utilization and 3-hydroxypropionate export (MJ_911) were up to 70-fold decreased in the coculture grown on myo-inositol, indicating reduced uptake and consumption of myo-inositol by M. jalaludinii due to the presence of A. rhamnosivorans. Comparing the whole transcriptome profiles of A. rhamnosivorans between cocultures and monocultures, the inventors identified an entire operon (AR1Y2_1112-1117) involved in 3-hydroxypropionate transport (AR1Y2_1114) and conversion to propionate, which was increased up to 19-fold in coculture versus monocultures (Fig. 3e). This observation confirms the active conversion of 3-hydroxypropionate to propionate by A. rhamnosivorans in coculture, which is in line with the metabolic prediction. In contrast, the expression in A. rhamnosivorans of the inositol uptake gene (AR1Y2_0316) and the inositol utilizing operon (AR1Y2_1104-1107) were decreased around 15-fold in the cocultures, suggesting the reduced use of myo-inositol in the presence of M. jalaludinii. Based on these results, the inventors reconstructed a model of metabolic interaction between M. jalaludinii and A. rhamnosivorans for phytate utilization (Fig. 3f and Fig. 9). Elucidation of in vivo phytate conversion by M. jalaludinii and A. rhamnosivorans. To interrogate the in vivo synergy between these two species in a mouse model, the inventors administered non-labeled phytate with either no microbes, M. jalaludinii alone or M. jalaludinii together with A. rhamnosivorans for two weeks before [13Ce]phytate oral challenge (Fig. 4a). The inventors quantified 13C-inositol phosphates by NMR and CE-MS analyses in mouse cecum and plasma as well as the bacteria in mouse colon after 3 h and 6 h oral gavage. The inventors observed that the [13Ce]phytate level was significantly lower after 3 h and 6 h oral challenge in groups receiving bacteria (Fig. 4b-c), indicating the active conversion of phytate by M. jalaludinii or M. jalaludinii plus A. rhamnosivorans in the murine digestive tract. Mice that received the bacteria (both M. jalaludinii with and without A. rhamnosivorans) had less than 0.5 nmol of [13Ce]phytate per mg cecal content as opposed to 4 nmol of [13Ce]lnsP6 per mg cecal content from mice that did not receive the bacteria after 3 h oral challenge. This is reflected by high levels of M. jalaludinii in mouse colon samples of bacterial treatment groups compared with the phytate-only group (Fig. 4d). Similarly, the level of A. rhamnosivorans was high in mouse colon samples after treatment while completely absent in M. jalaludinii treatment and only phytate groups (Fig. 4e). The difference of [13Ce]lnsP6 level between the treatment groups and the control group was smaller at 6h after of oral challenge, suggesting the residual mouse microbiome was capable of degrading InsPe but at a slower rate as compared to those with supplemented with M. jalaludinii (Fig. 4c). Importantly, no [13Ce]lnsPs and [13C6]-myo-inositol were detected in the mouse plasma at both 3 h and 6 h time points by CE-MS, indicating the microbiome was mainly responsible for dietary phytate consumption. Remarkably, the inventors detected large enrichment of 13C-propionate but not 13C-acetate or minor 13C-butyrate in mouse cecal samples, indicating the major production of propionate from oral phytate (Fig. 10). However, no significant difference in propionate accumulation was observed between the treatment groups and the control group which reflected the reported rapid absorption of short chain fatty acids by colonocytes. While [13Ce]lnsP6 was the most abundant inositol phosphate component in the mouse cecum, smaller amounts (<0.25nmol / mg cecum) of other inositol phosphates (lnsPs[3OH], lns(1,2,5,6)P4 and / or its enantiomer lns(2,3,4,5)P4 and lnsPs[5OH]) were also detected in the cecum samples of the mice (Fig. 4f-h). Of note, lnsPs[5OH] level was significantly lower in bacterial treatment groups (Fig. 4h) whereas lnsP4 and lnsPs[3OH] levels were higher in two treatment groups compared to the control group (Fig. 4f-g), implicating multiple phytate degradation pathways in presence and absence of these two administered bacteria. Based on these data, two main microbial phytate degradation routes in mouse cecum were deduced as summarized in Fig. 4i. Microbial phytate derived metabolites improved barrier integrity via activating tight junction genes in Caco-2 cell model. To further investigate potential health benefits of microbial phytate degradation by M. jalaludinii and A. rhamnosivorans, the inventors examined effects of the SCFA propionate as a major end metabolite from phytate degradation on barrier integrity using a Caco-2 cell model. The inventors incubated 20 mM propionate in 69 3-week seeded Caco-2 cells on transwell and measured the barrier integrity by transepithelial electrical resistance (TEER) analysis over the course of 30 h and quantified the expression of genes involved in tight junction by qPCR. The inventors observed a significant increase of TEER upon propionate incubation as compared to control (Fig. 5a). The inventors found that tight junction genes Claudin-1, Claudin-2 and E-cadherin were upregulated in propionate condition which is in line with the TEER measurement (Fig. 5b). To produce the bacterial supernatant that contains similar amounts of propionate for Caco-2 cell test, the inventors added phytate to a coculture of M. jalajudinii and A. rhamnosivorans and adjusted pH back to neutral in the end of fermentation of each addition (Fig. 11). The inventors observed that 10 % supplementation of the bacterial supernatant to the apical compartment improved epithelial barrier integrity (Fig. 5c) and increased activities of tight junction genes Claudin-1 and E-cadherin (Fig. 5d). All in all, these data suggest that metabolites derived from phytate breakdown by M. jalaludinii and A. rhamnosivorans, mainly consisting of propionate, improved the barrier integrity via activating tight junction genes. EXAMPLE 2 - Dietary supplementation Beneficial effect. The supplementation of a subject with a bacterium according to the present disclosure, e.g. Mitsuokella jalaludinii and optionally Anaerostipes rhamnosivorans provides a direct or synergistic effect on improved insulin resistance, presumably via additional propionate production. Treatment. Patients are treated as indicated below, according to the following 4 treatment arms: Treatment 1: 6 weeks, twice daily empty supplement. Treatment 2: 6 weeks, twice daily supplement with 108 living cells of a bacterium according to the present disclosure, i.e. Mitsuokella jalaludinii. Treatment 3: 6 weeks, twice daily supplement with 108 living cells of a bacterium according to the present disclosure, i.e. Mitsuokella jalaludinii and Anaerostipes rhamnosivorans. Treatment 3: 6 weeks, twice daily supplement with 108 living cells of a bacterium according to the present disclosure, i.e. Mitsuokella jalaludinii and Anaerostipes rhamnosivorans in combination with 25 gram nuts. No. of patients Condition Effect treatment 1 (patient 1) Effect treatment 2 (patient 2) Effect treatment 3 (patient 3) Effect treatment 4 (patient 4) 4 Insulin resistance No effect Reduction of Insulin Reduction of Insulin Reduction of Insulin resistance with 10%* resistance with 12.5%* resistance with 14.5%* * as determined by hyperinsulinemic euglycemic clamp, HOMA(-IR). It is expected that results similar to the putative effects as shown in the table above can be obtained with larger patient cohorts. EXAMPLE 3 - Use of other host bacteria (1) Another host bacterium, Escherichia coli is transformed according to standard methods with a gene set according to the present invention and comprising (PTP-like) phytase, major myo-inositol transporter lolT, myo-inositol 2-dehydrogenase, inosose dehydratase, 3D-(3,5 / 4)-trihydroxycyclohexane-1,2-dione hydrolase, 5-deoxy-glucuronate isomerase, 5-keto-2-deoxygluconokinase, 5-keto-2-deoxy-D-gluconate-6 phosphate aldolase, 2-hydroxy-3-oxopropionate reductase, and D-beta-hydroxypropionate permease. Preparation of Competent Cells. A single colony of E. coli is transferred into 5 mL of LB broth and incubated overnight at 37°C with shaking. Then, 50 mL of fresh LB broth is inoculated with 1 mL of the overnight culture. The culture is incubated at 37°C with shaking until it reaches an optical density at 600 nm (OD600) of 0.4-0.6. The culture is then transferred to a pre-chilled centrifuge tube and centrifuged at 4°C for 10 minutes at 3000 x g. The supernatant is discarded and the cell pellet is resuspended in 20 mL of ice-cold molecular biology-grade water. The, the cell pellet is centrifuged again and resuspended in 2.5 mL of ice-cold 10% glycerol, and transferred to small tubes. Transformation. 1-5 pL of each plasmid DNA (containing the target genes) is transferred to 50 pL of competent cells on ice, and gently mixed, and then incubated on ice for 30 minutes. The mixture is then transferred to a pre-chilled electroporation cuvette. The cells are electroporated using appropriate settings for E. coli. Immediately, 1 mL of SOC medium is added to the electroporated cells and the mixture is transferred to a sterile tube. The cells are incubated at 37°C with shaking for 1-2 hours. Plating. The transformed cells are plated onto LB agar plates containing the appropriate antibiotics for selection of successfully transformed cells. The plates are incubated at 37°C overnight. Analysis. The presence of the target genes is verified by PCR or DNA sequencing, and protein expression is confirmed by performing enzyme assays or Western blotting. It is found that the host bacterium is capable of converting phytate to 3-hydroxypropionate under anaerobic conditions (UHPLC-MS / MS as disclosed herein). EXAMPLE 4 - Use of other host bacteria (2) Additionally, Escherichia coli is transformed according to methods as described in Example 3 with a gene set according to the present invention and comprising permease, oxoacid CoA transferase, dehydratase, electron transfer flavoprotein, beta subunit, Electron transfer flavoprotein, alpha subunit, Acyl dehydrogenase, and oxoacid CoA transferase 5 It is found that the host bacterium is capable of converting 3-hydroxypropionate to propionate under anaerobic conditions.

Claims

1. Bacterium comprising a gene set that allows said bacterium to convert phytate to 3-hydroxypropionate or a salt or ester thereof, for use in preventing and / or treating metabolic syndrome, insulin resistance, insulin resistance-related condition or obesity, wherein the gene set comprises genes encoding the proteins: phytase, major myo-inositol transporter lolT, myo-inositol 2-dehydrogenase, inosose dehydratase, 3D-(3,5 / 4)-trihydroxycyclohexane-1,2-dione hydrolase, 5-deoxy-glucuronate isomerase, 5-keto-2-deoxygluconokinase, 5-keto-2-deoxy-D-gluconate-6 phosphate aldolase, 2-hydroxy-3-oxopropionate reductase, and D-beta-hydroxypropionate permease.

2. Bacterium for use according to claim 1, wherein the bacterium is in combination with a second bacterium comprising a gene set that allows said second bacterium to convert 3-hydroxypropionate or a salt or ester thereof to propionate or a salt or ester thereof, wherein the gene set of said second bacterium comprises genes encoding one or more of the proteins: permease, oxoacid CoA transferase, dehydratase, electron transfer flavoprotein beta subunit, electron transfer flavoprotein alpha subunit, and Acyl dehydrogenase.

3. Composition for use in preventing and / or treating metabolic syndrome, insulin resistance, insulin resistance-related condition or obesity, wherein the composition is obtainable by:a) growing a bacterium as defined in claim 1 and optionally a bacterium as defined in claim 2 in an aqueous medium suitable therefor;b) separating the bacterium as defined in claim 1 and optionally the bacterium as defined in claim 2 from the aqueous medium to thereby obtain the composition.

4. Bacterium for use or composition for use according to any one of the previous claims, wherein the bacterium defined in claim 1 is a Mitsuokella species, preferably Mitsuokella jalaludinii or relative thereof having a 16S rRNA gene sequence with at least 97% sequence identity with SEQ ID NO:93 and / or wherein the bacterium defined in claim 2 is an Anaerostipes species, preferably Anaerostipes rhamnosivorans or relative thereof having a 16S rRNA gene sequence with at least 97% sequence identity with SEQ ID NO:94.

5. Bacterium for use or composition for use according to any one of the previous claims, wherein the bacterium defined in claim 1 is Mitsuokella jalaludinii as deposited with deposit number CBS150836; and / or wherein the bacterium defined in claim 2 is Anaerostipes rhamnosivorans as deposited with deposit number CBS 140182.

6. Bacterium for use or composition for use according to any one of the previous claims, wherein the bacterium or composition is not comprised in fecal matter.

7. Bacterium for use according to any one of the previous claims, wherein the use is in preventing and / or treating insulin resistance or insulin resistance-related condition.

8. Bacterium for use according to any one of the previous claims, wherein the insulin resistance-related condition is chosen from dyslipidemia, (metabolic) Adenylosuccinate lyase deficiency ((M)ASLD) I (metabolic) dysfunction-associated steatohepatitis ((M)ASH), type 2 diabetes mellitus and insulin-resistance in endocrine disease.

9. Bacterium for use according to any one of the previous claims, wherein the bacterium is a human intestinal isolate bacterium.

10. Bacterium for use according to any one of the previous claims, wherein the bacterium is comprised in a composition further comprising a physiologically acceptable carrier.

11. Bacterium for use according to claim 10, wherein the composition is a food composition, preferably a dairy product, more preferably a fermented dairy product, such as yogurt or yogurt drink, or the composition is a pharmaceutical composition, preferably in solid dosage form, such as a capsule, a tablet, or a powder.

12. Bacterium for use according to claim 10 or 11, wherein in the composition the bacterium is present in lyophilized or microencapsulated form.

13. Bacterium for use according to any one of the previous claims, wherein the bacterium is present in an amount within the range of between 106 to 1015 colony forming units (CFU).

14. Bacterium for use according to any one of the previous claims, wherein the bacterium is administered separately, sequentially or simultaneously with phytate.

15. Bacterium for use according to any one of the previous claims for use as a probiotic.

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