Increased production of acetyl-phosphate and products derived therefrom in yeasts

Abstract

The present disclosure concerns a fusion polypeptide for making acetyl-phosphate from glucose, a recombinant yeast host cell expressing the fusion polypeptide as well as methods of using the fusion polypeptide. The fusion polypeptide comprising (i) a glucose-6-phosphate isomerase moiety and (ii) a phosphoketolase moiety.

Description

INCREASED PRODUCTION OF ACETYL-PHOSPHATE AND PRODUCTS DERIVED THEREFROM IN YEASTSCROSS-REFERENCE TO RELATED APPLICATION(S) AND DOCUMENT(S)This present patent application claims priority from U.S. provisional patent application 63 / 613,290 filed on December 21 , 2023 and incorporated herewith in its entirety. The present application also includes an electronic version of a sequence listing which is also incorporated herewith in its entirety.TECHNOLOGICAL FIELDThe present disclosure concerns a recombinant yeast host cell for producing acetyl-phosphate as well as products derived therefrom.BACKGROUNDWithin wildtype yeast strains, the majority of acetyl-coenzyme A (CoA) is generated within the mitochondrial matrix via the pyruvate dehydrogenase complex (PDH). As some yeasts, like Saccharomyces cerevisiae, are unable to directly transport acetyl-CoA from the mitochondria to the cytosol, they can rely on a native or on a non-native PDH “bypass” pathway to sustain their cytosolic needs for acetyl-CoA. In the PDH “bypass” pathway, acetyl-CoA is generated from acetaldehyde either via two enzymatic steps carried out by acetaldehyde dehydrogenase and acetyl-CoA synthetase or via a single enzyme step carried out by phosphotransacetylase. As acetyl-CoA is an important precursor to the generation of many valuable chemicals, much work has been performed aimed at increasing the supply of cytosolic acetyl-CoA.The entry point of carbon into the cytosolic pathway is fructose 6-phosphate (P). Fructose 6- P, under the influence of phosphoketolase (PHK) activity, will be transformed into acetyl- phosphate. However, fructose 6-P is also a substrate of phosphofructokinase and used in native glycolysis and is thus already in competition with these other pathways.There is thus a need in providing alternatives to shuttle fructose-6-phosphate into acetyl- phosphate (acetyl-P) to favor the production of high value chemical products derived from acetyl-CoA.BRIEF SUMMARYThe present disclosure concerns a recombinant yeast host cell capable of producing a higher amount of acetyl-phosphate and consequently a higher amount of derived products (e.g., fermentation products derived from acetyl-phosphate).According to a first aspect, the present disclosure provides a fusion polypeptide for making acetyl-phosphate from glucose, the fusion polypeptide comprising (i) a glucose-6-phosphate isomerase moiety and (ii) a phosphoketolase moiety. In some embodiments, the glucose-6-phosphate isomerase moiety has the amino acid sequence of SEQ ID NO: 2, 4, 6, 8, 10, 12, 14, 16, 18, 20, 22, 24, 26, 28 or 30 or is a variant of the amino acid sequence of SEQ ID NO: 2, 4, 6, 8, 10, 12, 14, 16, 18, 20, 22, 24, 26, 28 or 30 having glucose-6-phosphate isomerase activity. In other embodiments, the phosphoketolase moiety has the amino acid sequence of SEQ ID NO: 32 , 34, 36, 38, 40, 42, 44, 46, 48, 50, 52, 54, 56, 58, 60, 62, 64, 66, 68 or 70 or is a variant of the amino acid sequence of SEQ ID NO: 32, 34, 36, 38, 40, 42, 44, 46, 48, 50, 52, 54, 56, 58, 60, 62, 64, 66, 68 or 70 having phosphoketolase activity. In some embodiments, the fusion polypeptide further comprises an amino acid linker between the glucose-6- phosphate isomerase moiety and the phosphoketolase moiety. In specific embodiments, the amino acid linker has the amino acid sequence of SEQ ID NO: 72 or 74 or is a variant of the amino acid sequence of SEQ ID NO: 72 or 74. In some embodiments, the fusion polypeptide has the following formula (I):NH2-PGI-L-PHK-COOH (I) wherein NH2is the amino terminus of the fusion polypeptide, PGI is the glucose-6-phosphate isomerase moiety, L is an optional amino acid linker, PHK is the phosphoketolase moiety, and COOH is the carboxy terminus of the fusion polypeptide.According to a second aspect, the present disclosure provides a recombinant yeast host cell comprising the fusion polypeptide described herein. In some embodiments, the recombinant yeast host further comprises a heterologous polypeptide for converting acetyl-phosphate in acetyl-coenzyme A. In additional embodiment, the heterologous polypeptide for converting acetyl-phosphate in acetyl-coenzyme A comprises a heterologous phosphotransacetylase. In further embodiments, the heterologous phosphotransacetylase has the amino acid sequence of SEQ ID NO: 76, 80, 82, 84, 86, 88, 90, 92, 94, 96, 98, 100 or 102 or is a variant of the amino acid sequence of SEQ ID NO: 76, 80, 82, 84, 86, 88, 90, 92, 94, 96, 98, 100 or 102 having phosphotransacetylase activity. In a further embodiment, the recombinant yeast host comprises a native and / or heterologous polypeptide for converting acetyl-phosphate in acetate. In some embodiments, the native and / or heterologous polypeptide for converting acetyl-phosphate in acetate comprises a native or heterologous glycerol-3-phosphate phosphatase; a heterologous acetate kinase; and / or a heterologous phosphotransacetylase. In some embodiments, the native or heterologous glycerol-3-phosphate phosphatase comprises glycerol-3-phosphate phosphatase 1 and / or glycerol-3-phosphate phosphatase 2. In additional embodiments, the native or heterologous glycerol-3-phosphate phosphatase 1 comprises the amino acid sequence of SEQ ID NO: 104 or is a variant of the amino acid sequence of SEQ ID NO: 104 having glycerol-3-phosphate phosphatase activity. In further embodiments, the native or heterologous glycerol-3-phosphate phosphatase 2 comprises the amino acid sequence of SEQ ID NO: 106 or is a variant of the amino acid sequence of SEQID NO: 106 having glycerol-3-phosphate phosphatase activity. In some embodiments, the heterologous acetate kinase has the amino acid sequence of SEQ ID NO: 108, 110, 112, 114, 116, 118, 120, 122, 124, 126, 128 or 130 or is a variant of the amino acid sequence of SEQ ID NO: 108, 110, 112, 114, 116, 118, 120, 122, 124, 126, 128 or 130 having acetate kinase activity. In some embodiments, the heterologous phosphotransacetylase has the amino acid sequence of SEQ ID NO: 76, 78, 80, 82, 84, 86, 88, 90, 92, 94, 96, 98, 100, 102 or 160 or is a variant of the amino acid sequence of SEQ ID NO: 76, 78, 80, 82, 84, 86, 88, 90, 92, 94, 96, 98, 100, 102 or 160 having phosphotransacetylase activity. In some embodiments, the recombinant yeast host cell comprises a native or heterologous polypeptide for converting acetate into acetyl-coenzyme A. In further embodiments, the native or heterologous polypeptide for converting acetate into acetyl-coenzyme A comprises an acetyl-coenzyme A synthetase. In yet additional embodiments, the acetyl-coenzyme A synthetase has the amino acid sequence of SEQ ID NO: 132, 134, 136, 138, 140 or 142 or is a variant of the amino acid sequence of SEQ ID NO: 132, 134, 136, 138, 140 or 142 having acetyl-coenzyme A synthetase activity. In some embodiments, the recombinant yeast host cell comprises one or more heterologous polypeptide for converting acetyl-coenzyme A into a fermentation product. In additional embodiments, the fermentation product comprises acetone, farnesene, 3-hydroxy-propionic acid, p-coumaric acid, 2-phenylethanol, tyrosol, salidroside, polyhydroxybutyrate, carotenoid, a fatty acid ethyl ester, and / or isopropanol. In still other embodiments, the fermentation product further comprises ethanol. In some embodiments, the recombinant yeast host cell is from the genus Saccharomyces sp., and in further embodiments, from the species Saccharomyces cerevisiae.According to a third aspect, the present disclosure provides a process for making acetylphosphate from glucose, the method comprising contacting the fusion polypeptide described herein with glucose under condition to promote the formation of acetyl-phosphate. In some embodiments, the process comprises contacting the recombinant yeast host cell described herewith with glucose under condition to promote the formation of acetyl-phosphate.BRIEF DESCRIPTION OF THE DRAWINGSHaving thus generally described the nature of the invention, reference will now be made to the accompanying drawings, showing by way of illustration, a preferred embodiment thereof, and in which:Figure 1 provides metabolic pathways using the fusion PGI-PHK of the present disclosure for converting glucose 6-phosphate into acetyl-P and subsequently acetyl-phosphate into acetyl- coenzyme A (acetyl-CoA).Figures 2A and 2B provides embodiments of the PGI-PHK fusion proteins characterized in the Example. (Figure 2A) provide a PGI moiety (having the amino acid sequence of SEQ IDNO: 2) whose carboxy terminus is covalently associated with the amino terminus of an amino acid linker (Linker 1 , having the amino acid sequence of SEQ ID NO: 72). The carboxy terminus of the amino acid linker (Linker 1) is covalently associated with the amino terminus of the PHK moiety (having the amino acid sequence of SEQ ID NO: 32 lacking the N-terminal methionine residue). (Figure 2B) provide a PGI moiety (having the amino acid sequence of SEQ ID NO: 2) whose carboxy terminus is covalently associated with the amino terminus of an amino acid linker (Linker 2, having the amino acid sequence of SEQ ID NO: 74). The carboxy terminus of the amino acid linker (Linker 2) is covalently associated with the amino terminus of the PHK moiety (having the amino acid sequence of SEQ ID NO: 32 lacking the N-terminal methionine residue).Figure 3 compares the acetic acid production in various Saccharomyces cerevisiae strains following fermentation in YPD medium. Results are provided as the amount of acetic acid (g / L) present in the medium after fermentation in function of the Saccharomyces cerevisiae strain used.DETAILLED DESCRIPTIONAcetyl-CoA can be produced in the cytosol of yeasts from acetyl-P. It is known in the art that fructose 6-P, which can be obtained by the enzymatic treatment of glucose 6-phosphate with a glucose-6-phosphate isomerase (PGI), can be converted into acetyl-P via a phosphoketolase (PHK). Once formed, acetyl-P can be converted into acetate (by the enzyme activity of an acetate kinase (ACK) or a glycerol-3-phosphate phosphatase (GPP)), and acetate can be converted into acetyl-CoA (by the enzymatic activity of an acetyl-coenzyme A synthetase (ACS)). Alternatively, acetyl-P can be converted directly into acetyl-CoA by the enzymatic activity of a phosphotransacetylase (PTA).The present disclosure provides a fusion polypeptide comprising both PGI and PHK activities to increase the shuttling of fructose 6-P into acetyl-P (Figure 1). As such, glucose 6-P can be shuttled more efficiently towards the production of acetyl-P and ultimately towards the production of acetyl-CoA. The PGI-PHK fusion thus converts glucose transiently into fructose 6-P (via the enzymatic activity of the PGI moiety) and fructose 6-P into acetyl-P (via the enzymatic activity of the PHK moiety). Once formed, acetyl-P can be converted into acetate (by the enzyme activity of an ACK or a GPP), and acetate can be converted into acetyl-CoA (by the enzymatic activity of an ACS) (Figure 1). Alternatively or in combination, acetyl-P can be converted directly into acetyl-CoA by the enzymatic activity of a PTA (Figure 1).Fusion polypeptidesThe fusion polypeptides, which can be referred as PGI-PHK fusions in the present disclosure, comprises at least two moieties, each moiety having a distinct enzymatic activity. The fusion polypeptides of the present disclosure comprise at least one moiety exhibiting glucose-6-phosphate isomerase (PGI) activity. The fusion polypeptide of the present disclosure comprises at least one moiety exhibiting phosphoketolase (PHK) activity. The fusion polypeptides of the present disclosure exhibit both glucose-6-phosphate isomerase (PGI) activity and phosphoketolase (PHK) activity. The fusion polypeptides of the present disclosure can convert glucose-6-P into acetyl-P, as indicated on Figure 1 . The at least two moieties of the fusion polypeptides can be joined using one or more covalent bonds, just as, for example, one or more amine bonds. The at least two moieties of the fusion polypeptides can be joined directly to one another. Alternatively, the at least two moieties of the fusion polypeptides can be joined indirectly to one another by the presence of a linker. In some embodiments, the linker can comprise one or more amino acid residues. The fusion polypeptides can include, at their amino end, the PGI moiety. In such embodiment, the fusion polypeptide can include, at their carboxy end, the PHK moiety. Alternatively, the fusion polypeptide can include, at their amino end, the PHK moiety. In such embodiment, the fusion polypeptide can include, at their carboxy end, the PGI moiety.Glucose-6-phosphate isomerases or GPIs, also known as phosphoglucose isomerases or phosphohexose isomerases, are classified under Enzyme Commission No. 5.3.1.9 and are intended to encompass enzymes capable of converting D-glucose 6-phosphate (e.g., glucose 6-phosphate) into p-D-fructofuranose 6-phosphate (e.g., fructose 6-phosphate). Polypeptides (including fusion polypeptides) having PGI activity have the ability of converting D-glucose 6- phosphate (e.g., glucose 6-phosphate) into p-D-fructofuranose 6-phosphate (e.g., fructose 6- phosphate). In the context of the present disclosure, the PGI moiety of the fusion polypeptide provides the fusion polypeptide with the ability of converting D-glucose 6-phosphate (e.g., glucose 6-phosphate) into p-D-fructofuranose 6-phosphate (e.g., fructose 6-phosphate). The PGI moiety of the fusion polypeptides can be of prokaryotic origin or a variant thereof. In an embodiment, the PGI moiety can be obtained from Escherichia sp., and in further embodiments from Escherichia coli. In such embodiment, the PGI moiety can have the amino acid sequence of SEQ ID NO: 4 or be a variant of the amino acid sequence of SEQ ID NO: 4 having PGI activity. In addition, the PGI moiety can be encoded by the nucleic acid sequence of SEQ ID NO: 3 or a degenerate nucleic acid sequence encoding the amino acid sequence of SEQ ID NO: 4 (or a variant thereof). In an embodiment, the PGI moiety can be obtained from Bifidobacterium sp., and in further embodiments from Bifidobacterium adolescentis. In such embodiment, the PGI moiety can have the amino acid sequence of SEQ ID NO: 16 or be a variant of the amino acid sequence of SEQ ID NO: 16 having PGI activity. In addition, the PGI moiety can be encoded by the nucleic acid sequence of SEQ ID NO: 15 or a degenerate nucleic acid sequence encoding the amino acid sequence of SEQ ID NO: 16 (or a variant thereof). In an embodiment, the PGI moiety can be obtained from Bacillus sp., and in furtherembodiments from Bacillus subtilis. In such embodiment, the PGI moiety can have the amino acid sequence of SEQ ID NO: 26 or be a variant of the amino acid sequence of SEQ ID NO: 26 having PGI activity. In addition, the PGI moiety can be encoded by the nucleic acid sequence of SEQ ID NO: 25 or a degenerate nucleic acid sequence encoding the amino acid sequence of SEQ ID NO: 26 (or a variant thereof). In an embodiment, the PGI moiety can be obtained from Lachnoclostridium sp., and in further embodiments from Lachnoclostridium phytofermentans. In such embodiment, the PGI moiety can have the amino acid sequence of SEQ ID NO: 28 or be a variant of the amino acid sequence of SEQ ID NO: 28 having PGI activity. In addition, the PGI moiety can be encoded by the nucleic acid sequence of SEQ ID NO: 27 or a degenerate nucleic acid sequence encoding the amino acid sequence of SEQ ID NO: 28 (or a variant thereof). In an embodiment, the PGI moiety can be obtained from Lactiplantibacillus sp., and in further embodiments from Lactiplantibacillus plantarum. In such embodiment, the PGI moiety can have the amino acid sequence of SEQ ID NO: 30 or be a variant of the amino acid sequence of SEQ ID NO: 30 having PGI activity. In addition, the PGI moiety can be encoded by the nucleic acid sequence of SEQ ID NO: 29 or a degenerate nucleic acid sequence encoding the amino acid sequence of SEQ ID NO: 30 (or a variant thereof). The PGI moiety of the fusion polypeptides can be of eukaryotic origin (or a variant thereof). In some additional embodiments, the PGI moiety can be of fungal origin. In an embodiment, the PGI moiety can be obtained from Saccharomyces sp., and in further embodiments from Saccharomyces cerevisiae. In such embodiment, the PGI moiety can have the amino acid sequence of SEQ ID NO: 2 or be a variant of the amino acid sequence of SEQ ID NO: 2 having PGI activity. In addition, the PGI moiety can be encoded by the nucleic acid sequence of SEQ ID NO: 1 or a degenerate nucleic acid sequence encoding the amino acid sequence of SEQ ID NO: 2 (or a variant thereof). In an embodiment, the PGI moiety can be obtained from Kluyveromyces sp., and in further embodiments from Kluyveromyces marxianus. In such embodiment, the PGI moiety can have the amino acid sequence of SEQ ID NO: 6 or be a variant of the amino acid sequence of SEQ ID NO: 6 having PGI activity. In addition, the PGI moiety can be encoded by the nucleic acid sequence of SEQ ID NO: 5 or a degenerate nucleic acid sequence encoding the amino acid sequence of SEQ ID NO: 6 (or a variant thereof). In another embodiment, the PGI moiety can be obtained from Kluyveromyces lactis. In such embodiment, the PGI moiety can have the amino acid sequence of SEQ ID NO: 8 or be a variant of the amino acid sequence of SEQ ID NO: 8 having PGI activity. In addition, the PGI moiety can be encoded by the nucleic acid sequence of SEQ ID NO: 7 or a degenerate nucleic acid sequence encoding the amino acid sequence of SEQ ID NO: 8 (or a variant thereof). In an embodiment, the PGI moiety can be obtained from Ogataea sp., and in further embodiments from Ogataea parapolymorpha. In such embodiment, the PGI moiety can have the amino acid sequence of SEQ ID NO: 10 or be a variant of the amino acid sequence of SEQID NO: 10 having PGI activity. In addition, the PGI moiety can be encoded by the nucleic acid sequence of SEQ ID NO: 9 or a degenerate nucleic acid sequence encoding the amino acid sequence of SEQ ID NO: 10 (or a variant thereof). In an embodiment, the PGI moiety can be obtained from Zygosaccharomyces sp., and in further embodiments from Zygosaccharomyces rouxii. In such embodiment, the PGI moiety can have the amino acid sequence of SEQ ID NO: 12 or be a variant of the amino acid sequence of SEQ ID NO: 12 having PGI activity. In addition, the PGI moiety can be encoded by the nucleic acid sequence of SEQ ID NO: 11 or a degenerate nucleic acid sequence encoding the amino acid sequence of SEQ ID NO: 12 (or a variant thereof). In an embodiment, the PGI moiety can be obtained from Candida sp., and in further embodiments from Candida albicans. In such embodiment, the PGI moiety can have the amino acid sequence of SEQ ID NO: 14 or be a variant of the amino acid sequence of SEQ ID NO: 14 having PGI activity. In addition, the PGI moiety can be encoded by the nucleic acid sequence of SEQ ID NO: 13 or a degenerate nucleic acid sequence encoding the amino acid sequence of SEQ ID NO: 14 (or a variant thereof). In further embodiments, the PGI moiety can be obtained from Candida boidinii. In such embodiment, the PGI moiety can have the amino acid sequence of SEQ ID NO: 24 or be a variant of the amino acid sequence of SEQ ID NO: 24 having PGI activity. In addition, the PGI moiety can be encoded by the nucleic acid sequence of SEQ ID NO: 23 or a degenerate nucleic acid sequence encoding the amino acid sequence of SEQ ID NO: 24 (or a variant thereof). In an embodiment, the PGI moiety can be obtained from Millerozyma sp., and in further embodiments from Millerozyma farinosa. In such embodiment, the PGI moiety can have the amino acid sequence of SEQ ID NO: 18 or be a variant of the amino acid sequence of SEQ ID NO: 18 having PGI activity. In addition, the PGI moiety can be encoded by the nucleic acid sequence of SEQ ID NO: 17 or a degenerate nucleic acid sequence encoding the amino acid sequence of SEQ ID NO: 18 (or a variant thereof). In an embodiment, the PGI moiety can be obtained from Meyerozyma sp., and in further embodiments from Meyerozyma guilliermondii. In such embodiment, the PGI moiety can have the amino acid sequence of SEQ ID NO: 20 or be a variant of the amino acid sequence of SEQ ID NO: 20 having PGI activity. In addition, the PGI moiety can be encoded by the nucleic acid sequence of SEQ ID NO: 19 or a degenerate nucleic acid sequence encoding the amino acid sequence of SEQ ID NO: 20 (or a variant thereof). In an embodiment, the PGI moiety can be obtained from Scheffersomyces sp., and in further embodiments from Scheffersomyces stipitis. In such embodiment, the PGI moiety can have the amino acid sequence of SEQ ID NO: 22 or be a variant of the amino acid sequence of SEQ ID NO: 22 having PGI activity. In addition, the PGI moiety can be encoded by the nucleic acid sequence of SEQ ID NO: 21 or a degenerate nucleic acid sequence encoding the amino acid sequence of SEQ ID NO: 22 (or a variant thereof). In some embodiments, the PGI moiety can have the amino acid sequence of any one of SEQ ID NO: 2, 4, 6, 8, 10, 12, 14, 16, 18, 20, 22, 24, 26,28 or 30. In further embodiments, the PGI can be a variant of the amino acid sequence of SEQ ID NO: 2, 4, 6, 8, 10, 12, 14, 16, 18, 20, 22, 24, 26, 28 or 30, provided that the variant has PGI activity. In some embodiments, the N-terminal methionine residue which is included in the amino acid sequence of the PGI moiety is removed upon inclusion in the fusion protein.Phosphoketolases or PHKs are classified under Enzyme Commission No. 4.1 .2.9 and 4.1 .2.22 and are intended to include the enzymes capable of converting D-xylulose 5-phosphate to D- glyceraldehyde 3-phosphate and acetyl-P. The phosphoketolase can have a single-specificity activity (e.g., single-specificity phosphoketolase), and be only capable of converting D-xylulose 5-phosphate to D-glyceraldehyde 3-phosphate and acetyl-P. The phosphoketolase can have a multiple-specificity / dual-specificity (e.g., multiple-specificity or dual-specificity phosphoketolase), and be also capable of converting D-fructose 6-phosphate to D-erythrose 4-phosphate and / or D-sedoheptulose 7-phosphate into D-ribose 5-phosphate. Polypeptides (including fusion polypeptides) having PHK activity have the ability of converting D-xylulose 5- phosphate to D-glyceraldehyde 3-phosphate and acetyl phosphate. In the context of the present disclosure, the PHK moiety of the fusion polypeptide provides the fusion polypeptide with the ability of converting D-xylulose 5-phosphate to D-glyceraldehyde 3-phosphate and acetyl-P. The PHK moiety of the fusion polypeptides can be of prokaryotic origin (or a variant thereof). In an embodiment, the PHK moiety can be obtained from Bifidobacterium sp., and in further embodiments from Bifidobacterium adolescentis. In such embodiment, the PHK moiety can have the amino acid sequence of SEQ ID NO: 32 or be a variant of the amino acid sequence of SEQ ID NO: 32 having PHK activity. In addition, the PHK moiety can be encoded by the nucleic acid sequence of SEQ ID NO: 31 or a degenerate nucleic acid sequence encoding the amino acid sequence of SEQ ID NO: 32 (or a variant thereof). In some embodiments, the PHK moiety can be obtained from Bifidobacterium bifidum. In such embodiment, the PHK moiety can have the amino acid sequence of SEQ ID NO: 40 or be a variant of the amino acid sequence of SEQ ID NO: 40 having PHK activity. In addition, the PHK moiety can be encoded by the nucleic acid sequence of SEQ ID NO: 39 or a degenerate nucleic acid sequence encoding the amino acid sequence of SEQ ID NO: 40 (or a variant thereof). In some embodiments, the PHK moiety can be obtained from Bifidobacterium gallicium. In such embodiment, the PHK moiety can have the amino acid sequence of SEQ ID NO: 42 or be a variant of the amino acid sequence of SEQ ID NO: 42 having PHK activity. In addition, the PHK moiety can be encoded by the nucleic acid sequence of SEQ ID NO: 41 or a degenerate nucleic acid sequence encoding the amino acid sequence of SEQ ID NO: 42 (or a variant thereof). In some embodiments, the PHK moiety can be obtained from Bifidobacterium animalis. In such embodiment, the PHK moiety can have the amino acid sequence of SEQ ID NO: 44 or be a variant of the amino acid sequence of SEQ ID NO: 44having PHK activity. In addition, the PHK moiety can be encoded by the nucleic acid sequence of SEQ ID NO: 43 or a degenerate nucleic acid sequence encoding the amino acid sequence of SEQ ID NO: 44 (or a variant thereof). In some embodiments, the PHK moiety can be obtained from Bifidobacterium breve. In such embodiment, the PHK moiety can have the amino acid sequence of SEQ ID NO: 64 or be a variant of the amino acid sequence of SEQ ID NO: 64 having PHK activity. In addition, the PHK moiety can be encoded by the nucleic acid sequence of SEQ ID NO: 63 or a degenerate nucleic acid sequence encoding the amino acid sequence of SEQ ID NO: 64 (or a variant thereof). In some embodiments, the PHK moiety can be obtained from Bifidobacterium longum. In such embodiment, the PHK moiety can have the amino acid sequence of SEQ ID NO: 68 or be a variant of the amino acid sequence of SEQ ID NO: 68 having PHK activity. In addition, the PHK moiety can be encoded by the nucleic acid sequence of SEQ ID NO: 67 or a degenerate nucleic acid sequence encoding the amino acid sequence of SEQ ID NO: 68 (or a variant thereof). In an embodiment, the PHK moiety can be obtained from Lactiplantibacillus sp., and in further embodiments from Lactiplantibacillus plantarum. In such embodiment, the PHK moiety can have the amino acid sequence of SEQ ID NO: 46 or be a variant of the amino acid sequence of SEQ ID NO: 46 having PHK activity. In addition, the PHK moiety can be encoded by the nucleic acid sequence of SEQ ID NO: 45 or a degenerate nucleic acid sequence encoding the amino acid sequence of SEQ ID NO: 46 (or a variant thereof). Alternatively, the PHK moiety can have the amino acid sequence of SEQ ID NO: 60 or be a variant of the amino acid sequence of SEQ ID NO: 60 having PHK activity. In addition, the PHK moiety can be encoded by the nucleic acid sequence of SEQ ID NO: 59 or a degenerate nucleic acid sequence encoding the amino acid sequence of SEQ ID NO: 60 (or a variant thereof). Alternatively, the PHK moiety can have the amino acid sequence of SEQ ID NO: 62 or be a variant of the amino acid sequence of SEQ ID NO: 62 having PHK activity. In addition, the PHK moiety can be encoded by the nucleic acid sequence of SEQ ID NO: 61 or a degenerate nucleic acid sequence encoding the amino acid sequence of SEQ ID NO: 62 (or a variant thereof). In some embodiments, the PHK moiety can be obtained from Lactiplantibacillus easel. In such embodiment, the PHK moiety can have the amino acid sequence of SEQ ID NO: 38 or be a variant of the amino acid sequence of SEQ ID NO: 38 having PHK activity. In addition, the PHK moiety can be encoded by the nucleic acid sequence of SEQ ID NO: 37 or a degenerate nucleic acid sequence encoding the amino acid sequence of SEQ ID NO: 38 (or a variant thereof). In some embodiments, the PHK moiety can be obtained from Lactiplantibacillus acidophilus. In such embodiment, the PHK moiety can have the amino acid sequence of SEQ ID NO: 48 or be a variant of the amino acid sequence of SEQ ID NO: 48 having PHK activity. In addition, the PHK moiety can be encoded by the nucleic acid sequence of SEQ ID NO: 47 or a degenerate nucleic acid sequence encoding the amino acid sequence of SEQ ID NO: 48 (or a variant thereof). In some embodiments, the PHK moiety canbe obtained from Lactiplantibacillus pentosus. In such embodiment, the PHK moiety can have the amino acid sequence of SEQ ID NO: 66 or be a variant of the amino acid sequence of SEQ ID NO: 66 having PHK activity. In addition, the PHK moiety can be encoded by the nucleic acid sequence of SEQ ID NO: 65 or a degenerate nucleic acid sequence encoding the amino acid sequence of SEQ ID NO: 66 (or a variant thereof). In an embodiment, the PHK moiety can be obtained from Leuconostoc sp., and in further embodiments from Leuconostoc mesenteroides. In such embodiment, the PHK moiety can have the amino acid sequence of SEQ ID NO: 56 or be a variant of the amino acid sequence of SEQ ID NO: 56 having PHK activity. In addition, the PHK moiety can be encoded by the nucleic acid sequence of SEQ ID NO: 55 or a degenerate nucleic acid sequence encoding the amino acid sequence of SEQ ID NO: 56 (or a variant thereof). In an embodiment, the PHK moiety can be obtained from Oenococcus sp., and in further embodiments from Oenococcus oeni. In such embodiment, the PHK moiety can have the amino acid sequence of SEQ ID NO: 58 or be a variant of the amino acid sequence of SEQ ID NO: 58 having PHK activity. In addition, the PHK moiety can be encoded by the nucleic acid sequence of SEQ ID NO: 57 or a degenerate nucleic acid sequence encoding the amino acid sequence of SEQ ID NO: 58 (or a variant thereof). In an embodiment, the PHK moiety can be obtained from Clostridium sp., and in further embodiments from Clostridium acetobutylicum. In such embodiment, the PHK moiety can have the amino acid sequence of SEQ ID NO: 70 or be a variant of the amino acid sequence of SEQ ID NO: 70 having PHK activity. In addition, the PHK moiety can be encoded by the nucleic acid sequence of SEQ ID NO: 69 or a degenerate nucleic acid sequence encoding the amino acid sequence of SEQ ID NO: 70 (or a variant thereof). The PHK moiety of the fusion polypeptides can be of eukaryotic origin (or a variant thereof). In some additional embodiments, the PHK moiety can be of fungal origin. In an embodiment, the PHK moiety can be obtained from Aspergillus sp., and in further embodiments from Aspergillus niger. In such embodiment, the PHK moiety can have the amino acid sequence of SEQ ID NO: 34 or be a variant of the amino acid sequence of SEQ ID NO: 34 having PHK activity. In addition, the PHK moiety can be encoded by the nucleic acid sequence of SEQ ID NO: 33 or a degenerate nucleic acid sequence encoding the amino acid sequence of SEQ ID NO: 34 (or a variant thereof). In some embodiments, the PHK moiety can be obtained from Aspergillus nidulans. In such embodiment, the PHK moiety can have the amino acid sequence of SEQ ID NO: 52 or be a variant of the amino acid sequence of SEQ ID NO: 52 having PHK activity. In addition, the PHK moiety can be encoded by the nucleic acid sequence of SEQ ID NO: 51 or a degenerate nucleic acid sequence encoding the amino acid sequence of SEQ ID NO: 52 (or a variant thereof). In some embodiments, the PHK moiety can be obtained from Aspergillus clavatus. In such embodiment, the PHK moiety can have the amino acid sequence of SEQ ID NO: 54 or be a variant of the amino acid sequence of SEQ ID NO: 54 having PHK activity. In addition, the PHK moiety can be encoded by the nucleic acidsequence of SEQ ID NO: 53 or a degenerate nucleic acid sequence encoding the amino acid sequence of SEQ ID NO: 54 (or a variant thereof). In an embodiment, the PHK moiety can be obtained from Neurospora sp., and in further embodiments from Neurospora crassa. In such embodiment, the PHK moiety can have the amino acid sequence of SEQ ID NO: 36 or be a variant of the amino acid sequence of SEQ ID NO: 36 having PHK activity. In addition, the PHK moiety can be encoded by the nucleic acid sequence of SEQ ID NO: 35 or a degenerate nucleic acid sequence encoding the amino acid sequence of SEQ ID NO: 36 (or a variant thereof). In an embodiment, the PHK moiety can be obtained from Penicillium sp., and in further embodiments from Penicillium chrysogenum. In such embodiment, the PHK moiety can have the amino acid sequence of SEQ ID NO: 50 or be a variant of the amino acid sequence of SEQ ID NO: 50 having PHK activity. In addition, the PHK moiety can be encoded by the nucleic acid sequence of SEQ ID NO: 49 or a degenerate nucleic acid sequence encoding the amino acid sequence of SEQ ID NO: 50 (or a variant thereof). In some embodiments, the PHK moiety can have the amino acid sequence of any one of SEQ ID NO: 32, 34, 36, 38, 40, 42, 44, 46, 48, 50, 52, 54, 56, 58, 60, 62, 64, 66, 68 or 70. In further embodiments, the PHK can be a variant of the amino acid sequence of SEQ ID NO: 32, 34, 36, 38, 40, 42, 44, 46, 48, 50, 52, 54, 56, 58, 60, 62, 64, 66, 68 or 70, provided that the variant has PHK activity. In some embodiments, the N-terminal methionine residue which is included in the amino acid sequence of the PHK moiety is removed upon inclusion in the fusion protein. Additional embodiments of heterologous polypeptides having phosphoketolase activity are described in US patent 9988650 and are herewith included in their entirety.In embodiments in which the carboxy terminus of the PGI moiety is associated (directly or indirectly) with the amino terminus of the PHK moiety, the fusion polypeptide can have the following formula (I):NH2-PGI-L-PHK-COOH (I) wherein: NH2is the amino terminus of the fusion polypeptide,PGI is the PGI moiety of the fusion polypeptide,L is an optional amino acid linker,PHK is the PHK moiety of the fusion polypeptide,COOH is the carboxy terminus of the fusion polypeptide, and is an amine bound.In embodiments of the fusion polypeptide of formula (I), the PGI moiety can have the amino acid sequence of SEQ ID NO: 2, 4, 6, 8, 10, 12, 14, 16, 18, 20, 22, 24, 26, 28 or 30 or be a variant thereof, and the PHK moiety can have the amino acid sequence of SEQ ID NO: 32, 34,36, 38, 40, 42, 44, 46, 48, 50, 52, 54, 56, 58, 60, 62, 64, 66, 68 or 70 or be a variant thereof. In the embodiments of the fusion protein of formula (I), the N-terminal methionine residue which is included in the amino acid sequence of the PHK moiety can be removed. Embodiments of the combinations of amino acid sequences that can be present in the fusion polypeptide of formula (I) are shown in Table 1 .Table 1 . Combinations of amino acid sequences associated with the PGI moiety and the PHK moiety of the fusion polypeptides of formula (I).In embodiments in which the carboxy terminus of the PHK moiety is associated (directly or indirectly) with the amino terminus of the PGI moiety, the fusion polypeptide can have the following formula (II): NH2-PHK-L-PGI-COOH (II) wherein: NH2is the amino terminus of the fusion polypeptide,PHK is the PHK moiety of the fusion polypeptide,L is an optional amino acid linker,PGI is the PGI moiety of the fusion polypeptide, COOH is the carboxy terminus of the fusion polypeptide, and is an amine bound.In embodiments of the fusion polypeptide of formula (II), the PHK moiety can have the amino acid sequence of SEQ ID NO: 32, 34, 36, 38, 40, 42, 44, 46, 48, 50, 52, 54, 56, 58, 60, 62, 64, 66, 68 or 70 or be a variant thereof, and the PGI moiety can have the amino acid sequence ofSEQ ID NO: 2, 4, 6, 8, 10, 12, 14, 16, 18, 20, 22, 24, 26, 28 or 30 or be a variant thereof. In the embodiments of the fusion protein of formula (II), the N-terminal methionine residue which is included in the amino acid sequence of the PGI moiety can be removed. Embodiments of the combinations of amino acid sequences that can be present in the fusion polypeptide of formula (II) are shown in Table 2.Table 2. Combinations of amino acid sequences associated with the PHK moiety and the PGI moiety of the fusion polypeptides of formula (II).In some embodiments, the moieties of the fusion protein are directly associated with one another. For example, in the fusion protein of formula (I), the carboxy terminus of the PGI moiety can be directly associated (via an amino bound) to the amino terminus of the PHK moiety. In another example, the fusion protein of formula (II), the carboxy terminus of the PHK moiety can be directly associated (via an amine bound) to the amino terminus of the PGI moiety.In additional embodiments of the present disclosure, there may be a linker covalently associated to both moieties. In some embodiments, the linker may be an amino acid linker. In such embodiment, the amino terminus of the linker is covalently associated to the carboxy terminus of one of the moieties and the carboxy terminus of the linker is covalently associated with the amino terminus of the other moiety. In the fusion polypeptide of formula (I), the amino terminus of the linker is associated (directly or indirectly) with the carboxy terminus of the PGI moiety, while the carboxy terminus of the linker is associated (directly or indirectly) with the amino terminus of the PHK moiety. In the fusion polypeptide of formula (II), the amino terminus of the linker is associated (directly or indirectly) with the carboxy terminus of the PHK moiety, while the carboxy terminus of the linker is associated (directly or indirectly) with the amino terminus of the PGI moiety. The amino acid linker comprises at least one amino acid residue, and in some embodiments a plurality of consecutive amino acid residues. In some additional embodiments, the linker can comprise between one and fifty (50) amino acid residues. In some embodiments, the amino acid linker can be rigid (and can have for example the amino acidsequence of SEQ ID NO: 72 or a variant thereof or be encoded by the nucleic acid sequence of SEQ ID NO: 71 or a degenerate sequence thereof encoding the amino acid sequence of SEQ ID NO: 72). In additional embodiments, the amino acid linker can be flexible (and can have for example the amino acid sequence of SEQ ID NO: 74 or a variant thereof or be encoded by the nucleic acid sequence of SEQ ID NO: 73 or a degenerate sequence thereof encoding the amino acid sequence of SEQ ID NO: 74). Additional amino acid linkers include, without limitations, (G)n, (GS)n; (GGS)n; (GGGS)n; (G4S or SEQ ID NO: 309)n; (GGSG)n; (GSAT)n, wherein n = is an integer between 1 to 8 (or more). In an embodiment, the amino acid linker L is (GGGGS)n(also referred to as G4S) and, in still further embodiments, the amino acid linker L comprises more than one G4S (SEQ ID NO: 309) motifs. The amino acid linker can also be, in some embodiments, GSAGSAAGSGEF (SEQ ID NO: 310). Further amino acid linkers include, without limitations, (EAAK)nand (EAAAK - or SEQ ID NO: 311)n, wherein n = is an integer between 1 to 8 (or more). In some embodiments, the one or more (EAAK)n / (EAAAK - or SEQ ID NO: 311 )nmotifs can be separated by one or more additional amino acid residues. Additional amino acid linkers include those having one or more (AP)nmotifs wherein n = is an integer between 1 to 10 (or more).Recombinanthost cells forThe present disclosure provides a recombinant yeast host cell capable of expressing the fusion polypeptide. These recombinant yeast host cells can be obtained by introducing one or more copies of a heterologous nucleic acid molecule encoding the fusion protein.In some embodiments, the recombinant yeast host cell of the present disclosure can include one or more additional genetic modifications. The one or more additional genetic modifications can be made in the coding portion or the non-coding portion of a gene. For example, the recombinant yeast host cells can be obtained by introducing one or more genetic modifications in a corresponding native (parental) yeast host cell. When the genetic modification is aimed at reducing or inhibiting the expression of a specific targeted gene (which is endogenous / native to the host cell), the genetic modifications can be made in one or all copies of the targeted gene(s). When the genetic modification is aimed at increasing the expression of a specific targeted gene, the genetic modification can be made in one or multiple genetic locations. When the genetic modification is aimed at increasing the expression of a specific targeted gene, the genetic modification can be made in one or more regulatory sequence of a native gene to increase its expression. When the genetic modification is aimed at increasing the expression of a specific targeted gene, the genetic modification can be the addition of one or more copies of the heterologous gene encoding a heterologous polypeptide in the genome of the recombinant host. In the context of the present disclosure, when a yeast host cell is qualified as being “genetically engineered”, it is understood to mean that it has been manipulated toeither add at least one or more heterologous or exogenous nucleic acid residue and / or removed at least one endogenous (or native) nucleic acid residue. In some embodiments, the one or more nucleic acid residues that are added can be derived from a heterologous cell or the recombinant host cell itself. In the latter scenario, the nucleic acid residue(s) is (are) added at a genomic location which is different than the native genomic location. The genetic manipulations did not occur in nature and are the results of in vitro manipulations of the native yeast host cell.When expressed in recombinant yeast host cells, the fusion polypeptides and optionally the additional heterologous polypeptides described herein are encoded on one or more heterologous nucleic acid molecule. The term “heterologous” when used in reference to a nucleic acid molecule (such as a promoter or a coding sequence) refers to a nucleic acid molecule that is not natively found in the recombinant host cell. “Heterologous” also includes a native coding region or portion thereof, that is removed from the source organism and subsequently reintroduced into the source organism in a form that is different from the corresponding native gene, e.g., not in its natural location in the organism's genome or as additional copies at its natural location. The heterologous nucleic acid molecule is purposively introduced into the recombinant yeast host cell. In some embodiments, the term “heterologous” as used herein also refers to an element (nucleic acid or protein) that is derived from a source other than the endogenous source. Thus, for example, a heterologous element could be derived from a different strain of host cell or from an organism of a different taxonomic group (e.g., different kingdom, phylum, class order, family genus or species or any subgroup within one of these classifications).The term “heterologous” when used in reference to a polypeptide refers to a polypeptide that is not natively found in the recombinant yeast host cell or that is expressed from a genomic position that is not native in the recombinant yeast host cell. Thus, for example, a heterologous element could be derived from a different strain of host cell or from an organism of a different taxonomic group (e.g., different kingdom, phylum, class order, family genus or species or any subgroup within one of these classifications).The heterologous nucleic acid molecule present in the recombinant yeast host cell can be integrated in the host cell’s genome. The term “integrated” as used herein refers to genetic elements that are placed, through molecular biology techniques, into the chromosome of a yeast host cell. For example, genetic elements can be placed into the chromosome(s) of the host cell as opposed to in a vector such as a plasmid carried by the host cell. Methods for integrating genetic elements into the genome of a host cell are well known in the art and include homologous recombination, a double strand break mechanism, Cre-LoxP mediated recombination, delitto perfetto, meganuclease-mediated double strand break, MAD7, TALEN,and / or CRISPR / Cas9. The heterologous nucleic acid molecule can be present in one or more copies in the yeast host cell’s chromosome. The heterologous nucleic acid molecule can be integrated at a neutral integration site. The heterologous nucleic acid molecule(s) can be introduced in the host cell using a vector. A “vector,” e.g., a “plasmid”, “cosmid” or “artificial chromosome” (such as, for example, a yeast artificial chromosome) refers to an extra chromosomal element and is usually in the form of a circular double-stranded DNA molecule. Such vectors may be autonomously replicating sequences, genome integrating sequences, phage or nucleotide sequences, linear, circular or supercoiled, of a single- or double-stranded DNA or RNA, derived from any source, in which a number of nucleotide sequences have been joined or recombined into a unique construction which is capable of introducing a promoter fragment and DNA sequence for a selected gene product along with appropriate 3' untranslated sequence into a host cell.In some embodiments, heterologous nucleic acid molecules which can be introduced into the recombinant yeast host cells are codon-optimized with respect to the intended recipient recombinant yeast host cell. As used herein the term “codon-optimized coding region” means a nucleic acid coding region that has been adapted for expression in the cells of a given organism by replacing at least one or more than one, codons with one or more codons that are more frequently used in the genes of that organism. In general, highly expressed genes in an organism are biased towards codons that are recognized by the most abundant tRNA species in that organism. One measure of this bias is the “codon adaptation index” or “CAI,” which measures the extent to which the codons used to encode each amino acid in a particular gene are those which occur most frequently in a reference set of highly expressed genes from an organism. The CAI of codon optimized heterologous nucleic acid molecule described herein corresponds to between about 0.8 and 1.0, between about 0.8 and 0.9 or about 1.0. In some embodiments, heterologous nucleic acid molecules which can be introduced into the recombinant host cells are codon-optimized with respect to the intended recipient recombinant host cell so as to limit or prevent homologous recombination with the corresponding native gene.The heterologous nucleic acid molecules of the present disclosure can comprise a coding region for one or more polypeptides (including the fusion polypeptide) to be expressed by the recombinant yeast host cell. The DNA or RNA “coding region” of a heterologous nucleic acid molecule is a DNA or RNA molecule which is transcribed and / or translated into a polypeptide in a cell in vitro or in vivo when placed under the control of appropriate regulatory sequences. “Suitable regulatory regions” refer to nucleic acid regions located upstream (5' non-coding sequences), within or downstream (3' non-coding sequences) of a coding region, and which influence the transcription, RNA processing or stability or translation of the associated codingregion. Regulatory regions may include promoters, translation leader sequences, RNA processing sites, effector binding sites and stem-loop structures. The boundaries of the coding region are determined by a start codon at the 5' (amino) terminus and a translation stop codon at the 3' (carboxyl) terminus. A coding region can include, but is not limited to, prokaryotic regions, cDNA from mRNA, genomic DNA molecules, synthetic DNA molecules or RNA molecules. If the coding region is intended for expression in a eukaryotic cell, a polyadenylation signal and transcription termination sequence will usually be located 3' to the coding region. In an embodiment, the coding region can be referred to as an open reading frame. “Open reading frame" is abbreviated ORF and means a length of nucleic acid, either DNA, cDNA or RNA, that comprises a translation start signal or initiation codon, such as an ATG or AUG, and a termination codon and can be potentially translated into a polypeptide sequence.The nucleic acid molecule(s) described herein can comprise a non-coding region, for example a transcriptional and / or translational control regions. “Transcriptional and translational control regions” are DNA regulatory regions, such as promoters, enhancers, terminators, and the like, that provide for the expression of a coding region in a host cell. In eukaryotic cells, polyadenylation signals are control regions.In the heterologous nucleic acid molecules described herein, the promoter and the nucleic acid molecule coding for the one or more polypeptides (such as the one or more enzymes) can be operatively linked to one another. In the context of the present disclosure, the expressions “operatively linked” or “operatively associated” refers to fact that the promoter is physically associated to the nucleotide acid molecule coding forthe one or more polypeptides in a manner that allows, under certain conditions, for expression of the one or more polypeptides from the heterologous nucleic acid molecule. In an embodiment, the promoter can be located upstream (5’) of the nucleic acid sequence coding for the one or more polypeptide. In still another embodiment, the promoter can be located downstream (3’) of the nucleic acid sequence coding forthe one or more polypeptide. In the context of the present disclosure, one or more than one promoter can be included in the heterologous nucleic acid molecule. When more than one promoters are included in the heterologous nucleic acid molecule, each of the promoters is operatively linked to the nucleic acid sequence coding for the one or more polypeptide. The promoters can be located, in view of the nucleic acid molecule coding for the one or more protein, upstream, downstream as well as both upstream and downstream.“Promoter” refers to a DNA fragment capable of controlling the expression of a coding sequence or functional RNA. The term “expression,” as used herein, refers to the transcription and stable accumulation of sense (mRNA) from the heterologous nucleic acid molecule described herein. Expression may also refer to translation of mRNA into a polypeptide. Promoters may be derived in their entirety from a native gene or be composed of differentelements derived from different promoters found in nature or even comprise synthetic DNA segments. It is understood by those skilled in the art that different promoters may direct the expression at different stages of development or in response to different environmental or physiological conditions. Promoters which cause a gene to be expressed in most cells at most times at a substantial similar level are commonly referred to as “constitutive promoters”. It is further recognized that since in most cases the exact boundaries of regulatory sequences have not been completely defined, DNA fragments of different lengths may have identical promoter activity. A promoter is generally bounded at its 3' terminus by the transcription initiation site and extends upstream (5' direction) to include the minimum number of bases or elements necessary to initiate transcription at levels detectable above background. Within the promoter will be found a transcription initiation site (conveniently defined for example, by mapping with nuclease S1), as well as protein binding domains (consensus sequences) responsible for the binding of the polymerase.The promoter can be heterologous to the nucleic acid molecule encoding the one or more polypeptides. The promoter can be heterologous or derived from a strain being from the same genus or species as the yeast host cell. In an embodiment, the promoter is derived from the same genus or species of the yeast host cell and the heterologous polypeptide is derived from different genus than the yeast host cell.In the context of the present disclosure, the promoter controlling the expression of the heterologous polypeptide or the native polypeptide can be a constitutive promoter (such as, for example, tef2p (e.g., the promoter of the tef2 gene), cwp2p (e.g., the promoter of the cwp2 gene), ssal p (e.g., the promoter of the ssa1 gene), enol p (e.g., the promoter of the enol gene), hxk1 (e.g., the promoter of the hxk1 gene) and pgkl p (e.g., the promoter of the pgk1 gene). In some embodiment, the promoter is or comprises tef2p (e.g., the promoter of the tef2 gene). In some embodiment, the promoter is or comprises adhl p (e.g., the promoter of the adh1 gene). However, in some embodiments, it is preferable to limit the expression of the polypeptide. As such, the promoter controlling the expression of the heterologous polypeptide or the native polypeptide can be an inducible or modulated promoters such as, for example, a glucose-regulated promoter (e.g., the promoter of the hxt7 gene (referred to as hxt7p)) or a sulfite-regulated promoter (e.g., the promoter of the gpd2 gene (referred to as gpd2p or the promoter of the fzf1 gene (referred to as the fzfl p)), the promoter of the ssu1 gene (referred to as ssul p), the promoter of the ssu1-r gene (referred to as ssur1 -rp). In an embodiment, the promoter is an anaerobic-regulated promoters, such as, for example tdh1 p (e.g., the promoter of the tdh1 gene), pau5p (e.g., the promoter of the pau5 gene), hor7p (e.g., the promoter of the hor7 gene), adhl p (e.g., the promoter of the adh1 gene), tdh2p (e.g., the promoter of the tdh2 gene), tdh3p (e.g., the promoter of the tdh3 gene), gpdl p (e.g., the promoter of the gdp1gene), cdc19p (e.g., the promoter of the cdc19 gene), eno2p e.g., the promoter of the eno2 gene), pdcl p (e.g., the promoter of the pdc1 gene), hxt3p (e.g., the promoter of the hxt3 gene), dan1 (e.g., the promoter of the dan1 gene) and tpil p (e.g., the promoter of the tpi1 gene). One or more promoters can be used to allow the expression of each heterologous polypeptides in the recombinant yeast host cell.Inducible promoters include, but are not limited to glucose-regulated promoters (e.g., the promoter of the hxt7 gene (referred to as hxt7p); the promoter of the ctt1 gene (referred to as cttl p); the promoter of the glo1 gene (referred to as glol p); the promoter of the ygp1 gene (referred to as ygpl p); the promoter of the gsy2 gene (referred to as gsy2p); the promoter of the gpm1 gene (referred to as gpml p); and / or the promoter of the pgk1 gene (referred to as pgkl p)), molasses-regulated promoters (e.g., the promoter of the moll gene (referred to as mol1 p); heat shock-regulated promoters (e.g., the promoter of the glo1 gene (referred to as glol p); the promoter of the sti1 gene (referred to as stil p); the promoter of the ygp1 gene (referred to as ygp1 p); and / or the promoter of the gsy2 gene (referred to as gsy2p)), oxidative stress response promoters (e.g., the promoter of the cup1 gene (referred to as cupl p); the promoter of the ctt1 gene (referred to as cttl p); the promoter of the trx2 gene (referred to as trx2p); the promoter of the gpd1 gene (referred to as gpd1 p); the promoter of the hsp12 gene (referred to as hsp12p); the promoter of the hsp150 gene (referred to as hsp150p); the promoter of the ssc1 gene (referred to as sscl p)); osmotic stress response promoters (e.g., the promoter of the ctt1 gene (referred to as cttl p); the promoter of the glo1 gene (referred to as glo1 p); the promoter of the gpd1 gene (referred to as gpd1 p); the promoter of the ygp1 gene (referred to as ygpl p); the promoter of the hor7 gene (referred to as hor7p); and / or the promoter of the stl1 gene (referred to as stH p)), nitrogen-regulated promoters (e.g., the promoter of the ygp1 gene (referred to as ygpl p)), anaerobic-regulated promoters (e.g., the promoter from the aox1 gene (referred to as aox1 p); the promoter of the tir1 gene (referred to as tir1 p); the promoter of the pau5 gene (referred to as pau5p); the promoter of the dan1 gene (referred to as danl p), the promoter of the tdh1 gene (referred to as tdhl p); the promoter of the spi1 gene (referred to as spi 1 p); the promoter of the hxk1 gene (referred to as hxk1 p); the promoter of the anb1 gene (referred to as anbl p); the promoter of the hxt6 gene (referred to as hxt6p); the promoter of the trx1 gene (referred to as trx1 p); the promoter of the aac3 gene (referred to as aac3p); the promoter of the hor7 gene (referred to as hor7p); the promoter of the adh1 gene (referred to as adh1 p); the promoter of the tdh2 gene (referred to as tdh2p); the promoter of the tdh3 gene (referred to as tdh3p); the promoter of the gdp1 gene (referred to as gpdl p); the promoter of the cdc19 gene (referred to as cdc19p); the promoter of the eno2 gene (referred to as eno2p); the promoter of the pdc1 gene (referred to as pdc1 p); the promoter of the hxt3 gene (referred to as hxt3p); and / orthe promoter of the tpi1 gene (referred to tpi1 p)),ethanol-regulated promoters (including ethanol responsive promoters), redox-regulated promoters (e.g., including, but not limited to the promoter of the gpd2 gene (referred as gpd2p)), sulfite-regulated promoters (e.g., including, but not limited to the promoter of the fzf1 gene (referred to as the fzfl p); the promoter of the ssu1 gene (referred to as ssul p); and / or the promoter of the ssu1-r gene (referred to as the ssu1 -rp)); and stress-response promoters (e.g., including, but not limited to the promoter of the yap1 gene (referred to as yapl p)), the promoter of the ssa3 gene (referred to as ssa3p)) and / or the promoter of the hsp104 gene (referred to as hsp104p), a functional variant or a functional fragment thereof).Promoters that can be included in the recombinant yeast host cell of the present disclosure include, without limitation, the promoter of the tdh1 gene (referred to as tdhl p), of the hor7 gene (referred to as hor7p), of the hsp150 gene (referred to as hsp150p), of the hxt7 gene(referred to as hxt7p), of the gpm1 gene (referred to as gpm1 p), of the pgk1 gene (referred to as pgk1 p), of the stl1 gene (referred to as stl 1 p), of the tef2 gene (referred to as tef2p), of the tdh3 gene (referred to as tdh3p), of the fba1 gene (referred to as fbal p), of the eno2 gene(referred to as eno2p), and / or of the hyp2 gene (referred to as hyp2p).In some embodiments, the promoter can be obtained or derived from a native promoter present in Komagataella sp., such as, for example, Komagataella phaffii. Inducible promoters include, but are not limited to glucose-regulated promoters, fructose-regulated promoters, glycerolregulated promoters, heat shock-regulated promoters, oxidative stress response promoters, osmotic stress response promoters, nitrogen-regulated promoters, and ethanol-regulated promoters. In an embodiment, ethanol-regulated promoters include, without limitation, the promoter from the adh2 gene, which is also known as the adh3 gene (referred to as adh2p). Constitutive promoters include, without limitation, the promoter from the spi1 gene (referred to as spil p). In an embodiment, the promoter is a promoter from the gap1 gene (referred to as gapl p). In an embodiment, the promoter is a promoter from the hgt1 gene (referred to as hgtl p). In an embodiment, the promoter is a promoter from the glc3 gene (referred to as glc3p). In an embodiment, the promoter is a promoter from the acb2 gene (referred to as acb2p). In an embodiment, the promoter is a promoter from the pex8 gene (referred to as pex8p). In an embodiment, the promoter is a promoter from the urc1 gene (referred to as urcl p). In an embodiment, the promoter is a promoter from the tpo3 gene (referred to as top3p). In an embodiment, the promoter is a promoter from the bio2 gene (referred to as bio2p). In an embodiment, the promoter is a promoter from the gut1 gene (referred to as gutl p). In an embodiment, the promoter is a promoter from the cat1 gene (referred to as catl p). In an embodiment, the promoter is a promoter from the ic!1 gene (referred to as icll p). In an embodiment, the promoter is a promoter from the gcw14 gene (referred to as gcw14p).In some embodiments, the promoter can be obtained or derived from a native promoter present in Ogataea sp., such as, for example, Ogataea polymorpha. In an embodiment, the promoteris a promoter from the sori gene (referred to as sorl p), the O. polymorpha methanol oxidase mox1 gene (referred to as mox1 p), the O. polymorpha promoter from the gap1 gene (referred to as OpGAPI p), the O. polymorpha promoter from the gapdh gene (referred to as OpGAPDHp), the O. polymorpha promoter from the gcw14 gene (referred to as OpGCW14p), the O. Polymorpha promoter from the adh1 gene (referred to as OpADHI p), the O. polymorpha promoter from the Icl1 gene (referred to as OpICLI p), and / or the O. polymorpha promoter from the tef1 gene (referred to as OpTEFI p).In specific embodiments, the heterologous nucleic acid molecule encoding the heterologous enzyme comprises at least one of the adh2 and / or spi1 variant promoters described in US regular patent application 18 / 740,964 filed on June 12, 2024 and herewith incorporated by reference.Still in the context of the present disclosure, the promoter controlling the expression of the heterologous polypeptide or the native polypeptide can be a glycolytic promoter. For example, the glycolytic promoter can be a promoter (or a combination of promoters) from an alcohol dehydrogenase gene, a glucose-6-phosphate isomerase gene, a phosphofructokinase gene, an aldolase gene, a triosephosphate isomerase gene, a glyceraldehyde-3-phosphate dehydrogenase gene, a 3-phosphoglycerate kinase gene, a phosphoglycerate mutase, an enolase and / or a pyruvate kinase gene.In some embodiments, the present disclosure concerns the expression of a heterologous polypeptide (such as a heterologous fusion polypeptide), a variant thereof or a fragment thereof in a host cell. A variant comprises at least one amino acid difference when compared to the amino acid sequence of the wild-type polypeptide. The polypeptide “variants” have at least 50%, 55%, 60%, 65%, 70%, 75%, 80%, 85%, 90%, 95%, 96%, 97%, 98% or 99% identity to the corresponding wild-type heterologous polypeptides described herein. The term “percent identity”, as known in the art, is a relationship between two or more polypeptide sequences or two or more polynucleotide sequences, as determined by comparing the sequences. The level of identity can be determined conventionally using known computer programs. Identity can be readily calculated by known methods, including but not limited to those described in: Computational Molecular Biology (Lesk, A. M., ed.) Oxford University Press, NY (1988); Biocomputing: Informatics and Genome Projects (Smith, D. W., ed.) Academic Press, NY (1993); Computer Analysis of Sequence Data, Part I (Griffin, A. M., and Griffin, H. G., eds.) Humana Press, NJ (1994); Sequence Analysis in Molecular Biology (von Heinje, G., ed.) Academic Press (1987); and Sequence Analysis Primer (Gribskov, M. and Devereux, J., eds.) Stockton Press, NY (1991). Preferred methods to determine identity are designed to give the best match between the sequences tested. Methods to determine identity and similarity are codified in publicly available computer programs. Sequence alignments and percent identitycalculations may be performed using the Megalign program of the LASERGENE bioinformatics computing suite (DNASTAR Inc., Madison, Wis.). Multiple alignments of the sequences disclosed herein were performed using the Clustal method of alignment (Higgins and Sharp (1989) CABIOS. 5:151-153) with the default parameters (GAP PENALTY=10, GAP LENGTH PEN ALT Y= 10). Default parameters for pairwise alignments using the Clustal method were KTUPLB 1 , GAP PENALTY=3, WINDOW=5 and DIAGONALS SAVED=5.The variants exhibit the biological activity associated with the wild-type heterologous polypeptide. In an embodiment, the variant polypeptide exhibits at least 50%, 55%, 60%, 65%, 70%, 75%, 80%, 85%, 90%, 95%, 96%, 97%, 98% or 99% of the biological activity (which can be, in some embodiments, the enzymatic activity) of the corresponding wild-type heterologous polypeptide. The biological activity of the variants can be determined by methods and assays known in the art.The variants described herein may be (i) one in which one or more of the amino acid residues are substituted with a conserved or non-conserved amino acid residue (preferably a conserved amino acid residue) and such substituted amino acid residue may or may not be one encoded by the genetic code or (ii) one in which one or more of the amino acid residues includes a substituent group or (iii) one in which the mature polypeptide is fused with another compound, such as a compound to increase the half-life of the polypeptide (for example, polyethylene glycol) or (iv) one in which the additional amino acids are fused to the mature polypeptide for purification of the polypeptide.A “variant” can be a conservative variant or an allelic variant. As used herein, a conservative variant refers to alterations in the amino acid sequence that do not adversely affect the biological functions of the polypeptide. A substitution, insertion or deletion is said to adversely affect the protein when the altered sequence prevents or disrupts a biological function associated with the polypeptide. For example, the overall charge, structure or hydrophobic- hydrophilic properties of the polypeptide can be altered without adversely affecting a biological activity. Accordingly, the amino acid sequence can be altered, for example to render the polypeptide more hydrophobic or hydrophilic, without adversely affecting the biological activity of the polypeptide.A “variant” can be a fragment of a heterologous wild-type polypeptide or fragment of a variant polypeptide. In some embodiments, polypeptide “fragments” have at least at least 50, 100, 200, 300, 400, 500 or more consecutive amino acids of the corresponding wild-type polypeptide or the variant. A fragment comprises at least one less amino acid residue when compared to the amino acid sequence of the corresponding wild-type heterologous polypeptide or of the variant polypeptide. In some embodiments, the fragments correspondingto the wild-type polypeptide or variant polypeptide to which the signal sequence was removed. In some embodiments, the “fragments” have at least 50%, 55%, 60%, 65%, 70%, 75%, 80%, 85%, 90%, 95%, 96%, 97%, 98% or 99% identity to the corresponding wild-type polypeptides or variants. In some embodiments, fragments of the polypeptides can be employed for producing the corresponding full-length enzyme by peptide synthesis. Therefore, the fragments can be employed as intermediates for producing the full-length polypeptide.In the context of the present disclosure, the fragments exhibit the biological activity of the heterologous wild-type polypeptide or of the variant polypeptide. In an embodiment, the fragment polypeptide exhibits at least 50%, 55%, 60%, 65%, 70%, 75%, 80%, 85%, 90%, 95%, 96%, 97%, 98% or 99% of the biological activity of the corresponding heterologous wild-type polypeptide or of the variant. The biological activity of fragments can be determined by methods and assays known in the art.In some additional embodiments, the present disclosure also provides reducing the expression of or inactivating a native gene ortholog of a native gene known to encode a native polypeptide. A “gene ortholog” is understood to be a gene in a different species that evolved from a common ancestral gene by speciation. In the context of the present invention, a gene ortholog encodes a polypeptide exhibiting the same biological function than the native polypeptide. In some further embodiments, the present disclosure also provides reducing the expression or inactivating a native gene paralog of a native gene known to encode a native polypeptide. A “gene paralog” is understood to be a gene related by duplication within the genome. In the context of the present invention, a gene paralog encodes a polypeptide that could exhibit the same biological function than the native polypeptide.The recombinant host cell of the present disclosure has the ability (which can be intrinsic and / or provided or increased by the genetic modifications introduced) to convert a biomass into one or more fermentation products. The recombinant yeast host cell can be a yeast or a fungal cell. In the context of the present disclosure, the recombinant yeast host cell is a fermenting yeast cell because it is capable of converting the biomass into the one or more fermentation products. Suitable recombinant yeast yeast host cells can be, for example, from the genus Blastobotrys (formely known as Arxula), Candida, Debaryomyces, Hanseniaspora (formely known as Kloeckera), Kazachstania, Komagataella, Kluyveromyces, Ogataea, Pichia (formely known as Hansenula), Phaffia, Saccharomyces, Scheffersomyces, Schwanniomyces or Yarrowia. Suitable yeast species can include, for example, S. cerevisiae (including, but not limited to, var. diastaticus), Saccharomyces uvarum, Kazachstania bulderi, Kazachstania barnetti, Kazachstania exigua, Kluyveromyces lactis, Kluyveromyces marxianus, Komagataella phaffii, Candida albicans, Candida utilis, Scheffersomyces stipitis, Pichia kudriavzevii, Yarrowia lipolytica, Ogataea polymorpha, Phaffia rhodozyma, Blastobotrys adeninivorans,Debaryomyces hansenii or Schwanniomyces polymorphus. Suitable recombinant fungal host cells can be from the genus Phaffia, Schizosaccharomyces, and include, in some embodiments, the species Schizzosaccharomyces pombe. In some embodiments, the host cell can be an oleaginous yeast cell. For example, the oleaginous yeast host cell can be from the genus Blakeslea, Candida, Cryptococcus, Cunninghamella, Lipomyces, Mortierella, Mucor, Phycomyces, Pythium, Rhodotorula, Trichosporon or Yarrowia. In some alternative embodiments, the host cell can be an oleaginous microalgae host cell (e.g., for example, from the genus Thraustochytrium or Schizochytriurri). In an embodiment, the fermenting yeast or recombinant yeast host cell is from the genus Saccharomyces and, in some embodiments, from the species Saccharomyces cerevisiae.In an embodiment, the recombinant yeast host cell can convert glucose-6-phosphate to acetyl- coA. As indicated on Figure 1 , once glucose-6-phosphate is converted to acetyl-P by the fusion polypeptide (a variant or a fragment thereof), acetyl-P can be further converted into acetylcoenzyme A via two metabolic routes. The first metabolic route is the enzymatic conversion of acetyl-P directly into acetyl-coA using a polypeptide having phosphotransacetylase activity. The second metabolic route relies on the successive enzymatic conversion of acetyl-P into acetate (by the enzymatic activity of a polypeptide having acetate kinase activity or a polypeptide having glycerol-3-P phosphatase activity) and the conversion of acetate into acetyl-coA (by the enzymatic activity of a polypeptide having acetyl-coenzyme A synthetase activity.The ability of the recombinant yeast host cell to convert glucose-6-phosphate to acetylcoenzyme A can be native to the recombinant yeast host cell or can be provided / increased by the expression of a phosphotransacetylase (PTA). As such, the recombinant yeast host cell of the present disclosure can include, in such embodiments, a phosphotransacetylase. As used herein, the terms "phosphotransacetylase" and "PTA" are intended to include the enzymes capable of converting acetyl-phosphate into acetyl-coA. Phosphotransacetylases include those enzymes that correspond to Enzyme Commission Number 2.3.1 .8. The PTA can be native or heterologous to the recombinant yeast host cell. In some embodiments, the PTA is of prokaryotic origin (or a variant thereof). In other embodiments, the PTA can be encoded by a pta gene (e.g., PTA). In some embodiments, the PTA is derived from Bifidobacterium sp., and in further embodiments from Bifidobacterium adolescentis. In such embodiments, the PTA can have the amino acid sequence of SEQ ID NO: 76 or be a variant of the amino acid sequence of SEQ ID NO: 76 having PTA activity. The recombinant yeast host cell can include a heterologous nucleic acid molecule encoding the PTA. In such embodiment, the heterologous nucleic acid molecule can comprise the nucleic acid sequence of SEQ ID NO: 75 or a degenerate nucleic acid sequence encoding the amino acid sequence of SEQ ID NO: 76 (or avariant thereof). In further embodiments, the PTA is derived from Bifidobacterium animalis. In such embodiments, the PTA can have the amino acid sequence of SEQ ID NO: 98 or be a variant of the amino acid sequence of SEQ ID NO: 98 having PTA activity. The recombinant yeast host cell can include a heterologous nucleic acid molecule encoding the PTA. In such embodiment, the heterologous nucleic acid molecule can comprise the nucleic acid sequence of SEQ ID NO: 97 or a degenerate nucleic acid sequence encoding the amino acid sequence of SEQ ID NO: 98 (or a variant thereof). In some further embodiments, the PTA is derived from Bifidobacterium bifidum. In such embodiments, the PTA can have the amino acid sequence of SEQ ID NO: 160 or be a variant of the amino acid sequence of SEQ ID NO: 160 having PTA activity. The recombinant yeast host cell can include a heterologous nucleic acid molecule encoding the PTA. In such embodiment, the heterologous nucleic acid molecule can comprise the nucleic acid sequence of SEQ ID NO: 159 or a degenerate nucleic acid sequence encoding the amino acid sequence of SEQ ID NO: 160 (or a variant thereof). In some embodiments, the PTA is derived from Leuconostoc sp., and in further embodiments from Leuconostoc mesenteroides. In such embodiments, the PTA can have the amino acid sequence of SEQ ID NO: 78 or be a variant of the amino acid sequence of SEQ ID NO: 78 having PTA activity. The recombinant yeast host cell can include a heterologous nucleic acid molecule encoding the PTA. In such embodiment, the heterologous nucleic acid molecule can comprise the nucleic acid sequence of SEQ ID NO: 77 or a degenerate nucleic acid sequence encoding the amino acid sequence of SEQ ID NO: 78 (or a variant thereof). In some embodiments, the PTA is derived from Oenococcus sp., and in further embodiments from Oenococcus oenii. In such embodiments, the PTA can have the amino acid sequence of SEQ ID NO: 80 or be a variant of the amino acid sequence of SEQ ID NO: 80 having PTA activity. The recombinant yeast host cell can include a heterologous nucleic acid molecule encoding the PTA. In such embodiment, the heterologous nucleic acid molecule can comprise the nucleic acid sequence of SEQ ID NO: 79 or a degenerate nucleic acid sequence encoding the amino acid sequence of SEQ ID NO: 80 (or a variant thereof). In some embodiments, the PTA is derived from Salmonella sp., and in further embodiments from Salmonella enterica. In such embodiments, the PTA can have the amino acid sequence of SEQ ID NO: 88 or 90 or be a variant of the amino acid sequence of SEQ ID NO: 88 or 90 having PTA activity. The recombinant yeast host cell can include a heterologous nucleic acid molecule encoding the PTA. In such embodiment, the heterologous nucleic acid molecule can comprise the nucleic acid sequence of SEQ ID NO: 87 or 89 or a degenerate nucleic acid sequence encoding the amino acid sequence of SEQ ID NO: 88 or 90 (or a variant thereof). In some embodiments, the PTA is derived from Bacillus sp., and in further embodiments from Bacillus subtilis. In such embodiments, the PTA can have the amino acid sequence of SEQ ID NO: 86 or be a variant of the amino acid sequence of SEQ ID NO: 86 having PTA activity. The recombinant yeast host cell can include a heterologous nucleic acidmolecule encoding the PTA. In such embodiment, the heterologous nucleic acid molecule can comprise the nucleic acid sequence of SEQ ID NO: 85 or a degenerate nucleic acid sequence encoding the amino acid sequence of SEQ ID NO: 86 (or a variant thereof). In some embodiments, the PTA is derived from Clostridium sp., and in further embodiments from Clostridium kluveryi. In such embodiments, the PTA can have the amino acid sequence of SEQ ID NO: 92 or be a variant of the amino acid sequence of SEQ ID NO: 92 having PTA activity. The recombinant yeast host cell can include a heterologous nucleic acid molecule encoding the PTA. In such embodiment, the heterologous nucleic acid molecule can comprise the nucleic acid sequence of SEQ ID NO: 91 or a degenerate nucleic acid sequence encoding the amino acid sequence of SEQ ID NO: 91 (or a variant thereof). In some embodiments, the PTA is derived from Clostridium sp., and in further embodiments from Clostridium phytofermentans. In such embodiments, the PTA can have the amino acid sequence of SEQ ID NO: 100 or be a variant of the amino acid sequence of SEQ ID NO: 100 having PTA activity. The recombinant yeast host cell can include a heterologous nucleic acid molecule encoding the PTA. In such embodiment, the heterologous nucleic acid molecule can comprise the nucleic acid sequence of SEQ ID NO: 99 or a degenerate nucleic acid sequence encoding the amino acid sequence of SEQ ID NO: 100 (or a variant thereof). In some embodiments, the PTA is derived from Holophagae sp., and in further embodiments from Holophagae bacterium. In such embodiments, the PTA can have the amino acid sequence of SEQ ID NO: 102 or be a variant of the amino acid sequence of SEQ ID NO: 102 having PTA activity. The recombinant yeast host cell can include, a heterologous nucleic acid molecule encoding the PTA. In such embodiment, the heterologous nucleic acid molecule can comprise the nucleic acid sequence of SEQ ID NO: 101 or a degenerate nucleic acid sequence encoding the amino acid sequence of SEQ ID NO: 102 (or a variant thereof). In some embodiments, the PTA is derived from Azotobacter sp., and in further embodiments from Azotobacter vinelandii. In such embodiments, the PTA can have the amino acid sequence of SEQ ID NO: 82 or be a variant of the amino acid sequence of SEQ ID NO: 82 having PTA activity. The recombinant yeast host cell can include a heterologous nucleic acid molecule encoding the PTA. In such embodiment, the heterologous nucleic acid molecule can comprise the nucleic acid sequence of SEQ ID NO: 81 or a degenerate nucleic acid sequence encoding the amino acid sequence of SEQ ID NO: 82 (or a variant thereof). In some embodiments, the PTA is derived from Lactiplantibacillus sp., and in further embodiments from Lactiplantibacillus plantarum. In such embodiments, the PTA can have the amino acid sequence of SEQ ID NO: 84 or be a variant of the amino acid sequence of SEQ ID NO: 84 having PTA activity. The recombinant yeast host cell can include a heterologous nucleic acid molecule encoding the PTA. In such embodiment, the heterologous nucleic acid molecule can comprise the nucleic acid sequence of SEQ ID NO: 83 or a degenerate nucleic acid sequence encoding the amino acid sequence of SEQ ID NO:84 (or a variant thereof or a fragment thereof). In some embodiments, the PTA is of eukaryotic origin (or a variant thereof). In some embodiments, the PTA is derived from Phytophthora sp., and in further embodiments from Phytophthora ramorum. In such embodiments, the PTA can have the amino acid sequence of SEQ ID NO: 94 or be a variant of the amino acid sequence of SEQ ID NO: 94 having PTA activity. The recombinant yeast host cell can include a heterologous nucleic acid molecule encoding the PTA. In such embodiment, the heterologous nucleic acid molecule can comprise the nucleic acid sequence of SEQ ID NO: 93 or a degenerate nucleic acid sequence encoding the amino acid sequence of SEQ ID NO: 94 (or a variant thereof). In some embodiments, the PTA is derived from Globisporangium sp., and in further embodiments from Globisporangium splendens. In such embodiments, the PTA can have the amino acid sequence of SEQ ID NO: 96 or be a variant of the amino acid sequence of SEQ ID NO: 96 having PTA activity. The recombinant yeast host cell can include, a nucleic acid molecule can comprise the nucleic acid sequence of SEQ ID NO: 95 or a degenerate nucleic acid sequence encoding the amino acid sequence of SEQ ID NO: 96 (or a variant thereof). Additional sources of PTA that can be included in the recombinant yeast host cell of the present disclosure include, without limitation, Phytophthora sp., (including but not limited to Phytophthora cactorum, Phytophthora parasitica or Phytophthora idaei), Chlamydomonas sp. (including but not limited to Chlamydomonas reinhardtii), Clostridium sp. (including but not limited to Clostridium cellulolyticum), and Microcystis sp. (including but not limited to Microcystis aeruginosa).In embodiments in which the recombinant yeast host cell can convert glucose-6-phosphate to acetyl-coA, the recombinant yeast host cell can have the native ability to express and / or can be genetically modified to increase the expression of an acetate kinase (ACK) or a glycerol-3- phosphate phosphatase (GPP) (to convert acetyl-P into acetate) and / or an acetyl-coenzyme A synthetase (ACS) (to convert acetate into acetyl-coenzyme A). As such, the recombinant yeast host cell of the present disclosure can include, in such embodiments, an acetate kinase, a glycerol-3-phosphate phosphatase and / or an acetyl-coenzyme A synthetase. In one example, the recombinant yeast host cell of the present disclosure can include an acetate kinase and an acetyl-coenzyme A synthetase. In another example, the recombinant yeast host cell of the present disclosure can include a glycerol-3-phosphate phosphatase and an acetyl-coenzyme Asynthetase. In still another example, the recombinant yeast host cell of the present disclosure can include an acetate kinase, a glycerol-3-phosphate phosphatase and an acetyl-coenzyme A synthetase.In some embodiments, the recombinant yeast host cells of the present disclosure can include / express, in some embodiments, an acetate kinase. As used herein, the terms "acetate kinase" and "ACK" are intended to include the enzymes capable of converting acetate intoacetyl-phosphate (acetyl-P). Acetate kinases include those enzymes that correspond to Enzyme Commission Number 2.72.1. The ACK can be native or heterologous to the recombinant yeast host cell. In other embodiments, the ACK can be encoded by a ack gene e.g., ACK). In some embodiments, the ACK is of prokaryotic origin (or a variant thereof). In some embodiments, the ACK is derived from Bifidobacterium sp., and in further embodiments from Bifidobacterium adolescentis. In such embodiments, the ACK can have the amino acid sequence of SEQ ID NO: 108 or be a variant of the amino acid sequence of SEQ ID NO: 108 having ACK activity. The recombinant yeast host cell can include, a heterologous nucleic acid molecule encoding the ACK. In such embodiment, the heterologous nucleic acid molecule can comprise the nucleic acid sequence of SEQ ID NO: 107 or a degenerate nucleic acid sequence encoding the amino acid sequence of SEQ ID NO: 108 (or a variant thereof). In some embodiments, the ACK is derived from Leuconostoc sp., and in further embodiments from Leuconostoc mesenteroides. In such embodiments, the ACK can have the amino acid sequence of SEQ ID NO: 110 or be a variant of the amino acid sequence of SEQ ID NO: 110 having ACK activity. The recombinant yeast host cell can include, a heterologous nucleic acid molecule encoding the ACK. In such embodiment, the heterologous nucleic acid molecule can comprise the nucleic acid sequence of SEQ ID NO: 109 or a degenerate nucleic acid sequence encoding the amino acid sequence of SEQ ID NO: 110 (or a variant thereof). In some embodiments, the ACK is derived from Oenococcus sp., and in further embodiments from Oenococcus oenii. In such embodiments, the ACK can have the amino acid sequence of SEQ ID NO: 112 or be a variant of the amino acid sequence of SEQ ID NO: 112 having ACK activity. The recombinant yeast host cell can include a heterologous nucleic acid molecule encoding the ACK. In such embodiment, the heterologous nucleic acid molecule can comprise the nucleic acid sequence of SEQ ID NO: 111 or a degenerate nucleic acid sequence encoding the amino acid sequence of SEQ ID NO: 112 (or a variant thereof). In some embodiments, the ACK is derived from Escherichia sp., and in further embodiments from Escherichia coli. In such embodiments, the ACK can have the amino acid sequence of SEQ ID NO: 114 or be a variant of the amino acid sequence of SEQ ID NO: 114 having ACK activity. The recombinant yeast host cell can include a heterologous nucleic acid molecule encoding the ACK. In such embodiment, the heterologous nucleic acid molecule can comprise the nucleic acid sequence of SEQ ID NO: 113 or a degenerate nucleic acid sequence encoding the amino acid sequence of SEQ ID NO: 114 (or a variant thereof). In some embodiments, the ACK is derived from Bacillus sp., and in further embodiments from Bacillus subtilis. In such embodiments, the ACK can have the amino acid sequence of SEQ ID NO: 116 or be a variant of the amino acid sequence of SEQ ID NO: 116 having ACK activity. The recombinant yeast host cell can include a heterologous nucleic acid molecule encoding the ACK. In such embodiment, the heterologous nucleic acid molecule can comprise the nucleic acid sequence of SEQ ID NO:115 or a degenerate nucleic acid sequence encoding the amino acid sequence of SEQ ID NO:116 (or a variant thereof). In some embodiments, the ACK is derived from Clostridium sp., and in further embodiments from Clostridium acetobutylicum. In such embodiments, the ACK can have the amino acid sequence of SEQ ID NO: 118 or be a variant of the amino acid sequence of SEQ ID NO: 118 having ACK activity. The recombinant yeast host cell can include a heterologous nucleic acid molecule encoding the ACK. In such embodiment, the heterologous nucleic acid molecule can comprise the nucleic acid sequence of SEQ ID NO: 117 or a degenerate nucleic acid sequence encoding the amino acid sequence of SEQ ID NO: 118 (or a variant thereof). In some embodiments, the ACK is derived from Clostridium kluveryi. In such embodiments, the ACK can have the amino acid sequence of SEQ ID NO: 130 or be a variant of the amino acid sequence of SEQ ID NO: 130 having ACK activity. The recombinant yeast host cell can include a heterologous nucleic acid molecule encoding the ACK. In such embodiment, the heterologous nucleic acid molecule can comprise the nucleic acid sequence of SEQ ID NO: 129 or a degenerate nucleic acid sequence encoding the amino acid sequence of SEQ ID NO: 130 (or a variant thereof). In some embodiments, the ACK is derived from Salmonella sp., and in further embodiments from Salmonella enterica. In such embodiments, the ACK can have the amino acid sequence of SEQ ID NO: 120 or be a variant of the amino acid sequence of SEQ ID NO: 120 having ACK activity. The recombinant yeast host cell can include a heterologous nucleic acid molecule encoding the ACK. In such embodiment, the heterologous nucleic acid molecule can comprise the nucleic acid sequence of SEQ ID NO:119 or a degenerate nucleic acid sequence encoding the amino acid sequence of SEQ ID NO:120 (a variant thereof or a fragment thereof). In some embodiments, the ACK is derived from Lactiplantibacillus sp., and in further embodiments from Lactiplantibacillus plantarum. In such embodiments, the ACK can have the amino acid sequence of SEQ ID NO: 128 or be a variant of the amino acid sequence of SEQ ID NO: 128 having ACK activity. The recombinant yeast host cell can include a heterologous nucleic acid molecule encoding the ACK. In such embodiment, the heterologous nucleic acid molecule can comprise the nucleic acid sequence of SEQ ID NO: 127 or a degenerate nucleic acid sequence encoding the amino acid sequence of SEQ ID NO: 128 (or a variant thereof). In some embodiments, the ACK is of eukaryotic origin (or a variant thereof). In some embodiments, the ACK is derived from Phytophthora sp., and in further embodiments from Phytophthora ramorum. In such embodiments, the ACK can have the amino acid sequence of SEQ ID NO: 122 or be a variant of the amino acid sequence of SEQ ID NO: 122 having ACK activity. The recombinant yeast host cell can include a heterologous nucleic acid molecule encoding the ACK. In such embodiment, the heterologous nucleic acid molecule can comprise the nucleic acid sequence of SEQ ID NO: 121 or a degenerate nucleic acid sequence encoding the amino acid sequence of SEQ ID NO: 122 (or a variant thereof). In some embodiments, the ACK is derived from Chlamydomonas sp., andin further embodiments from Chlamydomonas reinhardtii. In such embodiments, the ACK can have the amino acid sequence of SEQ ID NO: 124 or be a variant of the amino acid sequence of SEQ ID NO: 124 having ACK activity. The recombinant yeast host cell can include a heterologous nucleic acid molecule encoding the ACK. In such embodiment, the heterologous nucleic acid molecule can comprise the nucleic acid sequence of SEQ ID NO: 123 or a degenerate nucleic acid sequence encoding the amino acid sequence of SEQ ID NO: 124 (or a variant thereof). In some embodiments, the ACK is derived from Aspergillus sp., and in further embodiments from Aspergillus nidulans. In such embodiments, the ACK can have the amino acid sequence of SEQ ID NO: 126 or be a variant of the amino acid sequence of SEQ ID NO: 126 having ACK activity. The recombinant yeast host cell can include a heterologous nucleic acid molecule encoding the ACK. In such embodiment, the heterologous nucleic acid molecule can comprise the nucleic acid sequence of SEQ ID NO: 125 or a degenerate nucleic acid sequence encoding the amino acid sequence of SEQ ID NO: 126 (or a variant thereof).The recombinant yeast host cell of the present disclosure can include, in some embodiments, a glycerol-3-phosphate phosphatase. As used herein, the term “glycerol-3-phosphate phosphatase” or “GPP” are intended to include the enzymes capable of dephosphorylating, amongst other substrates, acetyl-phosphate to generate acetate. Glycerol-3-phosphate phosphatases include those enzymes that correspond to Enzyme Commission Number 3.1 .3.21 . The GPP can be native or heterologous to the recombinant yeast host cell. The GPP can be of prokaryotic origin (or a variant thereof). The GPP can be of eukaryotic origin (or a variant thereof). In some embodiments, the GPP can be encoded by a gpp1 gene (e.g., GPP1) or a gpp2 gene (e.g., GPP2). In some embodiments, the GPP is derived from Saccharomyces sp., and in further embodiments from Saccharomyces cerevisiae. In such embodiments, the GPP can have the amino acid sequence of SEQ ID NO: 104 or 106 or be a variant of the amino acid sequence of SEQ ID NO: 104 or 106 having ACS activity. The recombinant yeast host cell can include, a heterologous nucleic acid molecule encoding the GPP. In such embodiment, the heterologous nucleic acid molecule can comprise the nucleic acid sequence of SEQ ID NO: 103 or 105 or a degenerate nucleic acid sequence encoding the amino acid sequence of SEQ ID NO: 104 or 106 (or a variant thereof). In some embodiments, the GPP1 is derived from Arabidopsis sp., and in further embodiments, from Arabidopsis thaliana (and can be associated with the NCBI Gene ID: 828690 or a variant thereof). In some embodiments, the GPP1 is derived from Lachnellula sp., and in further embodiments, from Lachnellula hyalina (and can be associated with the NCBI Gene ID: 41983435 or a variant thereof). In some embodiments, the GPP1 is derived from Scheffersomyces sp., and in further embodiments, from Scheffersomyces stipitis (and can be associated with the NCBI Gene ID: 4836794 or a variant thereof). In some embodiments, the GPP1 is derived from Aspergillus sp., and in furtherembodiments, from Aspergillus melleus (and can be associated with the NCBI Gene ID: 70114293 or a variant thereof). In some embodiments, the GPP1 is derived from Didymosphaeria sp., and in further embodiments, from Didymosphaeria variabile (and can be associated with the NCBI Gene ID: 80909868 or a variant thereof). In some embodiments, the GPP1 is derived from Ophidiomyces sp., and in further embodiments, from Ophidiomyces ophidiicola (and can be associated with the NCBI Gene ID: 73310376 or a variant thereof). In some embodiments, the GPP1 is derived from Purpureocillium sp., and in further embodiments, from Purpureocillium takamizusanense (and can be associated with the NCBI Gene ID: 72063146 or a variant thereof). In some embodiments, the GPP1 is derived from Chlorella sp., and in further embodiments, from Chlorella variabilis (and can be associated with the NCBI Gene ID: 17352997 or a variant thereof). In some embodiments, the GPP2 is derived from Colletotrichum sp., and in further embodiments, from Colletotrichum aenigma (and can be associated with the NCBI Gene ID: 59244509 or a variant thereof), from Colletotrichum aenigma (and can be associated with the NCBI Gene ID: 59249666 or a variant thereof) or from Colletotrichum siamense (and can be associated with the NCBI Gene ID: 59275989 or a variant thereof). In some embodiments, the GPP2 is derived from a parvovirus and, in some embodiments, from the Artibeus jamaicensis parvovirus 1 (and can be associated with the NCBI Gene ID: 11605582 or a variant thereof) or the Eidolon helvum parvovirus (and can be associated with the NCBI Gene ID: 11763499 or a variant thereof). In some embodiments, the GPP2 is derived from Saccharomyces sp., and in further embodiments, from Saccharomyces paradoxus (and can be associated with the NCBI Gene ID: 54630122 or a variant thereof). In some embodiments, the GPP2 is derived from Nicotiana sp., and in further embodiments, from Nicotiana attenuate (and can be associated with the NCBI Gene ID: 109234217 or a variant thereof). In some embodiments, the GPP2 is derived from Arabidopsis sp., and in further embodiments, from Arabidopsis thaliana (and can be associated with the NCBI Gene ID: 835849 or a variant thereof). In some embodiments, the GPP2 is derived from Sugiyamaella sp., and in further embodiments, from Sugiyamaella lignohabitans (and can be associated with the NCBI Gene ID: 30035078 or a variant thereof).

[0001] The recombinant yeast host cell of the present disclosure can include, in some embodiments, an acetyl-coenzyme A synthetase. As used herein, the term “acetyl-coA synthetase” and “ACS” are intended to include the enzymes capable of converting acetate to acetyl-coA. Acetyl-coA synthetases include those enzymes that correspond to Enzyme Commission Number 6.2.1 .1 . The ACS can be native or heterologous to the recombinant yeast host cell. In other embodiments, the ACS can be encoded by a acs1 gene (e.g., ACS1) or a acs2 gene (e.g., ACS2). The ACS can be of prokaryotic origin (or a variant thereof). In some embodiments, the ACS is derived from Salmonella sp., and in further embodiments from Salmonella enterica. In such embodiments, the ACS can have the amino acid sequence ofSEQ ID NO: 138 or be a variant of the amino acid sequence of SEQ ID NO: 138 having ACS activity. The recombinant yeast host cell can include a heterologous nucleic acid molecule encoding the ACS. In such embodiment, the heterologous nucleic acid molecule can comprise the nucleic acid sequence of SEQ ID NO: 137 or a degenerate nucleic acid sequence encoding the amino acid sequence of SEQ ID NO: 138 (or a variant thereof). In some embodiments, the ACS is derived from Acetobacter sp., and in further embodiments from Acetobacter aceti. In such embodiments, the ACS can have the amino acid sequence of SEQ ID NO: 140 or be a variant of the amino acid sequence of SEQ ID NO: 140 having ACS activity. The recombinant yeast host cell can include a heterologous nucleic acid molecule encoding the ACS. In such embodiment, the heterologous nucleic acid molecule can comprise the nucleic acid sequence of SEQ ID NO: 139 or a degenerate nucleic acid sequence encoding the amino acid sequence of SEQ ID NO: 140 (or a variant thereof). In some embodiments, the ACS is derived from Escherichia sp., and in further embodiments from Escherichia coli. In such embodiments, the ACS can have the amino acid sequence of SEQ ID NO: 141 or be a variant of the amino acid sequence of SEQ ID NO: 141 having ACS activity. The recombinant yeast host cell can include a heterologous nucleic acid molecule encoding the ACS. In such embodiment, the heterologous nucleic acid molecule can comprise the nucleic acid sequence of SEQ ID NO: 142 or a degenerate nucleic acid sequence encoding the amino acid sequence of SEQ ID NO: 141 (a variant thereof or a fragment thereof). The ACS can be of eukaryotic origin (or a variant thereof). In some embodiments, the ACS is derived from Saccharomyces sp., and in further embodiments from Saccharomyces cerevisiae. In such embodiments, the ACS can have the amino acid sequence of SEQ ID NO: 132 or 134 or be a variant of the amino acid sequence of SEQ ID NO: 132 or 134 having ACS activity. The recombinant yeast host cell can include, a heterologous nucleic acid molecule encoding the ACS. In such embodiment, the heterologous nucleic acid molecule can comprise the nucleic acid sequence of SEQ ID NO: 131 or 133 or a degenerate nucleic acid sequence encoding the amino acid sequence of SEQ ID NO: 132 or134 (or a variant thereof). In some embodiments, the ACS is derived from Zygosaccharomyces sp., and in further embodiments from Zygosaccharomyces bailii. In such embodiments, the ACS can have the amino acid sequence of SEQ ID NO: 136 or be a variant of the amino acid sequence of SEQ ID NO: 136 having ACS activity. The recombinant yeast host cell can include a heterologous nucleic acid molecule encoding the ACS. In such embodiment, the heterologous nucleic acid molecule can comprise the nucleic acid sequence of SEQ ID NO:135 or a degenerate nucleic acid sequence encoding the amino acid sequence of SEQ ID NO:136 (or a variant thereof). Additional sources of ACS that can be included in the recombinant yeast host cell of the present disclosure include, without limitation, Aedes togoi, Aliivibrio fischeri, Amaranthus sp., Arabidopsis thaliana, Archaeoglobus fulgidus, Aspergillus nidulans, Aspergillus niger, Bacillus subtilis, Bos taurus, Bradyrhizobium japonicum, Cereibactersphaeroides, Cryptosporidium parvum, Dunaliella tertiolecta, Euglena gracilis, Haloarcula marismortui, Homo sapiens, Hordeum vulgare, Ignicoccus hospitalis, Marmota monax, Methanosarcina acetivorans, Methanosarcina sp., Methanothermobacterthermautotrophicus, Methanothrix soehngenii, Methanothrix thermoacetophila (Uniprot A0B8F1 for exemple), Moorella thermoacetica, Mus musculus, Mus musculus oryctolagus cuniculus, Ovis aries, Pelotomaculum thermopropionicum, Penicillium chrysogenum, Phycomyces blakesleeanus, Pinus radiata, Pisum sativum, Populus trichocarpa, Pseudomonas putida (Uniprot Q6EMJ3 for example), Pyrobaculum aerophilum, Pyrococcus furiosus, Rattus norvegicus, Rhodotorula diobovata, Roseovarius sp., Saccharopolyspora erythraea, Spinacia oleracea, Streptomyces lividans, Taxus sp., and Zea mays. Embodiments of heterologous genes encoding heterologous polypeptides having acetyl-coA synthetase activity as well as heterologous polypeptides having acetyl-coA synthetase activity are provided in US patent application 2022 / 0090045, US patent application 63 / 700,998 filed on September 30, 2024, PCT patent application PCT / BR2024 / 050302, and PCT patent application PCT / IB2024 / 060781 and are herewith incorporated in their entirety.To provide additional substrate to the PGI-PHK fusion polypeptide, the recombinant yeast host cell of the present disclosure includes / expresses a native and / or heterologous enzyme that functions in the engineered non-oxidative pentose phosphate pathway. In such embodiment, the recombinant yeast host cell of the present disclosure comprises at least one of: a transaldolase, a transketolase, an epimerase or an isomerase. In some embodiments, the transaldolase has the ability to convert glyceraldehyde 3-phosphate into erythrose 4- phosphate and / or has the ability to convert sedoheptulose 7-phosphate into fructose 6- phosphate. In some embodiments, the transaldolase is native or heterologous to the recombinant yeast host cell. The transaldolase can be native or heterologous. In some embodiments, the recombinant yeast host cell comprises both native and heterologous copies of one or more gene encoding the transaldolase. In additional embodiments, the transaldolase is of prokaryotic or eukaryotic origin. In some embodiments, the transaldolase is a TAL1 polypeptide which is encoded by a tall gene. In some additional embodiments, the transaldolase is derived from Saccharomyces sp.; and in further embodiments, is derived from Saccharomyces cerevisiae. In such embodiment, the transaldolase can have the amino acid sequence of SEQ ID NO: 154 (or be a variant thereof); and / or be encoded by a heterologous nucleic acid molecule comprising the nucleic acid molecule of SEQ ID NO: 153 or be a degenerate nucleic acid sequence encoding the amino acid sequence of SEQ ID NO: 154 (or a variant thereof). In some embodiments, the transketolase has the ability to convert ribose 5- phosphate into glyceraldehyde 3-phosphate, to convert fructose 6-phosphate into xylulose 5- phosphate; to convert xylulose 5-phoshate into sedoheptulose 7-phosphate; and / or to convert glyceraldehyde 3-phosphate into erythrose 4-phosphate. The transketolase can be native orheterologous. In some embodiments, the recombinant yeast host cell comprises both native and heterologous copies of one or more gene encoding the transketolase. The transketolase can be of prokaryotic or eukaryotic origin. In some embodiments, the transketolase is a TKL1 polypeptide which can be encoded by a tkl1 gene. In specific embodiments, the transketolase is derived from Saccharomyces sp., and, in further specific embodiments, is derived from Saccharomyces cerevisiae. In some embodiments, the transketolase can have the amino acid sequence of SEQ ID NO: 152 (or be a variant thereof). In additional embodiments, the transketolase is encoded by a heterologous nucleic acid molecule comprising the nucleic acid sequence of SEQ ID NO: 151 or is a degenerate nucleic acid sequence encoding the amino acid sequence of SEQ ID NO: 152 (or a variant thereof). In some embodiments, the epimerase has the ability to convert ribulose 5-phosphate into xylulose 5-phosphate, and / or the ability to convert xylulose 5-phosphate into ribulose 5-phosphate. In some embodiments, the epimerase is native or heterologous to the recombinant yeast host cell. In some additional embodiments, the recombinant yeast host cell comprises native and heterologous copies of the genes encoding the epimerase. In some embodiment, the epimerase is of prokaryotic or eukaryotic origin. In some specific embodiment, the epimerase is a RPE1 polypeptide which is encoded by a rpe1 gene. In some further embodiments, the epimerase is derived from Saccharomyces sp., and, in some specific embodiments, is derived from Saccharomyces cerevisiae. In some specific embodiments, the epimerase has the amino acid sequence of SEQ ID NO: 156 (or be a variant thereof). In some additional specific embodiments, the epimerase is encoded by a heterologous nucleic acid molecule comprising the nucleic acid of SEQ ID NO: 155 or is a degenerate nucleic acid sequence encoding the amino acid sequence of SEQ ID NO: 156 (or a variant thereof). In some embodiments, the isomerase: has the ability to convert ribulose 5- phosphate into ribose 5-phosphate, and / or the ability to convert ribose 5-phosphate into ribulose 5-phosphate. In some specific embodiments, the isomerase is native or heterologous to the recombinant yeast host cell. In some additional embodiments, the recombinant yeast host cell comprises native and heterologous copies of the gene encoding the isomerase. In some additional embodiments, the isomerase is of prokaryotic or eukaryotic origin. In some specific embodiments, the isomerase is a RKI1 polypeptide which is encoded by a rki1 gene. In some specific embodiments, the isomerase is derived from Saccharomyces sp., and, in some specific embodiments, is derived from Saccharomyces cerevisiae. In some additional embodiments, the isomerase has the amino acid sequence of SEQ ID NO: 158 (or be a variant thereof). In some further additional embodiments, the isomerase is encoded by a heterologous nucleic acid molecule comprising the nucleic acid sequence of SEQ ID NO: 157 or is a degenerate nucleic acid sequence encoding the amino acid sequence of SEQ ID NO: 158 (or a variant thereof). In further embodiments, the recombinant yeast host cell comprises at least two copies (per haploid genome) of the transaldolase, the transketolase, the epimerase, and / orthe isomerase. In additional embodiments, the recombinant yeast host cell comprises at least three copies (per haploid genome) of the transaldolase, the transketolase, the epimerase, and / or the isomerase. In yet further embodiments, the recombinant yeast host cell comprises the transaldolase, the transketolase, the epimerase, and the isomerase.To further increase the production of acetyl-coA in the recombinant yeast host cell, it is possible to increase the conversion of pantothenate into acetyl-coA. In some embodiments, the recombinant yeast host cell comprises native and heterologous copies of the polypeptides involved in the conversion of pantothenate into acetyl-coA. In such embodiment, the recombinant yeast host cell of the present disclosure comprises at least one of pantothenate symporter (for example FEN2 which can be encoded by the fen2 gene) or a pantothenate kinase (for example CAB1 which can be encoded by the cab1 gene). The FEN2 polypeptide is a plasma membrane proton-pantothenate symporter. The FEN2 polypeptide is classified in 2.A.1.14.18 in the Transporter Classification Database. Increasing the expression of a native and / or a heterologous fen2 gene is expected to increase intracellular entry of pantothenate and, ultimately, favor the conversion of pantothenate into acetyl-coA. The recombinant yeast host cell of the present disclosure can have native and heterologous copies of the fen2 gene encoding the FEN2 polypeptide. In some embodiments, the FEN2 polypeptide is derived from Saccharomyces sp., and, in some additional embodiment, is derived from Saccharomyces cerevisiae. In additional embodiments, the FEN2 polypeptide has the amino acid sequence of SEQ ID NO: 307 (or is a variant thereof). In further embodiments, the FEN2 polypeptide is encoded by a heterologous nucleic acid molecule comprising a degenerate nucleic acid sequence encoding the amino acid sequence of SEQ ID NO: 307 (or a variant thereof). As used in the context of the present disclosure, “panthotenate kinases” are enzymes capable of phosphorylating pantothenate into 4’-phosphopantothenate, a precursor of acetyl-coA. In some embodiments, the pantothenate kinase is the CAB1 polypeptide which is encoded by the cab1 gene. In some embodiments, the pantothenate kinase is native or heterologous to the recombinant yeast host cell. In some additional embodiments, the recombinant yeast host cell comprises native and heterologous copies of the gene encoding the pantothenate kinase. In some embodiments, the pantothenate kinase is of prokaryotic or eukaryotic origin. In yet additional embodiment, the pantothenate kinase is derived from Saccharomyces sp., and in some further embodiments, is derived from Saccharomyces cerevisiae. In specific embodiments, the pantothenate kinase has the amino acid sequence of SEQ ID NO: 308 (or is a variant thereof). In additional embodiments, the pantothenate kinase is encoded by a heterologous nucleic acid molecule comprising a degenerate nucleic acid sequence encoding the amino acid sequence of SEQ ID NO: 308 (or a variant thereof). In yet additional embodiments, the recombinant yeast host cell can comprise the FEN2 polypeptide. In yet further embodiments, the recombinant yeast host cell can comprise the CAB1 polypeptide. Instill additional embodiments, the recombinant yeast host cell can comprise the FEN2 and the CAB1 polypeptide.In some embodiments, the recombinant yeast host cell of the present disclosure can be used to generate acetone and / or isopropanol from acetyl-coA. In such embodiment, the recombinant yeast host cell can include additional genetic modifications for increasing the expression of heterologous polypeptides and / of decreasing the expression of native genes. These additional genetic modifications can be included in the recombinant yeast host cell to increase acetone and / or isopropanol production (when compared to a corresponding recombinant yeast host cell lacking these additional genetic modifications).In embodiments in which the recombinant yeast host cell is designed for acetone and / or isopropanol production, it can include at least one of a thiolase, a coenzyme A transferase or an acetoacetate decarboxylase. In another embodiment, the recombinant yeast host cell can include at least one of a thiolase, a HMG CoA synthase, a HMG CoA lyase or an acetoacetate decarboxylase. In still another embodiment, the recombinant yeast host cell can include at least one of a thiolase, acetoacetyl-CoA hydrolase or an acetoacetate decarboxylase.In some embodiments, the recombinant yeast host cell comprises / expresses a thiolase. As used herein, the terms "thiolase", “THL”, “ERG10” and "PHAA" are intended to include the enzymes capable of converting acetyl-coA into acetoacetyl-coA. Thiolases include enzymes that correspond to Enzyme Commission Number 2.3.1.9. The thiolase can be native or heterologous to the recombinant yeast host cell. The recombinant yeast host cell can include a native thiolase and optionally in combination a heterologous thiolase. In other embodiments, the thiolase can be encoded by a thl gene (e.g., THL), a erg10 gene (e.g., ERG10) or a phaA gene (e.g., PHAA). In some embodiments, the thiolase is of prokaryotic origin (or a variant thereof). In some embodiments, the thiolase is derived from Clostridium sp., and in further embodiments from Clostridium acetobutylicum. In such embodiments, the thiolase can have the amino acid sequence of SEQ ID NO: 162 or be a variant of the amino acid sequence of SEQ ID NO: 162 having thiolase activity. The recombinant yeast host cell can include a heterologous nucleic acid molecule encoding the thiolase. In such embodiment, the heterologous nucleic acid molecule can comprise the nucleic acid sequence of SEQ ID NO:161 or a degenerate nucleic acid sequence encoding the amino acid sequence of SEQ ID NO:162 (or a variant thereof). In some embodiments, the thiolase is from Clostridium kluyveri. In such embodiments, the thiolase can have the amino acid sequence of SEQ ID NO: 164 or be a variant of the amino acid sequence of SEQ ID NO: 164 having thiolase activity. The recombinant yeast host cell can include a heterologous nucleic acid molecule encoding the thiolase. In such embodiment, the heterologous nucleic acid molecule can comprise the nucleic acid sequence of SEQ ID NO: 163 or a degenerate nucleic acid sequence encodingthe amino acid sequence of SEQ ID NO: 164 (or a variant thereof or a fragment thereof). In some embodiments, the thiolase is derived from Clostridium beijerinckii. In such embodiments, the thiolase can have the amino acid sequence of SEQ ID NO: 180 or be a variant of the amino acid sequence of SEQ ID NO: 180 having thiolase activity. The recombinant yeast host cell can include a heterologous nucleic acid molecule encoding the thiolase. In such embodiment, the heterologous nucleic acid molecule can comprise the nucleic acid sequence of SEQ ID NO: 179 or a degenerate nucleic acid sequence encoding the amino acid sequence of SEQ ID NO: 180 (or a variant thereof). In some embodiments, the thiolase is derived from Cupriavidus sp., and in further embodiments from Cupriavidus necator. In such embodiments, the thiolase can have the amino acid sequence of SEQ ID NO: 166 or be a variant of the amino acid sequence of SEQ ID NO: 166. The recombinant yeast host cell can include a heterologous nucleic acid molecule encoding the thiolase. In such embodiment, the heterologous nucleic acid molecule can comprise the nucleic acid sequence of SEQ ID NO: 165 or a degenerate nucleic acid sequence encoding the amino acid sequence of SEQ ID NO: 166 (or a variant thereof). In some embodiments, the thiolase is derived from Yarrowia sp., and in further embodiments from Yarrowia lipolytica. In such embodiments, the thiolase can have the amino acid sequence of SEQ ID NO: 168 or be a variant of the amino acid sequence of SEQ ID NO: 168 having thiolase activity. The recombinant yeast host cell can include a heterologous nucleic acid molecule encoding the thiolase. In such embodiment, the heterologous nucleic acid molecule can comprise the nucleic acid sequence of SEQ ID NO: 167 or a degenerate nucleic acid sequence encoding the amino acid sequence of SEQ ID NO: 168 (or a variant thereof). In some embodiments, the thiolase is derived from Thermoanaerobacterium sp., and in further embodiments from Thermoanaerobacterium thermosaccharolyticum. In such embodiments, the thiolase can have the amino acid sequence of SEQ ID NO: 170 or be a variant of the amino acid sequence of SEQ ID NO: 170 having thiolase activity. The recombinant yeast host cell can include a heterologous nucleic acid molecule encoding the thiolase. In such embodiment, the heterologous nucleic acid molecule can comprise the nucleic acid sequence of SEQ ID NO: 169 or a degenerate nucleic acid sequence encoding the amino acid sequence of SEQ ID NO: 170 (or a variant thereof). In some embodiments, the thiolase is derived from Paenibacillus sp., and in further embodiments from Paenibacillus polymyxa. In such embodiments, the thiolase can have the amino acid sequence of SEQ ID NO: 176 or be a variant of the amino acid sequence of SEQ ID NO: 176 having thiolase activity. The recombinant yeast host cell can include a heterologous nucleic acid molecule encoding the thiolase. In such embodiment, the heterologous nucleic acid molecule can comprise the nucleic acid sequence of SEQ ID NO: 175 or a degenerate nucleic acid sequence encoding the amino acid sequence of SEQ ID NO: 176 (or a variant thereof). In some embodiments, the thiolase is of eukaryotic origin (or a variant thereof). In some embodiments, the thiolase isderived from Saccharomyces sp., and in further embodiments from Saccharomyces cerevisiae. In such embodiments, the thiolase can have the amino acid sequence of SEQ ID NO: 144 or be a variant of the amino acid sequence of SEQ ID NO: 144 having thiolase activity. The recombinant yeast host cell can include a heterologous nucleic acid molecule encoding the thiolase. In such embodiment, the heterologous nucleic acid molecule can comprise the nucleic acid sequence of SEQ ID NO: 143 or a degenerate nucleic acid sequence encoding the amino acid sequence of SEQ ID NO: 144 (or a variant thereof). In some embodiments, the thiolase is derived from Saccoglossus sp., and in further embodiments from Saccoglossus kowalevskii. In such embodiments, the thiolase can have the amino acid sequence of SEQ ID NO: 172 or be a variant of the amino acid sequence of SEQ ID NO: 172 having thiolase activity. The recombinant yeast host cell can include a heterologous nucleic acid molecule encoding the thiolase. In such embodiment, the heterologous nucleic acid molecule can comprise the nucleic acid sequence of SEQ ID NO: 171 or a degenerate nucleic acid sequence encoding the amino acid sequence of SEQ ID NO: 172 (or a variant thereof). In some embodiments, the thiolase is derived from Strongylocentrotus sp., and in further embodiments from Strongylocentrotus purpuratus. In such embodiments, the thiolase can have the amino acid sequence of SEQ ID NO: 174 or be a variant of the amino acid sequence of SEQ ID NO: 174 having thiolase activity. The recombinant yeast host cell can include a heterologous nucleic acid molecule encoding the thiolase. In such embodiment, the heterologous nucleic acid molecule can comprise the nucleic acid sequence of SEQ ID NO: 173 or a degenerate nucleic acid sequence encoding the amino acid sequence of SEQ ID NO: 174 (or a variant thereof). In some embodiments, the thiolase is derived from Zygosaccharomyces sp., and in further embodiments from Zygosaccharomyces bailii. In such embodiments, the thiolase can have the amino acid sequence of SEQ ID NO: 178 or be a variant of the amino acid sequence of SEQ ID NO: 178 having thiolase activity. The recombinant yeast host cell can include a heterologous nucleic acid molecule encoding the thiolase. In such embodiment, the heterologous nucleic acid molecule can comprise the nucleic acid sequence of SEQ ID NO: 177 or a degenerate nucleic acid sequence encoding the amino acid sequence of SEQ ID NO: 178 (or a variant thereof). Additional sources of thiolases that can be included in the recombinant yeast host cell include, without limitation, Arabidopsis thaliana (Uniprot Q8S4Y1 or Q9FIK7, for example), Aspergillus fumigatus (Uniprot B0XMC1 , for example), Bacillus subtilis, Bacopa monnieri (Uniprot D9U856, for example), Bos taurus, Bradyrhizobium japonicum, Candida tropicalis, Catharanthus roseus, Caulobacter vibrioides, Clonorchis sinensis (Uniprot G7YHN5, for example), Dictyostelium discoideum (Uniprot Q86AD9, for example), Enterococcus faecalis, Escherichia coli (Uniprot P76461 , for example), Euphorbia helioscopia (Uniprot A0A0M4F9H9, for example), Gallus gallus (Uniprot F1 NT20, for example), Ginkgo biloba (Uniprot A0A1 S6KJS1 , for example), Halobacterium sp., Haloferax mediterranei (Uniprot I3R3D1 ,I3R3D0, I3RA72 or I3RA71 , for example), Helianthus annuus (Uniprot D2IH11 , for example), Homo sapiens (Uniprot Q9BWD1 , for example), Medicago sativa (Uniprot D0EUY6, for example), Metallosphaera sedula (Uniprot A4YEH9, for example), Methanothermococcus thermolithotrophicus (Uniprot A0A384E138, for example), Mycolicibacterium smegmatis, Ostrinia scapulalis (Uniprot B7XEI5, for example), Pyricularia oryzae, Pyrobaculum neutrophilum (Uniprot B1YB71 , for example), Rattus norvegicus, Rhizobium sp., Sanghuangporus baumii, Thermus thermophilus, Vitis vinifera x Vitis riparia, and Zoogloea ramigera (Uniprot P07256 or P07097, for example).In some embodiments, the recombinant yeast host cell comprises / expresses a coenzyme A transferase. As used herein, the terms "coenzyme A transferase", “coA transferase”, “CTFA / CTFB”, and “ATOA / ATOD” are intended to include the enzymes (or enzyme moieties) capable of converting acetoacetyl-coA and acetate into acetyl-coA and acetoacetate. Coenzyme A transferases include enzymes that correspond to Enzyme Commission Number 2.8.3.8. The coA transferase can be a monomer or a dimer (as for example CTFA / CTFB). The coA transferase can be native or heterologous to the recombinant yeast host cell. The recombinant yeast host cell can include a native coA transferase and optionally in combination a heterologous coA transferase. In other embodiments, the coA transferase can be encoded by the ctfa and ctfb genes (e.g., CTFA / CTFB) or by the atoA and atoD genes (e.g., ATOA / ATOD).In some embodiments, the coA transferase is of prokaryotic origin (or a variant thereof). In some embodiments, the coA transferase is derived from Alkaliphilus sp., and in further embodiments from Alkaliphilus metalliredigens. In such embodiments, the coA transferase can include a first polypeptide (CTFA) having the amino acid sequence of SEQ ID NO: 146 or being a variant of the amino acid sequence of SEQ ID NO: 146 having coA transferase activity (in the presence of CTFB). The recombinant yeast host cell can include a heterologous nucleic acid molecule encoding the CTFA. In such embodiment, the heterologous nucleic acid molecule encoding this first polypeptide can comprise the nucleic acid sequence of SEQ ID NO: 145 or a degenerate nucleic acid sequence encoding the amino acid sequence of SEQ ID NO: 146 (or a variant thereof). Alternatively or in combination, the coA transferase can include a second polypeptide (CTFB) having the amino acid sequence of SEQ ID NO: 148 or being a variant of the amino acid sequence of SEQ ID NO: 148 having coA transferase activity (in the presence of CTFA). The recombinant yeast host cell can include a heterologous nucleic acid molecule encoding the CTFB. In such embodiment, the heterologous nucleic acid molecule encoding this second polypeptide can comprise the nucleic acid sequence of SEQ ID NO: 147 or a degenerate nucleic acid sequence encoding the amino acid sequence of SEQ ID NO: 148 (or a variant thereof). In some embodiments, the coA transferase is derived fromClostridium sp., and in further embodiments from Clostridium acetobutylicum. In such embodiments, the coA transferase can include a first polypeptide (CTFA) having the amino acid sequence of SEQ ID NO: 182 or being a variant of the amino acid sequence of SEQ ID NO: 182 having coA transferase activity (in the presence of CTFB). The recombinant yeast host cell can include, a heterologous nucleic acid molecule encoding the CTFA. In such embodiment, the heterologous nucleic acid molecule encoding this first polypeptide can comprise the nucleic acid sequence of SEQ ID NO: 181 or a degenerate nucleic acid sequence encoding the amino acid sequence of SEQ ID NO: 182 (or a variant thereof ). Alternatively or in combination, the coA transferase can include a second polypeptide (CTFB) having the amino acid sequence of SEQ ID NO: 184 or being a variant of the amino acid sequence of SEQ ID NO: 184 having coA transferase activity (in the presence of CTFA). The recombinant yeast host cell can include, a heterologous nucleic acid molecule encoding the CTFB. In such embodiment, the heterologous nucleic acid molecule encoding this second polypeptide can comprise the nucleic acid sequence of SEQ ID NO: 183 or a degenerate nucleic acid sequence encoding the amino acid sequence of SEQ ID NO: 184 (or a variant thereof). In some embodiments, the coA transferase is derived from Thermosipho sp., and in further embodiments from. In such embodiments, the coA transferase can include a first polypeptide (CTFA) having the amino acid sequence of SEQ ID NO: 186 or being a variant of the amino acid sequence of SEQ ID NO: 186 having coA transferase activity (in the presence of CTFB). The recombinant yeast host cell can include, a heterologous nucleic acid molecule encoding the CTFA. In such embodiment, the heterologous nucleic acid molecule encoding this first polypeptide can comprise the nucleic acid sequence of SEQ ID NO: 185 or a degenerate nucleic acid sequence encoding the amino acid sequence of SEQ ID NO: 186 (or a variant thereof). Alternatively or in combination, the coA transferase can include a second polypeptide (CTFB) having the amino acid sequence of SEQ ID NO: 188 or being a variant of the amino acid sequence of SEQ ID NO: 188 having coA transferase activity (in the presence of CTFA). The recombinant yeast host cell can include, a heterologous nucleic acid molecule encoding the CTFB. In such embodiment, the heterologous nucleic acid molecule encoding this second polypeptide can comprise the nucleic acid sequence of SEQ ID NO: 187 or a degenerate nucleic acid sequence encoding the amino acid sequence of SEQ ID NO: 188 (or a variant thereof). In some embodiments, the coA transferase is derived from Escherichia sp., and in further embodiments from Escherichia coll. In such embodiments, the coA transferase can include a first polypeptide (CTFA) having the amino acid sequence of SEQ ID NO: 190 or being a variant of the amino acid sequence of SEQ ID NO: 190 having coA transferase activity (in the presence of CTFB). The recombinant yeast host cell can include a heterologous nucleic acid molecule encoding the CTFA. In such embodiment, the heterologous nucleic acid molecule encoding this first polypeptide can comprise the nucleic acid sequence of SEQ IDNO: 189 or a degenerate nucleic acid sequence encoding the amino acid sequence of SEQ ID NO: 190 (or a variant thereof). Alternatively or in combination, the coA transferase can include a second polypeptide (CTFB) having the amino acid sequence of SEQ ID NO: 192 or being a variant of the amino acid sequence of SEQ ID NO: 192 having coA transferase activity (in the presence of CTFA).The recombinant yeast host cell can include a heterologous nucleic acid molecule encoding the CTFB. In such embodiment, the heterologous nucleic acid molecule encoding this second polypeptide can comprise the nucleic acid sequence of SEQ ID NO: 191 or a degenerate nucleic acid sequence encoding the amino acid sequence of SEQ ID NO: 192 (or a variant thereof). In some embodiments, the coA transferase is derived from Paenibacillus sp., and in further embodiments from Paenibacillus polymyxa. In such embodiments, the coA transferase can include a first polypeptide (CTFA) having the amino acid sequence of SEQ ID NO: 194 or being a variant of the amino acid sequence of SEQ ID NO: 194 having coA transferase activity (in the presence of CTFB). The recombinant yeast host cell can include a heterologous nucleic acid molecule encoding the CTFA. In such embodiment, the heterologous nucleic acid molecule encoding this first polypeptide can comprise the nucleic acid sequence of SEQ ID NO: 193 or a degenerate nucleic acid sequence encoding the amino acid sequence of SEQ ID NO: 194 (or a variant thereof). Alternatively or in combination, the coA transferase can include a second polypeptide (CTFB) having the amino acid sequence of SEQ ID NO: 196 or being a variant of the amino acid sequence of SEQ ID NO: 196 having coA transferase activity (in the presence of CTFA). The recombinant yeast host cell can include a heterologous nucleic acid molecule encoding the CTFB. In such embodiment, the heterologous nucleic acid molecule encoding this second polypeptide can comprise the nucleic acid sequence of SEQ ID NO: 195 or a degenerate nucleic acid sequence encoding the amino acid sequence of SEQ ID NO: 196 (or a variant thereof). In some embodiments, the coA transferase is derived from Clostridium sp., and in further embodiments from Clostridium beijerinckii. In such embodiments, the coA transferase can include a first polypeptide (CTFA) having the amino acid sequence of SEQ ID NO: 198 or being a variant of the amino acid sequence of SEQ ID NO: 198 having coA transferase activity (in the presence of CTFB). The recombinant yeast host cell can include a heterologous nucleic acid molecule encoding the CTFA. In such embodiment, the heterologous nucleic acid molecule encoding this first polypeptide can comprise the nucleic acid sequence of SEQ ID NO: 197 or a degenerate nucleic acid sequence encoding the amino acid sequence of SEQ ID NO: 198 (or a variant thereof). Alternatively or in combination, the coA transferase can include a second polypeptide (CTFB) having the amino acid sequence of SEQ ID NO: 200 or being a variant of the amino acid sequence of SEQ ID NO: 200 having coA transferase activity (in the presence of CTFA). The recombinant yeast host cell can include a heterologous nucleic acid molecule encoding the CTFB. In such embodiment, the heterologous nucleic acid molecule encodingthis second polypeptide can comprise the nucleic acid sequence of SEQ ID NO: 199 or a degenerate nucleic acid sequence encoding the amino acid sequence of SEQ ID NO: 200 (or a variant thereof). In some embodiments, the coA transferase is derived from Clostridium saccharoperbutylacetonicum. In such embodiments, the coA transferase can include a first polypeptide (CTFA) having the amino acid sequence of SEQ ID NO: 202 or being a variant of the amino acid sequence of SEQ ID NO: 202 having coA transferase activity (in the presence of CTFB). The recombinant yeast host cell can include, a heterologous nucleic acid molecule encoding the CTFA. In such embodiment, the heterologous nucleic acid molecule encoding this first polypeptide can comprise the nucleic acid sequence of SEQ ID NO: 201 or a degenerate nucleic acid sequence encoding the amino acid sequence of SEQ ID NO: 202 (or a variant thereof). Alternatively or in combination, the coA transferase can include a second polypeptide (CTFB) having the amino acid sequence of SEQ ID NO: 204 or being a variant of the amino acid sequence of SEQ ID NO: 204 having coA transferase activity (in the presence of CTFA). The recombinant yeast host cell can include, a heterologous nucleic acid molecule encoding the CTFB. In such embodiment, the heterologous nucleic acid molecule encoding this second polypeptide can comprise the nucleic acid sequence of SEQ ID NO: 203 or a degenerate nucleic acid sequence encoding the amino acid sequence of SEQ ID NO: 204 (or a variant thereof). In some embodiments, the coA transferase is derived from Clostridium sp., and in further embodiments from Clostridium sticklandii. In such embodiments, the coA transferase can include a first polypeptide (CTFA) having the amino acid sequence of SEQ ID NO: 206 or being a variant of the amino acid sequence of SEQ ID NO: 206 having coA transferase activity (in the presence of CTFB). The recombinant yeast host cell can include a heterologous nucleic acid molecule encoding the CTFA. In such embodiment, the heterologous nucleic acid molecule encoding this first polypeptide can comprise the nucleic acid sequence of SEQ ID NO: 205 or a degenerate nucleic acid sequence encoding the amino acid sequence of SEQ ID NO: 206 (or a variant thereof). Alternatively or in combination, the coA transferase can include a second polypeptide (CTFB) having the amino acid sequence of SEQ ID NO: 208 or being a variant of the amino acid sequence of SEQ ID NO: 208 having coA transferase activity (in the presence of CTFA). The recombinant yeast host cell can include a heterologous nucleic acid molecule encoding the CTFB. In such embodiment, the heterologous nucleic acid molecule encoding this second polypeptide can comprise the nucleic acid sequence of SEQ ID NO: 207 or a degenerate nucleic acid sequence encoding the amino acid sequence of SEQ ID NO: 208 (or a variant thereof). In some embodiments, the coA transferase is derived from Clostridium bovifaecis. In such embodiments, the coA transferase can include a first polypeptide (CTFA) having the amino acid sequence of SEQ ID NO: 214 or being a variant of the amino acid sequence of SEQ ID NO: 214 having coA transferase activity (in the presence of CTFB). The recombinant yeast host cell can include a heterologous nucleic acid moleculeencoding the CTFA. In such embodiment, the heterologous nucleic acid molecule encoding this first polypeptide can comprise the nucleic acid sequence of SEQ ID NO: 213 or a degenerate nucleic acid sequence encoding the amino acid sequence of SEQ ID NO: 214 (or a variant thereof). Alternatively or in combination, the coA transferase can include a second polypeptide (CTFB) having the amino acid sequence of SEQ ID NO: 216 or being a variant of the amino acid sequence of SEQ ID NO: 216 having coA transferase activity (in the presence of CTFA). The recombinant yeast host cell can include a heterologous nucleic acid molecule encoding the CTFB. In such embodiment, the heterologous nucleic acid molecule encoding this second polypeptide can comprise the nucleic acid sequence of SEQ ID NO: 215 or a degenerate nucleic acid sequence encoding the amino acid sequence of SEQ ID NO: 216 (or a variant thereof). In some embodiments, the coA transferase is derived from Brevibacill us sp., and in further embodiments from Brevibacillus laterosporus. In such embodiments, the coA transferase can include a first polypeptide (CTFA) having the amino acid sequence of SEQ ID NO: 210 or being a variant of the amino acid sequence of SEQ ID NO: 210 having coA transferase activity (in the presence of CTFB). The recombinant yeast host cell can include, a heterologous nucleic acid molecule encoding the CTFA. In such embodiment, the heterologous nucleic acid molecule encoding this first polypeptide can comprise the nucleic acid sequence of SEQ ID NO: 209 or a degenerate nucleic acid sequence encoding the amino acid sequence of SEQ ID NO: 210 (or a variant thereof). Alternatively or in combination, the coA transferase can include a second polypeptide (CTFB) having the amino acid sequence of SEQ ID NO: 212 or being a variant of the amino acid sequence of SEQ ID NO: 212 having coA transferase activity (in the presence of CTFA). The recombinant yeast host cell can include, a heterologous nucleic acid molecule encoding the CTFB. In such embodiment, the heterologous nucleic acid molecule encoding this second polypeptide can comprise the nucleic acid sequence of SEQ ID NO: 211 or a degenerate nucleic acid sequence encoding the amino acid sequence of SEQ ID NO: 212 (or a variant thereof). In some embodiments, the coA transferase is of eukaryotic origin (or a variant thereof). Additional sources of coA transferase that can be included in the recombinant yeast host cell include, without limitation, Acetobacter aceti (Uniprot B3EY95, for example), Anaerobutyricum hallii (Uniprot Q2QIH1 or D2WEY8, for example), Anaerostipes caccae (Uniprot Q2QB27 or B0MC58, for example), Butyricicoccus porcorum, Butyrivibrio fibrisolvens (Uniprot D2WEY7, for example), Coprococcus sp., Faecalibacterium prausnitzii (Uniprot Q2QIH0, A8SFP6, C7H5K4 or D2WEZ2, for example), Megasphaera elsdenii, Roseburia hominis (Uniprot Q2TME9, for example), Roseburia intestinalis (Uniprot C7GB37, for example), Roseburia inulinivorans (Uniprot D2WEY6, for example), Thermoanaerobacterium saccharolyticum, Trypanosoma brucei, Eubacterium nodatum, and Eubacterium rectale (Uniprot D2WEY1 , for example).In some embodiments, the recombinant yeast host cell of the present disclosure includes / expresses an acetoacetate decarboxylase. As used herein, the terms “acetoacetate decarboxylase”, and “ADC” are intended to include the enzymes capable of converting acetoacetate to acetone and carbon dioxide. Acetoacetate decarboxylases include enzymes that correspond to Enzyme Commission Number 4.1 .1 .4. The acetoacetate decarboxylase can be native or heterologous to the recombinant yeast host cell. The recombinant yeast host cell can include a native acetoacetate decarboxylase and optionally in combination a heterologous acetoacetate decarboxylase. In other embodiments, the acetoacetate decarboxylase can be encoded by an adc gene (e.g., ADC). In some embodiments, acetoacetate decarboxylase is of prokaryotic origin (or a variant thereof). In some embodiments, the acetoacetate decarboxylase is derived from Paenibacillus sp., and in further embodiments from Paenibacillus polymyxa. In such embodiments, the acetoacetate decarboxylase can include a polypeptide having the amino acid sequence of SEQ ID NO: 150 or 218 or being a variant of the amino acid sequence of SEQ ID NO: 150 or 218 having ADC activity. In such embodiment, the heterologous nucleic acid molecule encoding this polypeptide can comprise the nucleic acid sequence of SEQ ID NO: 149 or 217 or a degenerate nucleic acid sequence encoding the amino acid sequence of SEQ ID NO: 150 or 218 (or variants thereof). In some embodiments, the acetoacetate decarboxylase is derived from Clostridium sp., and in further embodiments from Clostridium acetobutylicum. In such embodiments, the acetoacetate decarboxylase can include a polypeptide having the amino acid sequence of SEQ ID NO: 220 or being a variant of the amino acid sequence of SEQ ID NO: 220 having ADC activity. The recombinant yeast host cell can include, a heterologous nucleic acid molecule encoding the ADC. In such embodiment, the heterologous nucleic acid molecule can comprise the nucleic acid sequence of SEQ ID NO: 219 or a degenerate nucleic acid sequence encoding the amino acid sequence of SEQ ID NO: 220 (or a variant thereof). In some embodiments, the acetoacetate decarboxylase is derived from Clostridium beijerinckii. In such embodiments, the acetoacetate decarboxylase can include a polypeptide having the amino acid sequence of SEQ ID NO: 222 or being a variant of the amino acid sequence of SEQ ID NO: 222 having ADC activity. The recombinant yeast host cell can include, a heterologous nucleic acid molecule encoding the ADC. In such embodiment, the heterologous nucleic acid molecule can comprise the nucleic acid sequence of SEQ ID NO: 221 or a degenerate nucleic acid sequence encoding the amino acid sequence of SEQ ID NO: 222 (or a variant thereof). In some embodiments, the acetoacetate decarboxylase is derived from Bacillus sp., and in further embodiments from Bacillus amyloliquefaciens. In such embodiments acetoacetate decarboxylase can include a polypeptide having the amino acid sequence of SEQ ID NO: 236 or being a variant of the amino acid sequence of SEQ ID NO: 236 having ADC activity. The recombinant yeast host cell can include, a heterologous nucleic acid molecule encoding the ADC. In such embodiment,the heterologous nucleic acid molecule can comprise the nucleic acid sequence of SEQ ID NO: 235 or a degenerate nucleic acid sequence encoding the amino acid sequence of SEQ ID NO: 236 (or a variant thereof). In some embodiments, the acetoacetate decarboxylase is derived from Rhizobium sp., and in further embodiments from Rhizobium leguminosarum. In such embodiment, the acetoacetate decarboxylase can include a polypeptide having the amino acid sequence of SEQ ID NO: 224 or being a variant of the amino acid sequence of SEQ ID NO: 224 having ADC activity. The recombinant yeast host cell can include, a heterologous nucleic acid molecule encoding the ADC. In such embodiment, the heterologous nucleic acid molecule can comprise the nucleic acid sequence of SEQ ID NO: 223 or a degenerate nucleic acid sequence encoding the amino acid sequence of SEQ ID NO: 224 (or a variant thereof). In some embodiments, the acetoacetate decarboxylase is derived from Bradyrhizobium sp., and in further embodiments from Bradyrhizobium japonicum. In such embodiments, the acetoacetate decarboxylase can include a polypeptide having the amino acid sequence of SEQ ID NO: 226 or being a variant of the amino acid sequence of SEQ ID NO: 226 having ADC activity. The recombinant yeast host cell can include, a heterologous nucleic acid molecule encoding the ADC. In such embodiment, the heterologous nucleic acid molecule can comprise the nucleic acid sequence of SEQ ID NO: 225 or a degenerate nucleic acid sequence encoding the amino acid sequence of SEQ ID NO: 226 (or a variant thereof). In some embodiments, the acetoacetate decarboxylase is derived from Lacticaseibacillus sp., and in further embodiments from Lacticaseibacillus easel. In such embodiments, the acetoacetate decarboxylase can include a polypeptide having the amino acid sequence of SEQ ID NO: 230 or being a variant of the amino acid sequence of SEQ ID NO: 230 having ADC activity. The recombinant yeast host cell can include a heterologous nucleic acid molecule encoding the ADC. In such embodiment, the heterologous nucleic acid molecule can comprise the nucleic acid sequence of SEQ ID NO: 229 or a degenerate nucleic acid sequence encoding the amino acid sequence of SEQ ID NO: 230 (or a variant thereof). In some embodiments, the acetoacetate decarboxylase is derived from Lacticaseibacillus sp., and in further embodiments from Lacticaseibacillus rhamnosus. In such embodiments, the acetoacetate decarboxylase can include a polypeptide having the amino acid sequence of SEQ ID NO: 232 or being a variant of the amino acid sequence of SEQ ID NO: 232 having ADC activity. The recombinant yeast host cell can include, a heterologous nucleic acid molecule encoding the ADC. In such embodiment, the heterologous nucleic acid molecule can comprise the nucleic acid sequence of SEQ ID NO: 231 or a degenerate nucleic acid sequence encoding the amino acid sequence of SEQ ID NO: 232 (or a variant thereof). In some embodiments, acetoacetate decarboxylase is of eukaryotic origin (or a variant thereof). In some embodiments, the acetoacetate decarboxylase is derived from Tetrahymena sp., and in further embodiments from Tetrahymena thermophila. In such embodiments, the acetoacetate decarboxylase can includea polypeptide having the amino acid sequence of SEQ ID NO: 238 or being a variant of the amino acid sequence of SEQ ID NO: 238 having ADC activity. The recombinant yeast host cell can include, a heterologous nucleic acid molecule encoding the ADC. In such embodiment, the heterologous nucleic acid molecule can comprise the nucleic acid sequence of SEQ ID NO: 237 or a degenerate nucleic acid sequence encoding the amino acid sequence of SEQ ID NO: 238 (or a variant thereof). In some embodiments, the acetoacetate decarboxylase is derived from Aspergillus sp., and in further embodiments from Aspergillus niger. In such embodiments, the acetoacetate decarboxylase can include a polypeptide having the amino acid sequence of SEQ ID NO: 228 or being a variant of the amino acid sequence of SEQ ID NO: 228 having ADC activity. The recombinant yeast host cell can include, a heterologous nucleic acid molecule encoding the ADC. In such embodiment, the heterologous nucleic acid molecule can comprise the nucleic acid sequence of SEQ ID NO: 227 or a degenerate nucleic acid sequence encoding the amino acid sequence of SEQ ID NO: 228 (or a variant thereof). In some embodiments, the acetoacetate decarboxylase is derived from Aspergillus bertholletiae. In such embodiments, the acetoacetate decarboxylase can include a polypeptide having the amino acid sequence of SEQ ID NO: 234 or being a variant of the amino acid sequence of SEQ ID NO: 234 having ADC activity. The recombinant yeast host cell can include, a heterologous nucleic acid molecule encoding the ADC. In such embodiment, the heterologous nucleic acid molecule can comprise the nucleic acid sequence of SEQ ID NO:233 or a degenerate nucleic acid sequence encoding the amino acid sequence of SEQ ID NO:234 (or a variant thereof). Additional sources of ADC that can be included in the recombinant yeast host cell include, without limitation, Chromobacterium violaceum (Uniprot Q7NSA6, for example), Pseudomonas putida, and Ruminiclostridium cellulolyticum.In some embodiments, the recombinant yeast host cell includes / expresses an HMG CoA synthase (HGMS). As used herein, the terms “HMG CoA synthase”, and “HMGS” are intended to include the enzymes capable of converting acetoacetyl-CoA and acetyl-coA into (S)-3- hydroxy-3-methylglutaryl-CoA (HMG-CoA). HMG CoA synthase include enzymes that correspond to Enzyme Commission Number 2.3.3.10. The HMG CoA synthase can be native or heterologous to the recombinant yeast host cell. The recombinant yeast host cell can include a native HMG CoA synthase and optionally in combination a heterologous HMG CoA synthase. In other embodiments, the HMG CoA synthase can be encoded by an hgms gene. In some embodiments, HMG CoA synthase is of prokaryotic origin (or a variant thereof). In some embodiments, the HMG CoA synthase is derived from Lacticaseibacillus sp., and in further embodiments from Lacticaseibacillus easel. In such embodiments, the HMG CoA synthase can include a polypeptide having the amino acid sequence of SEQ ID NO: 242 or being a variant of the amino acid sequence of SEQ ID NO: 242 having HMGS activity. In suchembodiment, the heterologous nucleic acid molecule encoding this polypeptide can comprise the nucleic acid sequence of SEQ ID NO: 241 ora degenerate nucleic acid sequence encoding the amino acid sequence of SEQ ID NO: 242 (or a variant thereof). In some embodiments, the HMG CoA synthase is derived from Enterococcus sp., and in further embodiments from Enterococcus faecalis. In such embodiments, the HMG CoA synthase can include a polypeptide having the amino acid sequence of SEQ ID NO: 244 or being a variant of the amino acid sequence of SEQ ID NO: 244 having HMGS activity. In such embodiment, the heterologous nucleic acid molecule encoding this polypeptide can comprise the nucleic acid sequence of SEQ ID NO: 243 or a degenerate nucleic acid sequence encoding the amino acid sequence of SEQ ID NO: 244 (or a variant thereof). In some embodiments, the HMG CoA synthase is derived from Haloferax sp., and in further embodiments from Haloferax volcanii. In such embodiments, the HMG CoA synthase can include a polypeptide having the amino acid sequence of SEQ ID NO: 246 or being a variant of the amino acid sequence of SEQ ID NO: 246 having HMGS activity. In such embodiment, the heterologous nucleic acid molecule encoding this polypeptide can comprise the nucleic acid sequence of SEQ ID NO: 245 or a degenerate nucleic acid sequence encoding the amino acid sequence of SEQ ID NO: 246 (or a variant thereof). In some embodiments, the HMG CoA synthase is derived from Alloscardovia sp., and in further embodiments from Alloscardovia theropitheci. In such embodiments, the HMG CoA synthase can include a polypeptide having the amino acid sequence of SEQ ID NO: 248 or being a variant of the amino acid sequence of SEQ ID NO: 248 having HMGS activity. In such embodiment, the heterologous nucleic acid molecule encoding this polypeptide can comprise the nucleic acid sequence of SEQ ID NO: 247 ora degenerate nucleic acid sequence encoding the amino acid sequence of SEQ ID NO: 248 (or a variant thereof). In some embodiments, the HMG CoA synthase is derived from Listeria sp., and in further embodiments from Listeria monocytogenes. In such embodiments, the HMG CoA synthase can include a polypeptide having the amino acid sequence of SEQ ID NO: 250 or being a variant of the amino acid sequence of SEQ ID NO: 250 having HMGS activity. In such embodiment, the heterologous nucleic acid molecule encoding this polypeptide can comprise the nucleic acid sequence of SEQ ID NO: 249 or a degenerate nucleic acid sequence encoding the amino acid sequence of SEQ ID NO: 250 (ora variant thereof). In some embodiments, HMG CoA synthase is of eukaryotic origin (or a variant thereof). In some embodiments, the HMG CoA synthase is derived from Saccharomyces sp., and in further embodiments from Saccharomyces cerevisiae. In such embodiments, the HMG CoA synthase can include a polypeptide having the amino acid sequence of SEQ ID NO: 240 or being a variant of the amino acid sequence of SEQ ID NO: 240 having HMGS activity. In such embodiment, the heterologous nucleic acid molecule encoding this polypeptide can comprise the nucleic acid sequence of SEQ ID NO:239 or a degenerate nucleic acid sequence encoding the amino acid sequence of SEQ ID NO:240 (or a variant thereof).In some embodiments, the recombinant yeast host cell includes / expresses an HMG CoA lyase (HMGCL). As used herein, the terms “HMG CoA lyase”, and “HMGCL” are intended to include the enzymes capable of converting HMG-CoA to acetyl-CoA and acetoacetate. HMG CoA lyase includes enzymes that correspond to Enzyme Commission Number 4.1.3.4. The HMG CoA lyase can be native or heterologous to the recombinant yeast host cell. The recombinant yeast host cell can include a native HMG CoA lyase and optionally in combination a heterologous HMG CoA lyase. In other embodiments, the HMG CoA lyase can be encoded by an hmgcl gene. In some embodiments, HMG CoA lyase is of prokaryotic origin (or a variant thereof). In some embodiments, the HMG CoA lyase is derived from Pseudomonas sp., and in further embodiments from Pseudomonas monteilii. In such embodiments, the HMG CoA lyase can include a polypeptide having the amino acid sequence of SEQ ID NO: 254 or being a variant of the amino acid sequence of SEQ ID NO: 254 having HMGCL activity. In such embodiment, the heterologous nucleic acid molecule encoding this polypeptide can comprise the nucleic acid sequence of SEQ ID NO: 253 or a degenerate nucleic acid sequence encoding the amino acid sequence of SEQ ID NO: 254 (or a variant thereof). In some embodiments, the HMG CoA lyase is derived from Pseudomonas wayambapalatensis. In such embodiments, the HMG CoA lyase can include a polypeptide having the amino acid sequence of SEQ ID NO: 256 or being a variant of the amino acid sequence of SEQ ID NO: 256 having HMGCL activity. In such embodiment, the heterologous nucleic acid molecule encoding this polypeptide can comprise the nucleic acid sequence of SEQ ID NO: 255 or a degenerate nucleic acid sequence encoding the amino acid sequence of SEQ ID NO: 256 (or a variant thereof). In some embodiments, the HMG CoA lyase is derived from Pseudomonas citronellolis. In such embodiments, the HMG CoA lyase can include a polypeptide having the amino acid sequence of SEQ ID NO: 260 or being a variant of the amino acid sequence of SEQ ID NO: 260 having HMGCL activity. In such embodiment, the heterologous nucleic acid molecule encoding this polypeptide can comprise the nucleic acid sequence of SEQ ID NO: 259 or a degenerate nucleic acid sequence encoding the amino acid sequence of SEQ ID NO: 260 (or a variant thereof). In some embodiments, the HMG CoA lyase is derived from Pseudomonas cremoris. In such embodiments, the HMG CoA lyase can include a polypeptide having the amino acid sequence of SEQ ID NO: 262 or being a variant of the amino acid sequence of SEQ ID NO: 262 having HMGCL activity. In such embodiment, the heterologous nucleic acid molecule encoding this polypeptide can comprise the nucleic acid sequence of SEQ ID NO: 261 or a degenerate nucleic acid sequence encoding the amino acid sequence of SEQ ID NO: 262 (or a variant thereof). In some embodiments, the HMG CoA lyase is derived from Pseudomonaschengduensis. In such embodiments, the HMG CoA lyase can include a polypeptide having the amino acid sequence of SEQ ID NO: 264 or being a variant of the amino acid sequence of SEQ ID NO: 264 having HMGCL activity. In such embodiment, the heterologous nucleic acid molecule encoding this polypeptide can comprise the nucleic acid sequence of SEQ ID NO:263 or a degenerate nucleic acid sequence encoding the amino acid sequence of SEQ ID NO:264 (or a variant thereof). In some embodiments, the HMG CoA lyase is derived from Pseudomonas aeruginosa. In such embodiments, the HMG CoA lyase can include a polypeptide having the amino acid sequence of SEQ ID NO: 266 or being a variant of the amino acid sequence of SEQ ID NO: 266 having HMGCL activity. In such embodiment, the heterologous nucleic acid molecule encoding this polypeptide can comprise the nucleic acid sequence of SEQ ID NO: 265 or a degenerate nucleic acid sequence encoding the amino acid sequence of SEQ ID NO: 265 (or a variant thereof or a fragment thereof). In some embodiments, the HMG CoA lyase is derived from Azotobacter sp., and in further embodiments from Azotobacter vinelandii. In such embodiments, the HMG CoA lyase can include a polypeptide having the amino acid sequence of SEQ ID NO: 258 or being a variant of the amino acid sequence of SEQ ID NO: 258 having HMGCL activity. In such embodiment, the heterologous nucleic acid molecule encoding this polypeptide can comprise the nucleic acid sequence of SEQ ID NO: 257 or a degenerate nucleic acid sequence encoding the amino acid sequence of SEQ ID NO: 258 (or a variant thereof). In some embodiments, the HMG CoA lyase is derived from Bacillus sp., and in further embodiments from Bacillus subtilis. In such embodiments, the HMG CoA lyase can include a polypeptide having the amino acid sequence of SEQ ID NO: 268 or being a variant of the amino acid sequence of SEQ ID NO: 268 having HMGCL activity. In such embodiment, the heterologous nucleic acid molecule encoding this polypeptide can comprise the nucleic acid sequence of SEQ ID NO: 267 or a degenerate nucleic acid sequence encoding the amino acid sequence of SEQ ID NO: 267 (or a variant thereof). In some embodiments, the HMG CoA lyase is derived from Desulfotomaculum sp., and in further embodiments from Desulfotomaculum arcticum. In such embodiments, the HMG CoA lyase can include a polypeptide having the amino acid sequence of SEQ ID NO: 270 or being a variant of the amino acid sequence of SEQ ID NO: 270 having HMGCL activity. In such embodiment, the heterologous nucleic acid molecule encoding this polypeptide can comprise the nucleic acid sequence of SEQ ID NO: 269 or a degenerate nucleic acid sequence encoding the amino acid sequence of SEQ ID NO: 270 (or a variant thereof). In some embodiments, the HMG CoA lyase is derived from Desulfoscipio sp., and in further embodiments from Desulfoscipio geothermicus. In such embodiments, the HMG CoA lyase can include a polypeptide having the amino acid sequence of SEQ ID NO: 272 or being a variant of the amino acid sequence of SEQ ID NO: 272 having HMGCL activity. In such embodiment, the heterologous nucleic acid molecule encoding this polypeptide can comprise the nucleic acidsequence of SEQ ID NO: 271 or a degenerate nucleic acid sequence encoding the amino acid sequence of SEQ ID NO: 272 (or a variant thereof). In some embodiments, the HMG CoA lyase is derived from Acinetobacter sp., and in further embodiments from Acinetobacter baumannii. In such embodiments, the HMG CoA lyase can include a polypeptide having the amino acid sequence of SEQ ID NO: 274 or being a variant of the amino acid sequence of SEQ ID NO: 274 having HMGCL activity. In such embodiment, the heterologous nucleic acid molecule encoding this polypeptide can comprise the nucleic acid sequence of SEQ ID NO:273 or a degenerate nucleic acid sequence encoding the amino acid sequence of SEQ ID NO:274 (or a variant thereof). In some embodiments, the HMG CoA lyase is derived from from Acinetobacter Iwoffii. In such embodiments, the HMG CoA lyase can include a polypeptide having the amino acid sequence of SEQ ID NO: 276 or being a variant of the amino acid sequence of SEQ ID NO: 276 having HMGCL activity. In such embodiment, the heterologous nucleic acid molecule encoding this polypeptide can comprise the nucleic acid sequence of SEQ ID NO: 275 or a degenerate nucleic acid sequence encoding the amino acid sequence of SEQ ID NO: 276 (or a variant thereof). In some embodiments, the HMG CoA lyase is derived from Moraxella sp., and in further embodiments from Moraxella caviae. In such embodiments, the HMG CoA lyase can include a polypeptide having the amino acid sequence of SEQ ID NO: 278 or be a variant of the amino acid sequence of SEQ ID NO: 278 having HMGCL activity. In such embodiment, the heterologous nucleic acid molecule encoding this polypeptide can comprise the nucleic acid sequence of SEQ ID NO: 277 or a degenerate nucleic acid sequence encoding the amino acid sequence of SEQ ID NO: 278 (or a variant thereof). In some embodiments, the HMG CoA lyase is derived from Alcaligenaceae sp.. In such embodiments, the HMG CoA lyase can include a polypeptide having the amino acid sequence of SEQ ID NO: 280 or be a variant of the amino acid sequence of SEQ ID NO: 280 having HMGCL activity. In such embodiment, the heterologous nucleic acid molecule encoding this polypeptide can comprise the nucleic acid sequence of SEQ ID NO: 279 or a degenerate nucleic acid sequence encoding the amino acid sequence of SEQ ID NO: 280 (or a variant thereof). In some embodiments, HMG CoA lyase is of eukaryotic origin (or a variant thereof). In some embodiments, the HMG CoA lyase is derived from Danio sp., and in further embodiments from Danio rerio. In such embodiments, the HMG CoA lyase can include a polypeptide having the amino acid sequence of SEQ ID NO: 252 or being a variant of the amino acid sequence of SEQ ID NO: 252 having HMGCL activity. In such embodiment, the heterologous nucleic acid molecule encoding this polypeptide can comprise the nucleic acid sequence of SEQ ID NO:251 or a degenerate nucleic acid sequence encoding the amino acid sequence of SEQ ID NO:252 (or a variant thereof). In some embodiments, the HMG CoA lyase is derived from Macaca sp., and in further embodiments from Macaca fascicularis. In such embodiments, the HMG CoA lyase can include a polypeptide having the amino acid sequence of SEQ ID NO: 282 orbe a variant of the amino acid sequence of SEQ ID NO: 282 having HMGCL activity. In such embodiment, the heterologous nucleic acid molecule encoding this polypeptide can comprise the nucleic acid sequence of SEQ ID NO: 281 or a degenerate nucleic acid sequence encoding the amino acid sequence of SEQ ID NO: 282 (or a variant thereof). In some embodiments, the HMG CoA lyase is derived from Arabidopsis sp., and in further embodiments from Arabidopsis thaliana. In such embodiments, the HMG CoA lyase can include a polypeptide having the amino acid sequence of SEQ ID NO: 284 or be a variant of the amino acid sequence of SEQ ID NO: 284 having HMGCL activity. In such embodiment, the heterologous nucleic acid molecule encoding this polypeptide can comprise the nucleic acid sequence of SEQ ID NO:283 or a degenerate nucleic acid sequence encoding the amino acid sequence of SEQ ID NO:284 (or a variant thereof). In some embodiments, the HMG CoA lyase is derived from Gallus sp., and in further embodiments from Gallus gallus. In such embodiments, the HMG CoA lyase can include a polypeptide having the amino acid sequence of SEQ ID NO: 286 or be a variant of the amino acid sequence of SEQ ID NO: 286 having HMGCL activity. In such embodiment, the heterologous nucleic acid molecule encoding this polypeptide can comprise the nucleic acid sequence of SEQ ID NO: 285 or a degenerate nucleic acid sequence encoding the amino acid sequence of SEQ ID NO: 286 (or a variant thereof).In some embodiments, the recombinant yeast host cell includes / expresses an acetoacetyl- CoA hydrolase. As used herein, the terms “acetoacetyl-CoA hydrolase”, “thioesterase”, “TESB”, “YCIA”, “FADM1 ”, “FADM2” and “FADM” are intended to include the enzymes capable of converting acetoacetyl-CoA to acetyl-coA and acetoacetate. Acetoacetyl-CoA hydrolase includes enzymes that correspond to Enzyme Commission Number EC 3.1.2.11. The acetoacetyl-CoA hydrolase can be native or heterologous to the recombinant yeast host cell. The recombinant yeast host cell can include a native acetoacetyl-CoA hydrolase and optionally in combination a heterologous acetoacetyl-CoA hydrolase. In other embodiments, the acetoacetyl-CoA hydrolase can be encoded by a tesB”, “yciA”, “fad / VH”, “fadM2” or “fadM gene. In some embodiments, the acetoacetyl-CoA hydrolase is of prokaryotic origin (or a variant thereof). In some embodiments, the acetoacetyl-CoA hydrolase is derived from Escherichia sp., and in further embodiments from Escherichia coll. In such embodiments, the acetoacetyl- CoA hydrolase (TESB) can include a polypeptide having the amino acid sequence of SEQ ID NO: 287, 298, 299 or 300 or be a variant of the amino acid sequence of SEQ ID NO: 287, 298, 299 or 300 having acetoacetyl-CoA hydrolase activity. The recombinant yeast host cell can include, a heterologous nucleic acid molecule encoding the acetoacetyl-CoA hydrolase. In such embodiment, the heterologous nucleic acid molecule encoding this polypeptide can comprise a degenerate nucleic acid sequence encoding the amino acid sequence of SEQ ID NO: 287, 298, 299 or 300 (or variants thereof). In some embodiments, the acetoacetyl-CoAhydrolase is derived from Methylorubrum sp., and in further embodiments from Methylorubrum extorquens. In such embodiments, the acetoacetyl-CoA hydrolase can include a polypeptide having the amino acid sequence of SEQ ID NO: 288 or be a variant of the amino acid sequence of SEQ ID NO: 288 having acetoacetyl-CoA hydrolase activity. The recombinant yeast host cell can include, a heterologous nucleic acid molecule encoding the acetoacetyl-CoA hydrolase. In such embodiment, the heterologous nucleic acid molecule encoding this polypeptide can comprise a degenerate nucleic acid sequence encoding the amino acid sequence of SEQ ID NO: 288 (or a variant thereof). In some embodiments, the acetoacetyl-CoA hydrolase is derived from Pseudomonas sp., and in further embodiments from Pseudomonas aeruginosa. In such embodiments, the acetoacetyl-CoA hydrolase can include a polypeptide having the amino acid sequence of SEQ ID NO: 289 or be a variant of the amino acid sequence of SEQ ID NO: 289 having acetoacetyl-CoA hydrolase activity. The recombinant yeast host cell can include, a heterologous nucleic acid molecule encoding the acetoacetyl-CoA hydrolase. In such embodiment, the heterologous nucleic acid molecule encoding this polypeptide can comprise a degenerate nucleic acid sequence encoding the amino acid sequence of SEQ ID NO: 289 (or a variant thereof). In some embodiments, the acetoacetyl-CoA hydrolase is derived from Pseudomonas putida. In such embodiments, the acetoacetyl-CoA hydrolase can include a polypeptide having the amino acid sequence of SEQ ID NO: 292 or be a variant of the amino acid sequence of SEQ ID NO: 292 having acetoacetyl-CoA hydrolase activity. The recombinant yeast host cell can include, a heterologous nucleic acid molecule encoding the acetoacetyl-CoA hydrolase. In such embodiment, the heterologous nucleic acid molecule encoding this polypeptide can comprise a degenerate nucleic acid sequence encoding the amino acid sequence of SEQ ID NO: 292 (or a variant thereof). In some embodiments, the acetoacetyl-CoA hydrolase is derived from Campylobacter sp., and in further embodiments from Campylobacter jejuni. In such embodiments, the acetoacetyl-CoA hydrolase can include a polypeptide having the amino acid sequence of SEQ ID NO: 290 or 297 or be a variant of the amino acid sequence of SEQ ID NO: 290 or 297 having acetoacetyl-CoA hydrolase activity. The recombinant yeast host cell can include, a heterologous nucleic acid molecule encoding the acetoacetyl-CoA hydrolase. In such embodiment, the heterologous nucleic acid molecule encoding this polypeptide can comprise a degenerate nucleic acid sequence encoding the amino acid sequence of SEQ ID NO: 290 or 297 (or variants thereof). In some embodiments, the acetoacetyl-CoA hydrolase is derived from Mycobacterium sp., and in further embodiments from Mycobacterium tuberculosis. In such embodiments, the acetoacetyl-CoA hydrolase can include a polypeptide having the amino acid sequence of SEQ ID NO: 291 or be a variant of the amino acid sequence of SEQ ID NO: 291 having acetoacetyl-CoA hydrolase activity. The recombinant yeast host cell can include, a heterologous nucleic acid molecule encoding the acetoacetyl-CoA hydrolase. In such embodiment, the heterologous nucleic acid moleculeencoding this polypeptide can comprise a degenerate nucleic acid sequence encoding the amino acid sequence of SEQ ID NO: 291 (or a variant thereof). In some embodiments, the acetoacetyl-CoA hydrolase is derived from Fibrobacter sp., and in further embodiments from Fibrobacter succinogenes. In such embodiments, the acetoacetyl-CoA hydrolase can include a polypeptide having the amino acid sequence of SEQ ID NO: 293 or be a variant of the amino acid sequence of SEQ ID NO: 293 having acetoacetyl-CoA hydrolase activity. The recombinant yeast host cell can include, a heterologous nucleic acid molecule encoding the acetoacetyl- CoA hydrolase. In such embodiment, the heterologous nucleic acid molecule encoding this polypeptide can comprise a degenerate nucleic acid sequence encoding the amino acid sequence of SEQ ID NO: 293 (or a variant thereof). In some embodiments, the acetoacetyl- CoA hydrolase is derived from Alcanivorax sp., and in further embodiments from Alcanivorax borkumensis. In such embodiments, the acetoacetyl-CoA hydrolase can include a polypeptide having the amino acid sequence of SEQ ID NO: 294 or be a variant of the amino acid sequence of SEQ ID NO: 294 having acetoacetyl-CoA hydrolase activity. The recombinant yeast host cell can include, a heterologous nucleic acid molecule encoding the acetoacetyl-CoA hydrolase. In such embodiment, the heterologous nucleic acid molecule encoding this polypeptide can comprise a degenerate nucleic acid sequence encoding the amino acid sequence of SEQ ID NO: 294 (or a variant thereof). In some embodiments, the acetoacetyl-CoA hydrolase is derived from Haemophilus sp., and in further embodiments from Haemophilus influenzae. In such embodiments, the acetoacetyl-CoA hydrolase can include a polypeptide having the amino acid sequence of SEQ ID NO: 295 or be a variant of the amino acid sequence of SEQ ID NO: 295 having acetoacetyl-CoA hydrolase activity. The recombinant yeast host cell can include, a heterologous nucleic acid molecule encoding the acetoacetyl-CoA hydrolase. In such embodiment, the heterologous nucleic acid molecule encoding this polypeptide can comprise a degenerate nucleic acid sequence encoding the amino acid sequence of SEQ ID NO: 295 (or a variant thereof). In some embodiments, the acetoacetyl-CoA hydrolase is derived from Zymomonas sp., and in further embodiments from Zymomonas mobilis, and in still further embodiments, from Zymomonas mobilis subsp. mobilis. In such embodiments, the acetoacetyl-CoA hydrolase can include a polypeptide having the amino acid sequence of SEQ ID NO: 296 or be a variant of the amino acid sequence of SEQ ID NO: 296 having acetoacetyl- CoA hydrolase activity. The recombinant yeast host cell can include, a heterologous nucleic acid molecule encoding the acetoacetyl-CoA hydrolase. In such embodiment, the heterologous nucleic acid molecule encoding this polypeptide can comprise a degenerate nucleic acid sequence encoding the amino acid sequence of SEQ ID NO: 296 (or a variant thereof). In some embodiments, the acetoacetyl-CoA hydrolase is derived from Prevotella sp., and in further embodiments from Prevotella ruminicola. In such embodiments, the acetoacetyl-CoA hydrolase (FadM1) can include a polypeptide having the amino acid sequence of SEQ ID NO:301 or be a variant of the amino acid sequence of SEQ ID NO: 301 having acetoacetyl-CoA hydrolase activity. The recombinant yeast host cell can include, a heterologous nucleic acid molecule encoding the acetoacetyl-CoA hydrolase. In such embodiment, the heterologous nucleic acid molecule encoding this polypeptide can comprise a degenerate nucleic acid sequence encoding the amino acid sequence of SEQ ID NO: 301 (or a variant thereof). In additional embodiments, the acetoacetyl-CoA hydrolase (FadM2) can include a polypeptide having the amino acid sequence of SEQ ID NO: 302 or be a variant of the amino acid sequence of SEQ ID NO: 302 having acetoacetyl-CoA hydrolase activity. The recombinant yeast host cell can include, a heterologous nucleic acid molecule encoding the acetoacetyl-CoA hydrolase. In such embodiment, the heterologous nucleic acid molecule encoding this polypeptide can comprise a degenerate nucleic acid sequence encoding the amino acid sequence of SEQ ID NO: 302 (or a variant thereof). In some embodiments, the acetoacetyl-CoA hydrolase is derived from Providencia sp., and in further embodiments from Providencia sneebia. In such embodiments, the acetoacetyl-CoA hydrolase can include a polypeptide having the amino acid sequence of SEQ ID NO: 303 or be a variant of the amino acid sequence of SEQ ID NO: 303 having acetoacetyl-CoA hydrolase activity. The recombinant yeast host cell can include, a heterologous nucleic acid molecule encoding the acetoacetyl-CoA hydrolase. In such embodiment, the heterologous nucleic acid molecule encoding this polypeptide can comprise a degenerate nucleic acid sequence encoding the amino acid sequence of SEQ ID NO: 303 (or a variant thereof). In some embodiments, the acetoacetyl-CoA hydrolase is of eukaryotic origin (or a variant thereof).In embodiments in which it is preferred that the recombinant yeast host cell produces more acetone and less isopropanol, the recombinant yeast host cell can be engineered to have a downregulated native alcohol dehydrogenase (ADH) gene in combination with a heterologous alcohol dehydrogenase (ADH) gene, wherein the native ADH is capable of converting acetone to isopropanol and the heterologous alcohol dehydrogenase has a decreased activity in the conversion of the acetone to isopropanol when compared to the native ADH intended for downregulation in the recombinant yeast host cell.In embodiments in which it is preferred that the recombinant yeast host cell produces more acetone and less isopropanol, the recombinant yeast host cell can be engineered to have a downregulated native alcohol dehydrogenase (ADH) gene, wherein the native ADH is capable of converting acetone to isopropanol. The term "downregulated" means decreased in activity, e.g., decrease in enzymatic activity of the enzyme as compared to activity in a native host organism. As used in the context of the present disclosure, the downregulation of the native adh gene refers to a genetic modification which limits or impedes the expression of the native adh gene, when compared to a corresponding yeast strain which does not bear such geneticmodification. In some instances, the downregulation reduces but still allows the expression of the native adh gene and / or the expression of the native ADH. In other instances, the downregulation inhibits the expression of the native adh gene and / or the expression of the native ADH. The downregulation could be done by the known methods in the art, as for example by deletion of the native adh gene, inactivation of the adh gene by insertion or deletion of nucleic acids residues, replacement of the native promoter by a heterologous promoter less active or that does not activate under propagation and / or fermentation conditions or by modulation of a gene regulating the expression of the native adh gene. In one embodiment, the genetic modification for downregulating the native adh gene is a deletion of the native adh gene. In one embodiment the native ADH is the native ADH that is mainly responsible for the conversion of the acetone to isopropanol by the yeast host cell. In another embodiment, the native ADH is ADH1 (encoded by the adh1 gene). In another embodiment, the native ADH1 is encoded by the native adh1 gene from S. cerevisiae. Embodiments of such down regulation of the adh gene are disclosed in PCT patent application PCT / IB2024 / 060781 , filed on October 30, 2024 and are incorporated herewith in their entirety.In embodiments in which the recombinant yeast host cell has a downregulated native alcohol dehydrogenase (ADH) gene, the recombinant yeast host cell also comprises a heterologous ADH. The heterologous alcohol dehydrogenase has a decreased activity in the conversion of the acetone to isopropanol when compared to the native ADH intended for downregulation in the recombinant yeast host cell. In one embodiment, the heterologous alcohol dehydrogenase has a secondary alcohol activity inferior to the secondary alcohol activity of the native ADH intended for the downregulation in the yeast host cell. In another embodiment, the heterologous ADH allows the recombinant yeast host cell comprising a) an engineered metabolic pathway to convert acetyl-CoA and acetate to acetone and b) a downregulated ADH to produce a yield of isopropanol inferior to 0.5 g / L in a YPD media containing 120 g / L glucose at pH 6.0 following 48 hours of fermentation. In one embodiment, the heterologous ADH is a bacterial ADH. In other embodiments, the heterologous ADH can be encoded by an adha, adhp or adh4, gene. In a further embodiment, the heterologous ADH is not a S. cerevisiae ADH 1 or is not encoded by a S. cerevisiae adh1 gene. In some embodiments, the heterologous ADH is derived from Zymomonas sp., and in further embodiments from Zymomonas mobilis. In such embodiments, the heterologous ADH (ADHA) can include a polypeptide having the amino acid sequence of SEQ ID NO: 304 or be a variant of the amino acid sequence of SEQ ID NO: 304 having ADH activity. The recombinant yeast host cell can include, a heterologous nucleic acid molecule encoding the heterologous ADH. In such embodiment, the heterologous nucleic acid molecule encoding this polypeptide can comprise a degenerate nucleic acid sequence encoding the amino acid sequence of SEQ ID NO: 304 (or a variant thereof). In some embodiments, the heterologous ADH is derived from Zymomonas sp., and in furtherembodiments from Zymomonas mobilis. In such embodiments, the heterologous ADH (ADHP) can include a polypeptide having the amino acid sequence of SEQ ID NO: 305 or be a variant of the amino acid sequence of SEQ ID NO: 305 having ADH activity. The recombinant yeast host cell can include, a heterologous nucleic acid molecule encoding the heterologous ADH. In such embodiment, the heterologous nucleic acid molecule encoding this polypeptide can comprise a degenerate nucleic acid sequence encoding the amino acid sequence of SEQ ID NO: 305 (or a variant thereof). In some embodiments, the heterologous ADH is derived from Saccharomyces sp., and in further embodiments from Saccharomyces cerevisiae. In such embodiments, the heterologous ADH (ADH4) can include a polypeptide having the amino acid sequence of SEQ ID NO: 306 or be a variant of the amino acid sequence of SEQ ID NO: 306 having ADH activity. The recombinant yeast host cell can include, a heterologous nucleic acid molecule encoding the heterologous ADH. In such embodiment, the heterologous nucleic acid molecule encoding this polypeptide can comprise a degenerate nucleic acid sequence encoding the amino acid sequence of SEQ ID NO: 306 (or a variant). Embodiments of such heterologous adh gene are disclosed in PCT patent application PCT / IB2024 / 060781 , filed on October 30, 2024 and are incorporated herewith in their entirety.In some embodiments, the recombinant yeast host cell of the present disclosure can be used to generate farnesene from acetyl-coA. In such embodiment, the recombinant yeast host cell can include / express at least one of a NADPH or NADH-dependent 3-hydroxy-3-methylglutaryl coenzyme-A (HMG-CoA) reductase (like HMG1 , HMG2 or HMGR for example) or a farnese synthase. In an embodiment, the 3-hydroxy-3-methylglutaryl coenzyme-A (HMG-CoA) reductase is native or heterologous to the recombinant yeast host cell. In some specific embodiment, the recombinant yeast host cell comprises native and heterologous copies of the 3-hydroxy-3-methylglutaryl coenzyme-A (HMG-CoA) reductase. In an embodiment, the farnesene synthase is native or heterologous to the recombinant yeast host cell. In some specific embodiment, the recombinant yeast host cell comprises native and heterologous copies of the farnesene synthase. Embodiments of recombinant yeast host cells capable of generating farnesene are disclosed in Meadows et al., 2016, which is incorporated herewith in its entirety.In some embodiments, the recombinant yeast host cell of the present disclosure can be used to generate 3-hydroxy-propionic acid from acetyl-coA. In such embodiment, the recombinant yeast host cell can include / express at least one of an acetyl-coA carboxylase (like ACC1 for example) or a malonyl-CoA reductase (MCR). In some embodiments, the recombinant yeast host cell can include / express at least one of an acetyl-coA carboxylase (like ACC1 for example) and a malonyl-CoA reductase (MCR). In some embodiments, the acetyl-coA carboxylase is native or heterologous to the recombinant yeast host cell. In some additional embodiments,the recombinant yeast host cell comprises native and heterologous copies of the gene encoding the acetyl-coA carboxylase. In some embodiments, the malonyl-CoA reductase is native or heterologous to the recombinant yeast host cell. In some additional embodiments, the recombinant yeast host cell comprises native and heterologous copies of the gene encoding the malonyl-CoA reductase. Embodiments of recombinant yeast host cells capable of generating 3-hydroxy-propionic acid are disclosed in Qin et al., 2020, and Hellgren et al., 2020 which are both incorporated herewith in their entirety.In some embodiments, the recombinant yeast host cell of the present disclosure can be used to generate polyhydroxybutyrate from acetyl-coA. In some embodiments, the recombinant yeast host cell can include / express at least one of a beta-ketothiolase (PHAA / ERG10), NADPH-dependent acetoacetyl-CoA reductase (PHAB) or polyhydroxyalkanoate synthase (PHAC). In some embodiments, the beta-ketothiolase is native or heterologous to the recombinant yeast host cell. In some additional embodiments, the recombinant yeast host cell comprises native and heterologous copies of the gene encoding the beta-ketothiolase. In some embodiments, the NADPH-dependent acetoacetyl-CoA reductase is native or heterologous to the recombinant yeast host cell. In some additional embodiments, the recombinant yeast host cell comprises native and heterologous copies of the gene encoding the NADPH-dependent acetoacetyl-CoA reductase. In some embodiments, the polyhydroxyalkanoate synthase is native or heterologous to the recombinant yeast host cell. In some additional embodiments, the recombinant yeast host cell comprises native and heterologous copies of the gene encoding the polyhydroxyalkanoate synthase. Embodiments of recombinant yeast host cells capable of generating poly hydroxy butyrate are disclosed in Kocharin et al., 2013, which is incorporated herewith in its entirety.In some embodiments, the recombinant yeast host cell of the present disclosure can be used to generate carotenoid from acetyl-coA. In some embodiments, the recombinant yeast host cell can include / express at least one of a truncated HMG CoA reductase (tHMG1), geranylgeranyl diphosphate synthase (CRTE), phytoene synthase (CRTB) or phytoene desaturase (CRTI). In some embodiments, the truncated HMG CoA reductase is native or heterologous to the recombinant yeast host cell. In some additional embodiments, the recombinant yeast host cell comprises native and heterologous copies of the gene encoding the truncated HMG CoA reductase. In some embodiments, the geranylgeranyl diphosphate synthase is native or heterologous to the recombinant yeast host cell. In some additional embodiments, the recombinant yeast host cell comprises native and heterologous copies of the gene encoding the geranylgeranyl diphosphate synthase. In some embodiments, the phytoene synthase is native or heterologous to the recombinant yeast host cell. In some additional embodiments, the recombinant yeast host cell comprises native and heterologouscopies of the gene encoding the phytoene synthase. In some embodiments, the phytoene desaturase is native or heterologous to the recombinant yeast host cell. In some additional embodiments, the recombinant yeast host cell comprises native and heterologous copies of the gene encoding the phytoene desaturase. Embodiments of recombinant yeast host cells capable of generating carotenoids are disclosed in Su et al., 2020, which is incorporated herewith in its entirety.In some embodiments, the recombinant yeast host cell of the present disclosure can be used to generate fatty acid ethyl ester from acetyl-coA. In some embodiments, the recombinant yeast host cell can include / express at least one of a wax ester synthase, acetyl-CoA carboxylase (ACC1), fatty acid synthase (FAS1 and / or FAS2). In some embodiments, the wax ester synthase is native or heterologous to the recombinant yeast host cell. In some additional embodiments, the recombinant yeast host cell comprises native and heterologous copies of the gene encoding the wax ester synthase. In some embodiments, the acetyl-CoA carboxylase is native or heterologous to the recombinant yeast host cell. In some additional embodiments, the recombinant yeast host cell comprises native and heterologous copies of the gene encoding the acetyl-CoA carboxylase. In some embodiments, the fatty acid synthase is native or heterologous to the recombinant yeast host cell. In some additional embodiments, the recombinant yeast host cell comprises native and heterologous copies of the gene encoding the fatty acid synthase. Embodiments of recombinant yeast host cells capable of generating fatty acid esters are disclosed in de Jong et al., 2014, which is incorporated herewith in its entirety.In some embodiments, the recombinant yeast host cell of the present disclosure can be used to generate an alcohol, such as ethanol, from acetyl-coA. Embodiments of recombinant yeast host cells capable of generating ethanol and including further genetic modifications are disclosed in US patent 8871488, US patent 9181566, US patent 9422581 , US patent 9422582, US patent 9550999, US patent 9605269, US patent 9790521 , US patent 10006058, US patent 10240168, US patent 10428354, US patent 10570421 , US patent 11198881 , US patent 11332728, US patent 11447783, US patent 11753656, US patent application published under 20210380989, US patent application published under 20190338256, US patent application published under 20200224209, US patent application published under 20200377559, US patent application published under 20210047660, US patent application published under 20210147792, US patent application published under 20210207076, US patent application published under 20210221857, US patent application published under 20210292734, US patent application published under 20210332091 , US patent application published under 20210388397, US patent application published under 20210395756, US patent application published under 20220251582, US patent application published under 20220251608, USpatent application published under 20220259604, US patent application published under 20230002793, US patent application published under 20230091532, US patent application published under 20230331789, US patent application published under 20230193232, US patent application 18 / 688,829, and US patent application 18 / 844,795, and which are all incorporated in their entirety.Methods for making acetyl-P and associated fermentation productsThe present disclosure provides a process for making acetyl-P from glucose so as to favor the production of one or more fermentation product by the recombinant yeast host cell. The production of the one or more fermentation product is favored in the recombinant yeast host cell (when compared to a corresponding control yeast host cell) because it has the ability to express the PGI-PHK fusion protein (and the corresponding control yeast host cell does not have the ability to express the PGI-PHK fusion protein). In the present disclosure, the control yeast host cell comprises all the genetic modifications present in the recombinant yeast host cell except the one allowing the expression of the PGI-PHK fusion protein.Broadly, the process of the present disclosure comprises contacting the recombinant yeast host cell with a carbohydrate under conditions to allow the conversion of at least in part of the carbohydrate into acetyl-P and, eventually, into one or more fermentation products (e.g., fermenting step). The carbohydrate is present in a fermentation medium (sometimes referred to as a biomass). The process can optionally include a step of isolating the one or more fermentation product from the fermented fermentation medium (using distillation for example). The process can also optionally include a step of recuperating the distiller’s grain for animal nutrition. In some embodiments, the process can include, prior to the contacting step, a step of propagating the recombinant yeast host cell. In additional embodiments, the process can including, prior to the fermentation step, a step of liquefying the starch present in the biomass. The one or more fermentation product can comprise, without limitation, acetone, farnesene, 3- hydroxy-propionic acid, p-coumaric acid, 2-phenylethanol, tryosol, salidroside, polyhydroxybutyrate, carotenoid, a fatty acid ethyl ester, isopropanol, ethanol or combinations thereof. In some embodiments, the fermentation products can comprise at least two distinct fermentation products such as at least two of any one of the following: acetone, farnesene, 3- hydroxy-propionic acid, p-coumaric acid, 2-phenylethanol, tryosol, salidroside, polyhydroxybutyrate, carotenoid, a fatty acid ethyl ester, isopropanol or ethanol. In some specific embodiments, the fermentation product can comprise acetone and ethanol. In some embodiments, the fermentation products can comprise at least three distinct fermentation products such as at least three of any one of the following: acetone, farnesene, 3-hydroxy- propionic acid, p-coumaric acid, 2-phenylethanol, tryosol, salidroside, polyhydroxybutyrate,carotenoid, a fatty acid ethyl ester, isopropanol or ethanol. In some specific embodiments, the fermentation product can comprise acetone, isopropanol and ethanol.In some embodiments, the process of the present disclosure comprises a single fermentation (which can be a continuous, a batch or a fed batch for example). In other embodiments, the process of the present disclosure comprises a plurality of fermentations in which the recombinant yeast host cells are recycled between two rounds of fermentations. In some embodiments, the recombinant yeast host cells are only exogenously added in the initial fermentation cycle and are then recycled in further fermentation cycles. Each fermentation cycle of the process includes contacting a fermentation medium (comprising a fermentable carbohydrate) with a fermenting population under conditions so as to allow the conversion of the fermentable carbohydrate in a fermentation product (e.g., fermentation). At the end of the fermentation, the fermenting population present in the fermented fermentation medium is substantially isolated from the fermented fermentation medium and use to initiate another fermentation cycle. It is understood that, in such embodiments, the initial fermenting population consists essentially in the recombinant yeast host cells of the present disclosure and that, during the plurality of the fermentation cycles, the recycled fermenting population can include some contaminating wild (non-genetically modified) yeasts. The plurality of fermentation cycles can include at least one continuous fermentation. The plurality of fermentation cycles can only include continuous fermentations. The plurality of fermentation cycles can include at least one batch fermentation. The plurality of fermentation cycles can only include batch fermentations. The processes of the present disclosure can include an initial fermentation cycle at least one, two, three, four, five, six, seven, eight, nine, 10, 15, 20, 25, 30, 35, 40,45, 50, 55, 60, 65, 70, 75, 80, 85, 90, 95, 100, 105, 110, 115, 120, 125, 130, 135, 140, 145, 150, 155, 160, 165, 170, 175, 180, 185, 190, 195, 200 or more further fermentation cycles. In specific embodiments, the processes of the present disclosure include an initial fermentation cycle at least 39 further fermentation cycles. In specific embodiments, the processes of the present disclosure include an initial fermentation cycle at least 49 further fermentation cycles. In specific embodiments, the processes of the present disclosure include an initial fermentation cycle at least 59 further fermentation cycles. In specific embodiments, the processes of the present disclosure include an initial fermentation cycle at least 69 further fermentation cycles. In specific embodiments, the processes of the present disclosure include an initial fermentation cycle at least 79 further fermentation cycles. In specific embodiments, the processes of the present disclosure include an initial fermentation cycle at least 89 further fermentation cycles. In specific embodiments, the processes of the present disclosure include an initial fermentation cycle at least 99 further fermentation cycles. In specific embodiments, the processes of the present disclosure include an initial fermentation cycle at least 109 further fermentation cycles. In specific embodiments, the processes of the present disclosure include an initial fermentation cycle at least 119 furtherfermentation cycles. In specific embodiments, the processes of the present disclosure include an initial fermentation cycle at least 129 further fermentation cycles. In specific embodiments, the processes of the present disclosure include an initial fermentation cycle at least 139 further fermentation cycles. In specific embodiments, the processes of the present disclosure include an initial fermentation cycle at least 149 further fermentation cycles. In specific embodiments, the processes of the present disclosure include an initial fermentation cycle at least 159 further fermentation cycles. In specific embodiments, the processes of the present disclosure include an initial fermentation cycle at least 169 further fermentation cycles. In specific embodiments, the processes of the present disclosure include an initial fermentation cycle at least 179 further fermentation cycles. In specific embodiments, the processes of the present disclosure include an initial fermentation cycle at least 189 further fermentation cycles. In specific embodiments, the processes of the present disclosure include an initial fermentation cycle at least 199 further fermentation cycles.Each fermentation cycle (irrespective of its type) comprises a step of contacting the fermentation medium with a fermenting population of recombinant yeast host cells. The fermenting population will ferment (e.g., convert some of the biomass into a fermentation product) the fermentation medium to generate a fermented medium. The contacting step can include simultaneously adding the fermenting population and the fermentation medium to a fermenter. The contacting step can include adding the fermentation medium to a fermenter and subsequently adding the fermenting population to the fermentation medium. The contacting step can include adding fermentation medium to a fermenter already containing the fermentation population. After the fermentation, a fermented medium will be obtained, and it comprises a fermentation product and a fermented population. In a process comprising a batch fermentation cycle, the fermenting population is contacted (e.g., pitched) with a fermentation medium in a fermenter. The fermenting population can be added to the fermenter prior to, at the same time and / or after the fermentation medium has been added. In a process comprising a continuous fermentation cycle, the fermenting population can be added to the series of fermenters prior to, at the same time and / or after the fermentation medium has been added.The fermentation medium that can be fermented by the recombinant yeast host cells described herein includes any type of fermentable carbohydrate known in the art and described herein. In one embodiment, the carbohydrate source is a biomass. For example, the biomass can include, but is not limited to, starch, sugar and lignocellulosic materials comprising lignocellulosic fibers. Starch materials can include, but are not limited to, mashes such as corn, wheat, rye, barley, rice or milo. The starch present in the biomass can be totally or in part in a raw form or in a gelatinized form. When the biomass comprises or is derived from corn, it can include a corn mash. Sugar materials can include, but are not limited to, sugar beets, artichoke tubers, sweet sorghum, molasses or cane. The terms “lignocellulosic material”, “lignocellulosicsubstrate” and “cellulosic biomass” mean any type of biomass comprising cellulose, hemicellulose, lignin or combinations thereof, such as but not limited to woody biomass, forage grasses, herbaceous energy crops, non-woody-plant biomass, agricultural wastes and / or agricultural residues, forestry residues and / or forestry wastes, paper-production sludge and / or waste paper sludge, waste -water-treatment sludge, municipal solid waste, corn fiber from wet and dry mill corn ethanol plants and sugar-processing residues. The terms “hemicellulosics”, “hemicellulosic portions” and “hemicellulosic fractions” mean the non-lignin, non-cellulose elements of lignocellulosic material, such as but not limited to hemicellulose (i.e., comprising mannan, glucomannan and galactoglucomannan), pectins (e.g., homogalacturonans, rhamnogalacturonan I and II, and xylogalacturonan) and proteoglycans (e.g., arabinogalactan- protein). In some embodiments, the biomass can include and / or be supplemented with citric acid (especially when acetic acid or acetate is the first metabolic product).In a non-limiting example, the lignocellulosic material can include, but is not limited to, woody biomass, such as recycled wood pulp fiber, sawdust, hardwood, softwood, and combinations thereof; grasses, such as switch grass, cord grass, rye grass, reed canary grass, miscanthus or a combination thereof; sugar-processing residues, such as but not limited to sugar cane bagasse; sugar cane must; agricultural wastes, such as but not limited to rice straw, rice hulls, barley straw, corn cobs, cereal straw, wheat straw, canola straw, oat straw, oat hulls, and corn fiber; stover, such as but not limited to soybean stover, corn stover; succulents, such as but not limited to, agave; and forestry wastes, such as but not limited to, recycled wood pulp fiber, sawdust, hardwood (e.g., poplar, oak, maple, birch, willow), softwood or any combination thereof. Lignocellulosic material may comprise one species of fiber; alternatively, lignocellulosic material may comprise a mixture of fibers that originate from different lignocellulosic materials. Other lignocellulosic materials are agricultural wastes, such as cereal straws, including wheat straw, barley straw, canola straw and oat straw; corn fiber; stovers, such as corn stover and soybean stover; grasses, such as switch grass, reed canary grass, cord grass, and miscanthus; or combinations thereof.Substrates for cellulose activity assays can be divided into two categories, soluble and insoluble, based on their solubility in water. Soluble substrates include cellodextrins or derivatives, carboxymethyl cellulose (CMC) or hydroxyethyl cellulose (HEC). Insoluble substrates include crystalline cellulose, microcrystalline cellulose (Avicel), amorphous cellulose, such as phosphoric acid swollen cellulose (PASC), dyed or fluorescent cellulose, and pretreated lignocellulosic biomass. These substrates are generally highly ordered cellulosic material and thus only sparingly soluble.It will be appreciated that suitable lignocellulosic material may be any feedstock that contains soluble and / or insoluble cellulose, where the insoluble cellulose may be in a crystalline or noncrystalline form. In various embodiments, the lignocellulosic biomass comprises, for example,wood, corn, corn stover, sawdust, bark, molasses, sugarcane, leaves, agricultural and forestry residues, grasses such as switchgrass, ruminant digestion products, municipal wastes, paper mill effluent, newspaper, cardboard or combinations thereof.Paper sludge is also a viable feedstock for lactate or acetate production. Paper sludge is solid residue arising from pulping and paper-making and is typically removed from process wastewater in a primary clarifier. The cost of disposing of wet sludge is a significant incentive to convert the material for other uses, such as conversion to ethanol. Processes provided by the present invention are widely applicable. Moreover, the saccharification and / or fermentation products may be used to produce ethanol and acetone or higher value-added chemicals, such as organic acids, aromatics, esters, and polymer intermediates.In specific embodiments, the fermentation medium (or biomass) comprises sugarcane or a sugarcane derivative. After it has been harvested, the sugarcane is pressed or diffused to generate sugarcane juice and a solid fibrous residue, the cane bagasse. In the context of the present disclosure, sugarcane juice is considered to be a sugarcane derivative. The sugarcane juice can be clarified and concentrated by evaporation until sucrose crystallization is observed. The clarified sugarcane juice and the concentrated sugarcane juice are considered sugarcane derivatives. The sucrose crystals obtained after crystallization can be collected by centrifugation, generating a sucrose saturated viscous phase, called “cane molasses”. Cane molasses, which is also considered to be a sugarcane derivative, can include between 45 to 60 % sucrose and 5 to 20 % glucose plus fructose. In some embodiments, the fermentation medium comprises, as a sugarcane derivative, a sugarcane juice. In another embodiment, the fermentation medium comprises, as a sugarcane derivative, a cane molasses. In still another embodiment, the fermentation medium comprises, as a sugarcane derivative, both sugarcane juice and a cane molasses.The fermentation step of the process can be performed at temperatures of at least about 25°C, about 28°C, about 30°C, about 31 °C, about 32°C, about 33°C, about 34°C, about 35°C, about 36°C, about 37°C, about 38°C, about 39°C, about 40°C, about 41 °C, about 42°C or about 50°C. In some embodiments, the process can be conducted at temperatures above about 30°C, about 31 °C, about 32°C, about 33°C, about 34°C, about 35°C, about 36°C, about 37°C, about 38°C, about 39°C, about 40°C, about 41 °C, about 42°C or about 50°C.In some embodiments, prior to fermentation, a step of liquefying starch can be included in the process. In such embodiment, the liquefied starch is then submitted to a following fermentation step. The liquefaction of starch can be performed at a temperature of between about 70°C- 105°C to allow for proper gelatinization and hydrolysis of the starch. In an embodiment, the liquefaction occurs at a temperature of at least about 70°C, 75°C, 80°C, 85°C, 90°C, 95°C, 100°C or 105°C. Alternatively or in combination, the liquefaction occurs at a temperate of no more than about 105°C, 100°C, 95°C, 90°C, 85°C, 80°C, 75°C or 70°C. In yet anotherembodiment, the liquefaction occurs at a temperature between about 80°C and 85°C (which can include a thermal treatment spike at 105°C).During fermentation, the pH of the fermentation medium can be equal to or below 5.5, 5.4, 5.3, 5.2, 5.1 , 5.0, 4.9, 4.8, 4.7., 4.6, 4.5, 4.4, 4.3, 4.2, 4.1 , 4.0 or lower. In an embodiment, the pH of the fermentation medium (during fermentation) is between 4.0 and 5.5.In some embodiments, the processes of the present disclosure comprise producing ethanol at a particular rate. For example, in some embodiments, ethanol is produced at a rate of at least about 0.1 mg per hour per liter, at least about 0.25 mg per hour per liter, at least about 0.5 mg per hour per liter, at least about 0.75 mg per hour per liter, at least about 1 .0 mg per hour per liter, at least about 2.0 mg per hour per liter, at least about 5.0 mg per hour per liter, at least about 10 mg per hour per liter, at least about 15 mg per hour per liter, at least about 20.0 mg per hour per liter, at least about 25 mg per hour per liter, at least about 30 mg per hour per liter, at least about 50 mg per hour per liter, at least about 100 mg per hour per liter, at least about 200 mg per hour per liter, at least about 300 mg per hour per liter, at least about 400 mg per hour per liter, at least about 500 mg per hour per liter, at least about 600 mg per hour per liter, at least about 700 mg per hour per liter, at least about 800 mg per hour per liter, at least about 900 mg per hour per liter, at least about 1 g per hour per liter, at least about 1 .5 g per hour per liter, at least about 2 g per hour per liter, at least about 2.5 g per hour per liter, at least about 3 g per hour per liter, at least about 3.5 g per hour per liter, at least about 4 g per hour per liter, at least about 4.5 g per hour per liter, at least about 5 g per hour per liter, at least about 5.5 g per hour per liter, at least about 6 g per hour per liter, at least about 6.5 g per hour per liter, at least about 7 g per hour per liter, at least about 7.5 g per hour per liter, at least about 8 g per hour per liter, at least about 8.5 g per hour per liter, at least about 9 g per hour per liter, at least about 9.5 g per hour per liter, at least about 10 g per hour per liter, at least about 10.5 g per hour per liter, at least about 11 g per hour per liter, at least about 11 .5 g per hour per liter, at least about 12 g per hour per liter, at least about 12.5 g per hour per liter, at least about 13 g per hour per liter, at least about 13.5 g per hour per liter, at least about 14 g per hour per liter, at least about 14.5 g per hour per liter or at least about 15 g per hour per liter.In some embodiments, the processes of the present disclosure can produce ethanol at a rate of at least about 0.1 mg per hour per liter, at least about 0.25 mg per hour per liter, at least about 0.5 mg per hour per liter, at least about 0.75 mg per hour per liter, at least about 1 .0 mg per hour per liter, at least about 2.0 mg per hour per liter, at least about 5.0 mg per hour per liter, at least about 10 mg per hour per liter, at least about 15 mg per hour per liter, at least about 20.0 mg per hour per liter, at least about 25 mg per hour per liter, at least about 30 mg per hour per liter, at least about 50 mg per hour per liter, at least about 100 mg per hour per liter, at least about 200 mg per hour per liter, at least about 300 mg per hour per liter, at least about 400 mg per hour per liter, at least about 500 mg per hour per liter, at least about 600 mgper hour per liter, at least about 700 mg per hour per liter, at least about 800 mg per hour per liter, at least about 900 mg per hour per liter, at least about 1 g per hour per liter, at least about 1 .5 g per hour per liter, at least about 2 g per hour per liter, at least about 2.5 g per hour per liter, at least about 3 g per hour per liter, at least about 3.5 g per hour per liter, at least about 4 g per hour per liter, at least about 4.5 g per hour per liter, at least about 5 g per hour per liter, at least about 5.5 g per hour per liter, at least about 6 g per hour per liter, at least about 6.5 g per hour per liter, at least about 7 g per hour per liter, at least about 7.5 g per hour per liter, at least about 8 g per hour per liter, at least about 8.5 g per hour per liter, at least about 9 g per hour per liter, at least about 9.5 g per hour per liter, at least about 10 g per hour per liter, at least about 10.5 g per hour per liter, at least about 11 g per hour per liter, at least about 11 .5 g per hour per liter, at least about 12 g per hour per liter, at least about 12.5 g per hour per liter, at least about 13 g per hour per liter, at least about 13.5 g per hour per liter, at least about 14 g per hour per liter, at least about 14.5 g per hour per liter, at least about 15 g per hour per liter or more than a control strain (e.g., a wild-type strain or a parental strain) and grown under the same conditions.Ethanol production can be measured using any method known in the art. For example, the quantity of ethanol in fermentation samples can be assessed using HPLC analysis. Many ethanol assay kits are commercially available that use, for example, alcohol oxidase enzymebased assays.In the process described herein, it is possible to add an exogenous source (e.g., to dose) of an enzyme to facilitate saccharification or improve fermentation yield. As such, the process can comprise including one or more dose of one or more exogenous enzyme during the liquefaction / saccharification and / or the fermentation step. The exogenous enzyme can be provided in a purified form or in combination with other enzymes (e.g., a cocktail). In the context of the present disclosure, the term “exogenous” refers to a characteristic of the enzyme, namely that it has not been produced during the saccharification or the fermentation step, but that it was produced prior to the saccharification or the fermentation step. The exogenous enzyme that can be used during the saccharification / fermentation process can include, without limitation, an alpha-amylase, a glucoamylase, a protease, a phytase, a pullulanase, a cellulase, a xylanase, a trehalase or any combination thereof.In the process described herein, it is possible to add a nitrogen source (usually urea or ammonia) to facilitate liquefaction / saccharification or improve fermentation yield. As such, the process can comprise including one or more amount of the nitrogen source prior to or during the saccharification and / or the fermentation step.The present invention will be more readily understood by referring to the following examples which are given to illustrate the invention rather than to limit its scope.EXAMPLEThe genotypes of the various Saccharomyces cerevisiae characterized in the Example are presented in Table 3.Table 3. Genotypes of the various Saccharomyces cerevisiae strains or isolates (Sc*) of the present example. PGI refers to gluceose-6-phosphate of S. cerevisiae having the amino acid of SEQ ID NO: 2 (encoded by the nucleic acid sequence of SEQ ID NO: 1). PHK refers to the phosphoketolase of B. adolescentis having the amino acid sequence of SEQ ID NO: 32 lacking the N-terminal methionine residue (encoded by the nucleic acid sequence of SEQ ID NO: 31 lacking the 5’ atg codon). Linker 1 refers to the linker of SEQ ID NO: 72 (encoded by the nucleic acid sequence of SEQ ID NO: 71), while linker 2 refers to the linker of SEQ ID NO: 74 (encoded by the nucleic acid sequence of SEQ ID NO: 73). All the strains in this table include the following genetic modifications allowing the yeast to make acetone from acetate and acetylcoenzyme A: expression of heterologous Erg10 (2 copies / haploid genome, amino acid sequence of SEQ ID NO: 144, and nucleic acid sequence of SEQ ID NO: 143), heterologous CTFA (2 copies / haploid genome, amino acid sequence of SEQ ID NO: 146, nucleic acid sequence of SEQ ID NO: 145), heterologous CTFB (2 copies / haploid genome, amino acid sequence of SEQ ID NO: 148, nucleic acid sequence of SEQ ID NO: 147), heterologous ADC (2 copies / haploid genome, amino acid sequence of SEQ ID NO: 150, nucleic acid sequence of SEQ ID NO: 149), heterologous TKL1 (1 copy / haploid genome, amino acid sequence of SEQ ID NO: 152, nucleic acid sequence of SEQ ID NO: 151), TAL1 (1 copy / haploid genome, amino acid sequence of SEQ ID NO: 154, nucleic acid sequence of SEQ ID NO: 153), RPE1 (1 copy / haploid genome, amino acid sequence of SEQ ID NO: 156, nucleic acid sequence of SEQ ID NO: 155), and RKI1 (1 copy / haploid genome, amino acid sequence of SEQ ID NO: 158, nucleic acid sequence of SEQ ID NO: 157). The table below provides the additional genetic modifications introduced into each strain / isolate characterized. All the genetic modifications were made at neutral integrating sites.Fermentations. The strains described in Table 1 were propagated overnight aerobically in YPD media with 40 g / L glucose at 32°C. The propagated strains were pitched into YPD media comprising 120 g / L of glucose at 1 % of the total fermentation volume, 0.3 ml into 30 ml media contained within a sealed 60 ml serum vial. Fermentations were carried out for 40 hours at 32°C. Following fermentation, acetic acid contained within the supernatant was quantified using high pressure liquid chromatography.Two fusions proteins were designed to be expressed in Saccharomyces cerevisiae (Figure 2). As indicated on Figure 2, a PGI moiety was associated with a PHK moiety via either a more rigid linker, linker 1 (Figure 2A) or a more flexible linker, linker 2 (Figure 2B).It was then determined if the expression of these fusion proteins would promote the production of acetyl-phosphate (acetyl-P) in the yeast. In order to do so, the fusion proteins were expressed in yeasts genetically engineered for upregulation of the non-oxidative pentose phosphate pathway to limit downstream bottlenecks in acetyl-P generation. In S. cerevisiae, acetyl-P is a non-native metabolite and when present is efficiently converted to acetic acid through promiscuous phosphatase activity from the native GPP1 and GPP2 glycerol-3- phosphatases. It is therefore possible to determine if a further genetic modification modulates acetyl-phosphate production indirectly by measuring the acetic acid produced by the yeast.The heterologous expression of PHK alone led to a ~1 .4 g / L increase in acetic acid produced when compared to the control (see Sc-E2 vs. parental strain Sc-E1 , Figure 3 and Table 4). The heterologous expression of PGI alone had no impact on acetic acid production when compared to the control (see Sc-E5 vs. parental strain Sc-E1 , Figure 3 and Table 4). The heterologous expression of PGI and PHK together (but not as a fusion protein) led to a 15% increase in acetic acid production as compared to the heterologous expression of PHK alone (~1.6 g / L, see Sc-E8 vs. Sc-E2, Figure 3 and Table 4). The heterologous expression of the PGI-PHK fusion proteins increased acetic acid production by nearly 2-fold over isolate Sc-8 (but not as a fusion protein, see Sc-E5 and Sc-E6 vs. Sc-E8, Figure 3 and Table 4).Table 4. Amounts of acetate and ethanol (g / L) produced by variants S. cerevisiae strains after fermentation.REFERENCESDe Jong, B.W., Shi, S., Siewers, V. and Nielsen, J., 2014. Improved production of fatty acid ethyl esters in Saccharomyces cerevisiae through up-regulation of the ethanol degradation pathway and expression of the heterologous phosphoketolase pathway. Microbial cell factories, 13(1), pp.1-10.Gu, Y, Ma, J., Zhu, Y, Ding, X. and Xu, P., 2020. Engineering Yarrowia lipolytica as a chassis for de novo synthesis of five aromatic-derived natural products and chemicals. ACS synthetic biology, 9(8), pp.2096-2106.Guo, W., Huang, Q., Feng, Y, Tan, T., Niu, S., Hou, S., Chen, Z., Du, Z.Q., Shen, Y. and Fang, X., 2020. Rewiring central carbon metabolism for tyrosol and salidroside production in Saccharomyces cerevisiae. Biotechnology and Bioengineering, 117(8), pp.2410-2419.Hassing, E.J., de Groot, RA., Marquenie, V.R., Pronk, J.T. and Daran, J.M.G., 2019. Connecting central carbon and aromatic amino acid metabolisms to improve de novo 2- phenylethanol production in Saccharomyces cerevisiae. Metabolic engineering, 56, pp.165- 180.Hellgren, J., Godina, A., Nielsen, J. and Siewers, V., 2020. Promiscuous phosphoketolase and metabolic rewiring enables novel non-oxidative glycolysis in yeast for high-yield production of acetyl-CoA derived products. Metabolic engineering, 62, pp.150-160.Kocharin, K., Siewers, V. and Nielsen, J., 2013. Improved poly hydroxy butyrate production by Saccharomyces cerevisiae through the use of the phosphoketolase pathway. Biotechnology and bioengineering, 110(8), pp.2216-2224.Liu, Q., Yu, T., Li, X., Chen, Y, Campbell, K., Nielsen, J. and Chen, Y, 2019. Rewiring carbon metabolism in yeast for high level production of aromatic chemicals. Nature communications, 10(1), p.4976.Meadows, A.L., Hawkins, K.M., Tsegaye, Y, Antipov, E., Kim, Y, Raetz, L., Dahl, R.H., Tai, A., Mahatdejkul-Meadows, T., Xu, L. and Zhao, L., 2016. Rewriting yeast central carbon metabolism for industrial isoprenoid production. Nature, 537(7622), pp.694-697.Qin, N., Li, L., Ji, X., Li, X., Zhang, Y, Larsson, C., Chen, Y, Nielsen, J. and Liu, Z., 2020. Rewiring central carbon metabolism ensures increased provision of acetyl-CoA and NADPH required for 3-OH-propionic acid production. ACS Synthetic Biology, 9(12), pp.3236-3244.Rajkumar, A.S. and Morrissey, J.R, 2020. Rational engineering of Kluyveromyces marxianus to create a chassis for the production of aromatic products. Microbial Cell Factories, 19, pp.1 - 19.Su, B., Song, D. and Zhu, H., 2020. Metabolic engineering of Saccharomyces cerevisiae for enhanced carotenoid production from xylose-glucose mixtures. Frontiers in Bioengineering and Biotechnology, 8, p.435.

Claims

WHAT IS CLAIMED IS:1 . A fusion polypeptide for making acetyl-phosphate from glucose, the fusion polypeptide comprising (i) a glucose-6-phosphate isomerase moiety and (ii) a phosphoketolase moiety.

2. The fusion polypeptide of claim 1 , wherein the glucose-6-phosphate isomerase moiety has the amino acid sequence of SEQ ID NO: 2, 4, 6, 8, 10, 12, 14, 16, 18, 20, 22, 24, 26, 28 or 30 or is a variant of the amino acid sequence of SEQ ID NO: 2, 4, 6, 8, 10, 12, 14, 16, 18, 20, 22, 24, 26, 28 or 30 having glucose-6-phosphate isomerase activity.

3. The fusion polypeptide of claim 1 or 2, wherein the phosphoketolase moiety has the amino acid sequence of SEQ ID NO: 32, 34, 36, 38, 40, 42, 44, 46, 48, 50, 52, 54, 56, 58, 60, 62, 64, 66, 68 or 70 or is a variant of the amino acid sequence of SEQ ID NO: 32, 34, 36, 38, 40, 42, 44, 46, 48, 50, 52, 54, 56, 58, 60, 62, 64, 66, 68 or 70 having phosphoketolase activity.

4. The fusion polypeptide of any one of claims 1 to 3, further comprising an amino acid linker between the glucose-6-phosphate isomerase moiety and the phosphoketolase moiety.

5. The fusion polypeptide of claim 4, wherein the amino acid linker has the amino acid sequence of SEQ ID NO: 72 or 74 or is a variant of the amino acid sequence of SEQ ID NO: 72 or 74.

6. The fusion polypeptide of any one of claims 1 to 5 having the following formula (I):NH2-PGI-L-PHK-COOH (I) wherein: NH2is the amino terminus of the fusion polypeptide;PGI is the glucose-6-phosphate isomerase moiety;L is the optional amino acid linker;PHK is the phosphoketolase moiety; andCOOH is the carboxy terminus of the fusion polypeptide.

7. A recombinant yeast host cell comprising the fusion polypeptide of any one of claims 1 to 6.

8. The recombinant yeast host cell of claim 7, further comprising a heterologous polypeptide for converting acetyl-phosphate in acetyl-coenzyme A.

9. The recombinant yeast host cell of claim 8, wherein the heterologous polypeptide for converting acetyl-phosphate in acetyl-coenzyme A comprises a heterologous phosphotransacetylase.

10. The recombinant yeast host cell of claim 9, wherein the heterologous phosphotransacetylase has the amino acid sequence of SEQ ID NO: 76, 80, 82, 84, 86, 88,90, 92, 94, 96, 98, 100 or 102 or is a variant of the amino acid sequence of SEQ ID NO: 76, 80, 82, 84, 86, 88, 90, 92, 94, 96, 98, 100 or 102 having phosphotransacetylase activity.

11. The recombinant yeast host cell of any one of claims 7 to 10 comprising a native and / or heterologous polypeptide for converting acetyl-phosphate in acetate.

12. The recombinant yeast host cell of claim 11 , wherein the native and / or heterologous polypeptide for converting acetyl-phosphate in acetate comprises:• a native or heterologous glycerol-3-phosphate phosphatase; and / or• a heterologous acetate kinase.

13. The recombinant yeast host cell of claim 12, wherein the native or heterologous glycerol-3-phosphate phosphatase comprises glycerol-3-phosphate phosphatase 1 and / or glycerol-3-phosphate phosphatase 2.

14. The recombinant yeast host cell of claim 13, wherein the native or heterologous glycerol-3-phosphate phosphatase 1 comprises the amino acid sequence of SEQ ID NO: 104 or is a variant of the amino acid sequence of SEQ ID NO: 104 having glycerol-3-phosphate phosphatase activity.

15. The recombinant yeast host cell of claim 13 or 14, wherein the native or heterologous glycerol-3-phosphate phosphatase 2 comprises the amino acid sequence of SEQ ID NO: 106 or is a variant of the amino acid sequence of SEQ ID NO: 106 having glycerol-3-phosphate phosphatase activity.

16. The recombinant yeast host cell of any one of claims 12 to 15, wherein the heterologous acetate kinase has the amino acid sequence of SEQ ID NO: 108, 110, 112, 114, 116, 118, 120, 122, 124, 126, 128 or 130 or is a variant of the amino acid sequence of SEQ ID NO: 108, 110, 112, 114, 116, 118, 120, 122, 124, 126, 128 or 130 having acetate kinase activity.

17. The recombinant yeast host cell of any one of claims 7 to 16 comprising a native or heterologous polypeptide for converting acetate into acetyl-coenzyme A.

18. The recombinant yeast host cell of claim 17, wherein the native or heterologous polypeptide for converting acetate into acetyl-coenzyme A comprises an acetyl-coenzyme A synthetase.

19. The recombinant yeast host cell of claim 18, wherein the acetyl-coenzyme A synthetase has the amino acid sequence of SEQ ID NO: 132, 134, 136, 138, 140 or 142 or is a variant of the amino acid sequence of SEQ ID NO: 132, 134, 136, 138, 140 or 142 having acetyl- coenzyme A synthetase activity.

20. The recombinant yeast host cell of any one of claims 7 to 19 comprising one or more heterologous polypeptide for converting acetyl-coenzyme A into a fermentation product.

21. The recombinant yeast host cell of claim 20, wherein the fermentation product comprises acetone, farnesene, 3-hydroxy-propionic acid, p-coumaric acid, 2-phenylethanol, tyrosol, salidroside, polyhydroxybutyrate, carotenoid, a fatty acid ethyl ester, and / or isopropanol.

22. The recombinant yeast host cell of claim 20 or 21 , wherein the fermentation product further comprises ethanol.

23. The recombinant yeast host cell of any one of claims 7 to 22 being from the genus Saccharomyces sp.

24. The recombinant yeast host cell of claim 23 being from the species Saccharomyces cerevisiae.

25. A process for making acetyl-phosphate from glucose, the method comprising contacting the fusion polypeptide of any one of claims 1 to 6 with glucose under condition to promote the formation of acetyl-phosphate.

26. The process of claim 25 comprising contacting the recombinant yeast host cell of any one of claims 7 to 24 with glucose under condition to promote the formation of acetyl- phosphate.

Images