{"ymdb_id":"YMDB00410","created_at":"2011-05-29T18:14:00.000Z","updated_at":"2016-09-08T18:35:27.000Z","name":"(R)-Acetoin","cas":"53584-56-8","state":"Liquid","melting_point":"15 oC","description":"(R)-Acetoin is the R isomer of acetoin. Acetoin is a product of fermentation; it is a component of the butanediol cycle in microorganisms. It is a neutral, four carbon molecule used as an external energy store by a number of fermentive bacteria. Acetoin is a colorless or pale yellow to green yellow liquid with a pleasant buttery odor, it is responsible for almond or buttery aromas.","experimental_water_solubility":"1000 mg/mL at 20 oC [YALKOWSKY,SH \u0026 DANNENFELSER,RM (1992)]","experimental_logp_hydrophobicity":null,"location":"cytoplasm","synthesis_reference":null,"chebi_id":"15686","hmdb_id":"HMDB03243","kegg_id":"C00810","pubchem_id":"439314","cs_id":"388445","foodb_id":null,"wikipedia_link":"Acetoin","biocyc_id":"CPD-10353","iupac":"(3R)-3-hydroxybutan-2-one","traditional_iupac":"(R)-acetoin","logp":"-0.1422039953333334","pka":"17.81975350602122","alogps_solubility":"4.73e+02 g/l","alogps_logp":"-0.66","alogps_logs":"0.73","acceptor_count":"2","donor_count":"1","rotatable_bond_count":"1","polar_surface_area":"37.3","refractivity":"22.390900000000002","polarizability":"9.109409699439318","formal_charge":"0","physiological_charge":"0","pka_strongest_basic":"-3.357098011793852","pka_strongest_acidic":"13.723456226493909","bioavailability":"1","number_of_rings":"0","rule_of_five":"1","ghose_filter":"0","veber_rule":"1","mddr_like_rule":"0","synonyms":[".gamma.-Hydroxy-.beta.-oxobutane","(R)-2-Acetoin","(R)-3-Hydroxy-2-butanone","(R)-3-Hydroxybutan-2-one","(R)-Acetoin","(R)-Dimethylketol","1-Hydroxyethyl methyl ketone","2-Acetoin","2-Butanol-3-one","2-Butanone, 3-hydroxy-","2-Hydroxy-3-butanone","2-hydroxy-3-oxobutane","2,3-Butanolone","3-Hydroxy-2-butanone","3-hydroxy-2-butanone (acetoin)","3-hydroxy-2-butanone (acetoine)","3-hydroxybutan-2-one","3-hydroxybutan-2-one (acetoin)","3-hydroxyl-2-butanone","Acetoin","acetoin (3-hydroxy-2-butanone)","acetoine","Acetyl methyl carbinol","b-oxobutane","beta-oxobutane","Butan-2-one 3-hydroxy","Dimethylketol","gamma-Hydroxy-beta-oxobutane","Methanol, acetylmethyl-"],"pathways":[{"name":"Butanoate metabolism","kegg_map_id":"00650"}],"growth_conditions":[],"references":[{"pubmed_id":21062828,"citation":"Scheer, M., Grote, A., Chang, A., Schomburg, I., Munaretto, C., Rother, M., Sohngen, C., Stelzer, M., Thiele, J., Schomburg, D. (2011). \"BRENDA, the enzyme information system in 2011.\" Nucleic Acids Res 39:D670-D676."},{"pubmed_id":18846089,"citation":"Herrgard, M. J., Swainston, N., Dobson, P., Dunn, W. B., Arga, K. Y., Arvas, M., Bluthgen, N., Borger, S., Costenoble, R., Heinemann, M., Hucka, M., Le Novere, N., Li, P., Liebermeister, W., Mo, M. L., Oliveira, A. P., Petranovic, D., Pettifer, S., Simeonidis, E., Smallbone, K., Spasic, I., Weichart, D., Brent, R., Broomhead, D. S., Westerhoff, H. V., Kirdar, B., Penttila, M., Klipp, E., Palsson, B. O., Sauer, U., Oliver, S. G., Mendes, P., Nielsen, J., Kell, D. B. (2008). \"A consensus yeast metabolic network reconstruction obtained from a community approach to systems biology.\" Nat Biotechnol 26:1155-1160."},{"pubmed_id":12902239,"citation":"Vuralhan, Z., Morais, M. A., Tai, S. L., Piper, M. D., Pronk, J. T. (2003). \"Identification and characterization of phenylpyruvate decarboxylase genes in Saccharomyces cerevisiae.\" Appl Environ Microbiol 69:4534-4541."},{"pubmed_id":10938079,"citation":"Gonzalez, E., Fernandez, M. R., Larroy, C., Sola, L., Pericas, M. A., Pares, X., Biosca, J. A. (2000). \"Characterization of a (2R,3R)-2,3-butanediol dehydrogenase as the Saccharomyces cerevisiae YAL060W gene product. Disruption and induction of the gene.\" J Biol Chem 275:35876-35885."},{"pubmed_id":21051339,"citation":"UniProt Consortium (2011). \"Ongoing and future developments at the Universal Protein Resource.\" Nucleic Acids Res 39:D214-D219."},{"pubmed_id":16968089,"citation":"Mahadevan, K., Farmer, L. (2006). \"Key odor impact compounds in three yeast extract pastes.\" J Agric Food Chem 54:7242-7250."}],"proteins":[{"created_at":"2011-05-24T20:26:42.000Z","updated_at":"2011-07-22T17:53:52.000Z","name":"Pyruvate decarboxylase isozyme 2","uniprot_id":"P16467","uniprot_name":"PDC5_YEAST","enzyme":true,"transporter":false,"gene_name":"PDC5","num_residues":563,"molecular_weight":"61911.60156","theoretical_pi":"6.4","general_function":"Involved in magnesium ion binding","specific_function":"Second most abundant of three pyruvate decarboxylases (PDC1, PDC5, PDC6) implicated in the nonoxidative conversion of pyruvate to acetaldehyde and carbon dioxide during alcoholic fermentation. Most of the produced acetaldehyde is subsequently reduced to ethanol, but some is required for cytosolic acetyl-CoA production for biosynthetic pathways. The enzyme is also one of five 2-oxo acid decarboxylases (PDC1, PDC5, PDC6, ARO10, and THI3) able to decarboxylate more complex 2-oxo acids (alpha-keto-acids) than pyruvate, which seem mainly involved in amino acid catabolism. Here the enzyme catalyzes the decarboxylation of amino acids, which, in a first step, have been transaminated to the corresponding 2-oxo acids. In a third step, the resulting aldehydes are reduced to alcohols, collectively referred to as fusel oils or alcohols. Its preferred substrates are the transaminated amino acids valine, isoleucine, phenylalanine, and tryptophan, whereas leucine is no substrate. In a side-reaction the carbanionic intermediate (or active aldehyde) generated by decarboxylation or by activation of an aldehyde can react with an aldehyde via condensation (or carboligation) yielding a 2-hydroxy ketone, collectively called acyloins","reactions":[{"id":1184,"direction":"\u003e","locations":"cytoplasm","altext":null,"export":true,"pw_reaction_id":null,"source":null},{"id":1186,"direction":"\u003e","locations":"cytoplasm","altext":null,"export":true,"pw_reaction_id":null,"source":null},{"id":1228,"direction":"\u003e","locations":"cytoplasm","altext":null,"export":true,"pw_reaction_id":null,"source":null},{"id":1658,"direction":"\u003c\u003e","locations":"cytoplasm","altext":null,"export":true,"pw_reaction_id":null,"source":null},{"id":1841,"direction":"\u003e","locations":"cytoplasm","altext":null,"export":true,"pw_reaction_id":null,"source":null},{"id":1933,"direction":"\u003e","locations":"cytoplasm","altext":null,"export":true,"pw_reaction_id":null,"source":null},{"id":1934,"direction":"\u003e","locations":"cytoplasm","altext":null,"export":true,"pw_reaction_id":null,"source":null},{"id":2319,"direction":"\u003e","locations":"Cytoplasm. Nucleus;Cytoplasm;Nucleus","altext":"A 2-oxo acid = an aldehyde + CO(2).","export":false,"pw_reaction_id":null,"source":null},{"id":2320,"direction":"\u003e","locations":"Cytoplasm. Nucleus;Cytoplasm","altext":"3-(indol-3-yl)pyruvate = 2-(indol-3-yl)acetaldehyde + CO(2).","export":false,"pw_reaction_id":null,"source":null},{"id":2321,"direction":"\u003e","locations":"Cytoplasm. Nucleus;Cytoplasm","altext":"Phenylpyruvate = phenylacetaldehyde + CO(2).","export":false,"pw_reaction_id":null,"source":null},{"id":2322,"direction":"\u003e","locations":"Cytoplasm. Nucleus;Cytoplasm","altext":"Pyruvate = Acetaldehyde + CO(2).","export":false,"pw_reaction_id":null,"source":null},{"id":2323,"direction":"\u003e","locations":"Cytoplasm. Nucleus;Cytoplasm","altext":"A 2-oxo acid + an aldehyde = A 2-hydroxy ketone + CO(2).","export":false,"pw_reaction_id":null,"source":null},{"id":2324,"direction":"\u003e","locations":"Cytoplasm. Nucleus;Cytoplasm","altext":"An aldehyde + an aldehyde = A 2-hydroxy ketone.","export":false,"pw_reaction_id":null,"source":null},{"id":14096,"direction":"\u003e","locations":null,"altext":null,"export":true,"pw_reaction_id":"PW_R006520","source":"Smpdb"},{"id":14097,"direction":"\u003e","locations":null,"altext":null,"export":true,"pw_reaction_id":"PW_R006525","source":"Smpdb"},{"id":14098,"direction":"\u003e","locations":null,"altext":null,"export":true,"pw_reaction_id":"PW_R006537","source":"Smpdb"},{"id":14099,"direction":"\u003e","locations":null,"altext":null,"export":true,"pw_reaction_id":"PW_R006557","source":"Smpdb"},{"id":14100,"direction":"\u003e","locations":null,"altext":null,"export":true,"pw_reaction_id":"PW_R006971","source":"Smpdb"},{"id":14101,"direction":"\u003e","locations":null,"altext":null,"export":true,"pw_reaction_id":"PW_R006979","source":"Smpdb"}],"signal_regions":"None","transmembrane_regions":"None","pdb_id":null,"cellular_location":"Cytoplasm. Nucleus","genbank_gene_id":"U53881","genbank_protein_id":"1256902","gene_card_id":"PDC5","chromosome_location":"chromosome 12","locus":"YLR134W","synonyms":[],"enzyme_classes":["4.1.1.-","4.1.1.1"],"go_classes":[{"category":"Component","description":" Not Available"},{"category":"Function","description":" metal ion binding"},{"category":"Function","description":" vitamin binding"},{"category":"Function","description":" magnesium ion binding"},{"category":"Function","description":" thiamin pyrophosphate binding"},{"category":"Function","description":" catalytic activity"},{"category":"Function","description":" transferase activity"},{"category":"Function","description":" lyase activity"},{"category":"Function","description":" carbon-carbon lyase activity"},{"category":"Function","description":" carboxy-lyase activity"},{"category":"Function","description":" binding"},{"category":"Function","description":" ion binding"},{"category":"Function","description":" cation binding"},{"category":"Process","description":" Not Available"}],"pfams":[{"name":"TPP_enzyme_C","identifier":"PF02775"},{"name":"TPP_enzyme_M","identifier":"PF00205"},{"name":"TPP_enzyme_N","identifier":"PF02776"}],"pathways":[{"name":"Glycolysis / Gluconeogenesis","kegg_map_id":"00010"},{"name":"Ethanol fermentation","kegg_map_id":null},{"name":"Isoleucine degradation","kegg_map_id":null},{"name":"Phenylalanine metabolism","kegg_map_id":"00360"},{"name":"Pyruvate metabolism","kegg_map_id":"00620"},{"name":"Tryptophan metabolism","kegg_map_id":"00380"},{"name":"Tyrosine metabolism","kegg_map_id":"00350"},{"name":"Valine Degradation","kegg_map_id":null}],"gene_sequence":"ATGTCTGAAATAACCTTAGGTAAATATTTATTTGAAAGATTGAGCCAAGTCAACTGTAACACCGTCTTCGGTTTGCCAGGTGACTTTAACTTGTCTCTTTTGGATAAGCTTTATGAAGTCAAAGGTATGAGATGGGCTGGTAACGCTAACGAATTGAACGCTGCCTATGCTGCTGATGGTTACGCTCGTATCAAGGGTATGTCCTGTATTATTACCACCTTCGGTGTTGGTGAATTGTCTGCTTTGAATGGTATTGCCGGTTCTTACGCTGAACATGTCGGTGTTTTGCACGTTGTTGGTGTTCCATCCATCTCTTCTCAAGCTAAGCAATTGTTGTTGCATCATACCTTGGGTAACGGTGACTTCACTGTTTTCCACAGAATGTCTGCCAACATTTCTGAAACCACTGCCATGATCACTGATATTGCTAACGCTCCAGCTGAAATTGACAGATGTATCAGAACCACCTACACTACCCAAAGACCAGTCTACTTGGGTTTGCCAGCTAACTTGGTTGACTTGAACGTCCCAGCCAAGTTATTGGAAACTCCAATTGACTTGTCTTTGAAGCCAAACGACGCTGAAGCTGAAGCTGAAGTTGTTAGAACTGTTGTTGAATTGATCAAGGATGCTAAGAACCCAGTTATCTTGGCTGATGCTTGTGCTTCTAGACATGATGTCAAGGCTGAAACTAAGAAGTTGATGGACTTGACTCAATTCCCAGTTTACGTCACCCCAATGGGTAAGGGTGCTATTGACGAACAACACCCAAGATACGGTGGTGTTTACGTTGGTACCTTGTCTAGACCAGAAGTTAAGAAGGCTGTAGAATCTGCTGATTTGATATTGTCTATCGGTGCTTTGTTGTCTGATTTCAATACCGGTTCTTTCTCTTACTCCTACAAGACCAAAAATATCGTTGAATTCCACTCTGACCACATCAAGATCAGAAACGCCACCTTCCCAGGTGTTCAAATGAAATTTGCCTTGCAAAAATTGTTGGATGCTATTCCAGAAGTCGTCAAGGACTACAAACCTGTTGCTGTCCCAGCTAGAGTTCCAATTACCAAGTCTACTCCAGCTAACACTCCAATGAAGCAAGAATGGATGTGGAACCATTTGGGTAACTTCTTGAGAGAAGGTGATATTGTTATTGCTGAAACCGGTACTTCCGCCTTCGGTATTAACCAAACTACTTTCCCAACAGATGTATACGCTATCGTCCAAGTCTTGTGGGGTTCCATTGGTTTCACAGTCGGCGCTCTATTGGGTGCTACTATGGCCGCTGAAGAACTTGATCCAAAGAAGAGAGTTATTTTATTCATTGGTGACGGTTCTCTACAATTGACTGTTCAAGAAATCTCTACCATGATTAGATGGGGTTTGAAGCCATACATTTTTGTCTTGAATAACAACGGTTACACCATTGAAAAATTGATTCACGGTCCTCATGCCGAATATAATGAAATTCAAGGTTGGGACCACTTGGCCTTATTGCCAACTTTTGGTGCTAGAAACTACGAAACCCACAGAGTTGCTACCACTGGTGAATGGGAAAAGTTGACTCAAGACAAGGACTTCCAAGACAACTCTAAGATTAGAATGATTGAAGTTATGTTGCCAGTCTTTGATGCTCCACAAAACTTGGTTAAACAAGCTCAATTGACTGCCGCTACTAACGCTAAACAATAA","protein_sequence":"MSEITLGKYLFERLSQVNCNTVFGLPGDFNLSLLDKLYEVKGMRWAGNANELNAAYAADGYARIKGMSCIITTFGVGELSALNGIAGSYAEHVGVLHVVGVPSISSQAKQLLLHHTLGNGDFTVFHRMSANISETTAMITDIANAPAEIDRCIRTTYTTQRPVYLGLPANLVDLNVPAKLLETPIDLSLKPNDAEAEAEVVRTVVELIKDAKNPVILADACASRHDVKAETKKLMDLTQFPVYVTPMGKGAIDEQHPRYGGVYVGTLSRPEVKKAVESADLILSIGALLSDFNTGSFSYSYKTKNIVEFHSDHIKIRNATFPGVQMKFALQKLLDAIPEVVKDYKPVAVPARVPITKSTPANTPMKQEWMWNHLGNFLREGDIVIAETGTSAFGINQTTFPTDVYAIVQVLWGSIGFTVGALLGATMAAEELDPKKRVILFIGDGSLQLTVQEISTMIRWGLKPYIFVLNNNGYTIEKLIHGPHAEYNEIQGWDHLALLPTFGARNYETHRVATTGEWEKLTQDKDFQDNSKIRMIEVMLPVFDAPQNLVKQAQLTAATNAKQ"},{"created_at":"2011-05-24T20:27:16.000Z","updated_at":"2011-07-22T17:53:52.000Z","name":"Pyruvate decarboxylase isozyme 3","uniprot_id":"P26263","uniprot_name":"PDC6_YEAST","enzyme":true,"transporter":false,"gene_name":"PDC6","num_residues":563,"molecular_weight":"61579.89844","theoretical_pi":"6.11","general_function":"Involved in magnesium ion binding","specific_function":"Minor of three pyruvate decarboxylases (PDC1, PDC5, PDC6) implicated in the nonoxidative conversion of pyruvate to acetaldehyde and carbon dioxide during alcoholic fermentation. Most of the produced acetaldehyde is subsequently reduced to ethanol, but some is required for cytosolic acetyl-CoA production for biosynthetic pathways. The enzyme is also one of five 2-oxo acid decarboxylases (PDC1, PDC5, PDC6, ARO10, and THI3) able to decarboxylate more complex 2-oxo acids (alpha-keto-acids) than pyruvate, which seem mainly involved in amino acid catabolism. Here the enzyme catalyzes the decarboxylation of amino acids, which, in a first step, have been transaminated to the corresponding 2-oxo acids. In a third step, the resulting aldehydes are reduced to alcohols, collectively referred to as fusel oils or alcohols. Its preferred substrates are the transaminated amino acids valine, isoleucine, phenylalanine, and tryptophan, whereas leucine is no substrate. In a side-reaction the carbanionic intermediate (or active aldehyde) generated by decarboxylation or by activation of an aldehyde can react with an aldehyde via condensation (or carboligation) yielding a 2-hydroxy ketone, collectively called acyloins. The expression level of this protein in the presence of fermentable carbon sources is so low that it can not compensate for the other two pyruvate decarboxylases to sustain fermentation","reactions":[{"id":1184,"direction":"\u003e","locations":"cytoplasm","altext":null,"export":true,"pw_reaction_id":null,"source":null},{"id":1186,"direction":"\u003e","locations":"cytoplasm","altext":null,"export":true,"pw_reaction_id":null,"source":null},{"id":1228,"direction":"\u003e","locations":"cytoplasm","altext":null,"export":true,"pw_reaction_id":null,"source":null},{"id":1658,"direction":"\u003c\u003e","locations":"cytoplasm","altext":null,"export":true,"pw_reaction_id":null,"source":null},{"id":1841,"direction":"\u003e","locations":"cytoplasm","altext":null,"export":true,"pw_reaction_id":null,"source":null},{"id":1933,"direction":"\u003e","locations":"cytoplasm","altext":null,"export":true,"pw_reaction_id":null,"source":null},{"id":1934,"direction":"\u003e","locations":"cytoplasm","altext":null,"export":true,"pw_reaction_id":null,"source":null},{"id":2319,"direction":"\u003e","locations":"Cytoplasm. Nucleus;Cytoplasm;Nucleus","altext":"A 2-oxo acid = an aldehyde + CO(2).","export":false,"pw_reaction_id":null,"source":null},{"id":2320,"direction":"\u003e","locations":"Cytoplasm. Nucleus;Cytoplasm","altext":"3-(indol-3-yl)pyruvate = 2-(indol-3-yl)acetaldehyde + CO(2).","export":false,"pw_reaction_id":null,"source":null},{"id":2321,"direction":"\u003e","locations":"Cytoplasm. Nucleus;Cytoplasm","altext":"Phenylpyruvate = phenylacetaldehyde + CO(2).","export":false,"pw_reaction_id":null,"source":null},{"id":2322,"direction":"\u003e","locations":"Cytoplasm. Nucleus;Cytoplasm","altext":"Pyruvate = Acetaldehyde + CO(2).","export":false,"pw_reaction_id":null,"source":null},{"id":2323,"direction":"\u003e","locations":"Cytoplasm. Nucleus;Cytoplasm","altext":"A 2-oxo acid + an aldehyde = A 2-hydroxy ketone + CO(2).","export":false,"pw_reaction_id":null,"source":null},{"id":2324,"direction":"\u003e","locations":"Cytoplasm. Nucleus;Cytoplasm","altext":"An aldehyde + an aldehyde = A 2-hydroxy ketone.","export":false,"pw_reaction_id":null,"source":null},{"id":14096,"direction":"\u003e","locations":null,"altext":null,"export":true,"pw_reaction_id":"PW_R006520","source":"Smpdb"},{"id":14097,"direction":"\u003e","locations":null,"altext":null,"export":true,"pw_reaction_id":"PW_R006525","source":"Smpdb"},{"id":14098,"direction":"\u003e","locations":null,"altext":null,"export":true,"pw_reaction_id":"PW_R006537","source":"Smpdb"},{"id":14099,"direction":"\u003e","locations":null,"altext":null,"export":true,"pw_reaction_id":"PW_R006557","source":"Smpdb"},{"id":14100,"direction":"\u003e","locations":null,"altext":null,"export":true,"pw_reaction_id":"PW_R006971","source":"Smpdb"},{"id":14101,"direction":"\u003e","locations":null,"altext":null,"export":true,"pw_reaction_id":"PW_R006979","source":"Smpdb"},{"id":14283,"direction":"\u003e","locations":null,"altext":null,"export":true,"pw_reaction_id":"PW_R006759","source":"Smpdb"},{"id":14285,"direction":"\u003e","locations":null,"altext":null,"export":true,"pw_reaction_id":"PW_R006770","source":"Smpdb"}],"signal_regions":"None","transmembrane_regions":"None","pdb_id":null,"cellular_location":"Cytoplasm","genbank_gene_id":"X55905","genbank_protein_id":"4116","gene_card_id":"PDC6","chromosome_location":"chromosome 7","locus":"YGR087C","synonyms":[],"enzyme_classes":["4.1.1.-","4.1.1.1"],"go_classes":[{"category":"Component","description":" Not Available"},{"category":"Function","description":" metal ion binding"},{"category":"Function","description":" vitamin binding"},{"category":"Function","description":" magnesium ion binding"},{"category":"Function","description":" thiamin pyrophosphate binding"},{"category":"Function","description":" catalytic activity"},{"category":"Function","description":" transferase activity"},{"category":"Function","description":" lyase activity"},{"category":"Function","description":" carbon-carbon lyase activity"},{"category":"Function","description":" carboxy-lyase activity"},{"category":"Function","description":" binding"},{"category":"Function","description":" ion binding"},{"category":"Function","description":" cation binding"},{"category":"Process","description":" Not Available"}],"pfams":[{"name":"TPP_enzyme_C","identifier":"PF02775"},{"name":"TPP_enzyme_M","identifier":"PF00205"},{"name":"TPP_enzyme_N","identifier":"PF02776"}],"pathways":[{"name":"Glycolysis / Gluconeogenesis","kegg_map_id":"00010"},{"name":"Ethanol fermentation","kegg_map_id":null},{"name":"Isoleucine degradation","kegg_map_id":null},{"name":"Phenylalanine metabolism","kegg_map_id":"00360"},{"name":"Pyruvate metabolism","kegg_map_id":"00620"},{"name":"Tryptophan metabolism","kegg_map_id":"00380"},{"name":"Tyrosine metabolism","kegg_map_id":"00350"},{"name":"Valine Biosynthesis","kegg_map_id":null},{"name":"Valine Degradation","kegg_map_id":null},{"name":"isoleucine biosynthesis","kegg_map_id":null}],"gene_sequence":"ATGTCTGAAATTACTCTTGGAAAATACTTATTTGAAAGATTGAAGCAAGTTAATGTTAACACCATTTTTGGGCTACCAGGCGACTTCAACTTGTCCCTATTGGACAAGATTTACGAGGTAGATGGATTGAGATGGGCTGGTAATGCAAATGAGCTGAACGCCGCCTATGCCGCCGATGGTTACGCACGCATCAAGGGTTTATCTGTGCTGGTAACTACTTTTGGCGTAGGTGAATTATCCGCCTTGAATGGTATTGCAGGATCGTATGCAGAACACGTCGGTGTACTGCATGTTGTTGGTGTCCCCTCTATCTCCGCTCAGGCTAAGCAATTGTTGTTGCATCATACCTTGGGTAACGGTGATTTTACCGTTTTTCACAGAATGTCCGCCAATATCTCAGAAACTACATCAATGATTACAGACATTGCTACAGCCCCTTCAGAAATCGATAGGTTGATCAGGACAACATTTATAACACAAAGGCCTAGCTACTTGGGGTTGCCAGCGAATTTGGTAGATCTAAAGGTTCCTGGTTCTCTTTTGGAAAAACCGATTGATCTATCATTAAAACCTAACGATCCCGAAGCTGAAAAGGAAGTTATTGATACCGTACTAGAATTGATCCAGAATTCGAAAAACCCTGTTATACTATCGGATGCCTGTGCTTCTAGGCACAACGTTAAAAAAGAAACCCAGAAGTTAATTGATTTGACGCAATTCCCAGCTTTTGTGACACCTCTAGGTAAAGGGTCAATAGATGAACAGCATCCCAGATATGGCGGTGTTTATGTGGGAACGCTGTCCAAACAAGACGTGAAACAGGCCGTTGAGTCGGCTGATTTGATCCTTTCGGTCGGTGCTTTGCTCTCTGATTTTAACACAGGTTCGTTTTCCTACTCCTACAAGACTAAAAATGTAGTGGAGTTTCATTCCGATTACGTAAAGGTGAAGAACGCTACGTTCCTCGGTGTACAAATGAAATTTGCACTACAAAACTTACTGAAGGTTATTCCCGATGTTGTTAAGGGCTACAAGAGCGTTCCCGTACCAACCAAAACTCCCGCAAACAAAGGTGTACCTGCTAGCACGCCCTTGAAACAAGAGTGGTTGTGGAACGAATTGTCCAAATTCTTGCAAGAAGGTGATGTTATCATTTCCGAGACCGGCACGTCTGCCTTCGGTATCAATCAAACTATCTTTCCTAAGGACGCCTACGGTATCTCGCAGGTGTTGTGGGGGTCCATCGGTTTTACAACAGGAGCAACTTTAGGTGCTGCCTTTGCCGCTGAGGAGATTGACCCCAACAAGAGAGTCATCTTATTCATAGGTGACGGGTCTTTGCAGTTAACCGTCCAAGAAATCTCCACCATGATCAGATGGGGGTTAAAGCCGTATCTTTTTGTCCTTAACAACGACGGCTACACTATCGAAAAGCTGATTCATGGGCCTCACGCAGAGTACAACGAAATCCAGACCTGGGATCACCTCGCCCTGTTGCCCGCATTTGGTGCGAAAAAGTACGAAAATCACAAGATCGCCACTACGGGTGAGTGGGATGCCTTAACCACTGATTCAGAGTTCCAGAAAAACTCGGTGATCAGACTAATTGAACTGAAACTGCCCGTCTTTGATGCTCCGGAAAGTTTGATCAAACAAGCGCAATTGACTGCCGCTACAAATGCCAAACAATAA","protein_sequence":"MSEITLGKYLFERLKQVNVNTIFGLPGDFNLSLLDKIYEVDGLRWAGNANELNAAYAADGYARIKGLSVLVTTFGVGELSALNGIAGSYAEHVGVLHVVGVPSISAQAKQLLLHHTLGNGDFTVFHRMSANISETTSMITDIATAPSEIDRLIRTTFITQRPSYLGLPANLVDLKVPGSLLEKPIDLSLKPNDPEAEKEVIDTVLELIQNSKNPVILSDACASRHNVKKETQKLIDLTQFPAFVTPLGKGSIDEQHPRYGGVYVGTLSKQDVKQAVESADLILSVGALLSDFNTGSFSYSYKTKNVVEFHSDYVKVKNATFLGVQMKFALQNLLKVIPDVVKGYKSVPVPTKTPANKGVPASTPLKQEWLWNELSKFLQEGDVIISETGTSAFGINQTIFPKDAYGISQVLWGSIGFTTGATLGAAFAAEEIDPNKRVILFIGDGSLQLTVQEISTMIRWGLKPYLFVLNNDGYTIEKLIHGPHAEYNEIQTWDHLALLPAFGAKKYENHKIATTGEWDALTTDSEFQKNSVIRLIELKLPVFDAPESLIKQAQLTAATNAKQ"},{"created_at":"2011-05-24T20:31:18.000Z","updated_at":"2011-07-22T17:53:52.000Z","name":"Pyruvate decarboxylase isozyme 1","uniprot_id":"P06169","uniprot_name":"PDC1_YEAST","enzyme":true,"transporter":false,"gene_name":"PDC1","num_residues":563,"molecular_weight":"61494.89844","theoretical_pi":"6.11","general_function":"Involved in magnesium ion binding","specific_function":"Major of three pyruvate decarboxylases (PDC1, PDC5, PDC6) implicated in the nonoxidative conversion of pyruvate to acetaldehyde and carbon dioxide during alcoholic fermentation. Most of the produced acetaldehyde is subsequently reduced to ethanol, but some is required for cytosolic acetyl-CoA production for biosynthetic pathways. The enzyme is also one of five 2-oxo acid decarboxylases (PDC1, PDC5, PDC6, ARO10, and THI3) able to decarboxylate more complex 2-oxo acids (alpha-ketoacids) than pyruvate, which seem mainly involved in amino acid catabolism. Here the enzyme catalyzes the decarboxylation of amino acids, which, in a first step, have been transaminated to the corresponding 2-oxo acids. In a third step, the resulting aldehydes are reduced to alcohols, collectively referred to as fusel oils or alcohols. Its preferred substrates are the transaminated amino acids valine, isoleucine, phenylalanine, and tryptophan, whereas leucine is no substrate. In a side-reaction the carbanionic intermediate (or active aldehyde) generated by decarboxylation or by activation of an aldehyde can react with an aldehyde via condensation (or carboligation) yielding a 2-hydroxy ketone, collectively called acyloins","reactions":[{"id":1184,"direction":"\u003e","locations":"cytoplasm","altext":null,"export":true,"pw_reaction_id":null,"source":null},{"id":1186,"direction":"\u003e","locations":"cytoplasm","altext":null,"export":true,"pw_reaction_id":null,"source":null},{"id":1228,"direction":"\u003e","locations":"cytoplasm","altext":null,"export":true,"pw_reaction_id":null,"source":null},{"id":1658,"direction":"\u003c\u003e","locations":"cytoplasm","altext":null,"export":true,"pw_reaction_id":null,"source":null},{"id":1841,"direction":"\u003e","locations":"cytoplasm","altext":null,"export":true,"pw_reaction_id":null,"source":null},{"id":1933,"direction":"\u003e","locations":"cytoplasm","altext":null,"export":true,"pw_reaction_id":null,"source":null},{"id":1934,"direction":"\u003e","locations":"cytoplasm","altext":null,"export":true,"pw_reaction_id":null,"source":null},{"id":2319,"direction":"\u003e","locations":"Cytoplasm. Nucleus;Cytoplasm;Nucleus","altext":"A 2-oxo acid = an aldehyde + CO(2).","export":false,"pw_reaction_id":null,"source":null},{"id":2320,"direction":"\u003e","locations":"Cytoplasm. Nucleus;Cytoplasm","altext":"3-(indol-3-yl)pyruvate = 2-(indol-3-yl)acetaldehyde + CO(2).","export":false,"pw_reaction_id":null,"source":null},{"id":2321,"direction":"\u003e","locations":"Cytoplasm. Nucleus;Cytoplasm","altext":"Phenylpyruvate = phenylacetaldehyde + CO(2).","export":false,"pw_reaction_id":null,"source":null},{"id":2322,"direction":"\u003e","locations":"Cytoplasm. Nucleus;Cytoplasm","altext":"Pyruvate = Acetaldehyde + CO(2).","export":false,"pw_reaction_id":null,"source":null},{"id":2323,"direction":"\u003e","locations":"Cytoplasm. Nucleus;Cytoplasm","altext":"A 2-oxo acid + an aldehyde = A 2-hydroxy ketone + CO(2).","export":false,"pw_reaction_id":null,"source":null},{"id":2324,"direction":"\u003e","locations":"Cytoplasm. Nucleus;Cytoplasm","altext":"An aldehyde + an aldehyde = A 2-hydroxy ketone.","export":false,"pw_reaction_id":null,"source":null},{"id":14096,"direction":"\u003e","locations":null,"altext":null,"export":true,"pw_reaction_id":"PW_R006520","source":"Smpdb"},{"id":14097,"direction":"\u003e","locations":null,"altext":null,"export":true,"pw_reaction_id":"PW_R006525","source":"Smpdb"},{"id":14098,"direction":"\u003e","locations":null,"altext":null,"export":true,"pw_reaction_id":"PW_R006537","source":"Smpdb"},{"id":14099,"direction":"\u003e","locations":null,"altext":null,"export":true,"pw_reaction_id":"PW_R006557","source":"Smpdb"},{"id":14100,"direction":"\u003e","locations":null,"altext":null,"export":true,"pw_reaction_id":"PW_R006971","source":"Smpdb"},{"id":14101,"direction":"\u003e","locations":null,"altext":null,"export":true,"pw_reaction_id":"PW_R006979","source":"Smpdb"}],"signal_regions":"None","transmembrane_regions":"None","pdb_id":"1QPB","cellular_location":"Cytoplasm. Nucleus","genbank_gene_id":"X77316","genbank_protein_id":"871533","gene_card_id":"PDC1","chromosome_location":"chromosome 12","locus":"YLR044C","synonyms":[],"enzyme_classes":["4.1.1.-","4.1.1.1"],"go_classes":[{"category":"Component","description":" Not Available"},{"category":"Function","description":" metal ion binding"},{"category":"Function","description":" vitamin binding"},{"category":"Function","description":" magnesium ion binding"},{"category":"Function","description":" thiamin pyrophosphate binding"},{"category":"Function","description":" catalytic activity"},{"category":"Function","description":" transferase activity"},{"category":"Function","description":" lyase activity"},{"category":"Function","description":" carbon-carbon lyase activity"},{"category":"Function","description":" carboxy-lyase activity"},{"category":"Function","description":" binding"},{"category":"Function","description":" ion binding"},{"category":"Function","description":" cation binding"},{"category":"Process","description":" Not Available"}],"pfams":[{"name":"TPP_enzyme_C","identifier":"PF02775"},{"name":"TPP_enzyme_M","identifier":"PF00205"},{"name":"TPP_enzyme_N","identifier":"PF02776"}],"pathways":[{"name":"Glycolysis / Gluconeogenesis","kegg_map_id":"00010"},{"name":"Ethanol fermentation","kegg_map_id":null},{"name":"Isoleucine degradation","kegg_map_id":null},{"name":"Phenylalanine metabolism","kegg_map_id":"00360"},{"name":"Pyruvate metabolism","kegg_map_id":"00620"},{"name":"Tryptophan metabolism","kegg_map_id":"00380"},{"name":"Tyrosine metabolism","kegg_map_id":"00350"},{"name":"Valine Degradation","kegg_map_id":null}],"gene_sequence":"ATGTCTGAAATTACTTTGGGTAAATATTTGTTCGAAAGATTAAAGCAAGTCAACGTTAACACCGTTTTCGGTTTGCCAGGTGACTTCAACTTGTCCTTGTTGGACAAGATCTACGAAGTTGAAGGTATGAGATGGGCTGGTAACGCCAACGAATTGAACGCTCGTTACGCCGCTGATGGTTACGCTCGTATCAAGGGTATGTCTTGTATCATCACCACCTTCGGTGTCGGTGAATTGTCTGCTTTGAACGGTATTGCCGGTTCTTACGCTGAACACGTCGGTGTTTTGCACGTTGTTGGTGTCCCATCCATCTCTTCTCAAGCTAAGCAATTGTTGTTGCACCACACCTTGGGTAACGGTGACTTCACTGTTTTCCACAGAATGTCTGCCAACATTTCTGAAACCACTGCTATGATCACTGACATCTGTACCGCCCCAGCTGAAATTGACAGATGTATCAGAACCACTTACGTCACCCAAAGACCAGTCTACTTAGGTTTGCCAGCTAACTTGGTCGACTTGAACGTCCCAGCTAAGTTGTTGCAAACTCCAATTGACATGTCTTTGAAGCCAAACGATGCTGAATCCGAAAAGGAAGTCATTGACACCATCTTGGTCTTGGCTAAGGATGCTAAGAACCCAGTTATCTTGGCTGATGCTTGTTGTTCCAGACACGACGTCAAGGCTGAAACTAAGAAGTTGATTGACTTGACTCAATTCCCAGCTTTCGTCACCCCAATGGGTAAGGGTTCCATTAGCGAACAACACCCAAGATACGGTGGTGTTTACGTCGGTACCTTGTCCAAGCCAGAAGTTAAGGAAGCCGTTGAATCTGCTGACTTGATTTTGTCTGTCGGTGCTTTGTTGTCTGATTTCAACACCGGTTCTTTCTCTTACTCTTACAAGACCAAGAACATTGTCGAATTCCACTCCGACCACATGAAGATCAGAAACGCCACTTTCCCAGGTGTCCAAATGAAATTCGTTTTGCAAAAGTTGTTGACCAATATTGCTGACGCCGCTAAGGGTTACAAGCCAGTTGCTGTCCCAGCTAGAACTCCAGCTAACGCTGCTGTCCCAGCTTCTACCCCATTGAAGCAAGAATGGATGTGGAACCAATTGGGTAACTTCTTGCAAGAAGGTGATGTTGTCATTGCTGAAACCGGTACCTCCGCTTTCGGTATCAACCAAACCACTTTCCCAAACAACACCTACGGTATCTCTCAAGTCTTATGGGGTTCCATTGGTTTCACCACTGGTGCTACCTTGGGTGCTGCTTTCGCTGCTGAAGAAATTGATCCAAAGAAGAGAGTTATCTTATTCATTGGTGACGGTTCTTTGCAATTGACTGTTCAAGAAATCTCCACCATGATCAGATGGGGCTTGAAGCCATACTTGTTCGTCTTGAACAACGATGGTTACACCATTGAAAAGTTGATTCACGGTCCAAAGGCTCAATACAACGAAATTCAAGGTTGGGACCACCTATCCTTGTTGCCAACTTTCGGTGCTAAGGACTACGAAACCCACAGAGTCGCTACCACCGGTGAATGGGACAAGTTGACCCAAGACAAGTCTTTCAACGACAACTCTAAGATCAGAATGATTGAGGTTATGTTGCCAGTCTTCGATGCTCCACAAAACTTGGTTGAACAAGCTAAGTTGACTGCTGCTACCAACGCTAAGCAATAA","protein_sequence":"MSEITLGKYLFERLKQVNVNTVFGLPGDFNLSLLDKIYEVEGMRWAGNANELNAAYAADGYARIKGMSCIITTFGVGELSALNGIAGSYAEHVGVLHVVGVPSISAQAKQLLLHHTLGNGDFTVFHRMSANISETTAMITDIATAPAEIDRCIRTTYVTQRPVYLGLPANLVDLNVPAKLLQTPIDMSLKPNDAESEKEVIDTILALVKDAKNPVILADACCSRHDVKAETKKLIDLTQFPAFVTPMGKGSIDEQHPRYGGVYVGTLSKPEVKEAVESADLILSVGALLSDFNTGSFSYSYKTKNIVEFHSDHMKIRNATFPGVQMKFVLQKLLTTIADAAKGYKPVAVPARTPANAAVPASTPLKQEWMWNQLGNFLQEGDVVIAETGTSAFGINQTTFPNNTYGISQVLWGSIGFTTGATLGAAFAAEEIDPKKRVILFIGDGSLQLTVQEISTMIRWGLKPYLFVLNNDGYTIEKLIHGPKAQYNEIQGWDHLSLLPTFGAKDYETHRVATTGEWDKLTQDKSFNDNSKIRMIEIMLPVFDAPQNLVEQAKLTAATNAKQ"},{"created_at":"2011-05-27T01:43:51.000Z","updated_at":"2011-05-29T05:06:34.000Z","name":"Probable diacetyl reductase [(R)-acetoin forming] 2","uniprot_id":"P39713","uniprot_name":"BDH2_YEAST","enzyme":true,"transporter":false,"gene_name":"BDH2","num_residues":417,"molecular_weight":"46098.19922","theoretical_pi":"6.03","general_function":"Involved in zinc ion binding","specific_function":"Catalyzes the irreversible reduction of 2,3-butanediol to (S)-acetoin in the presence of NADH (Potential)","reactions":[{"id":2640,"direction":"\u003e","locations":"Cytoplasm. Nucleus","altext":"(R)-acetoin + NAD(+) = diacetyl + NADH.","export":false,"pw_reaction_id":null,"source":null}],"signal_regions":"None","transmembrane_regions":"None","pdb_id":null,"cellular_location":"Cytoplasm. Nucleus","genbank_gene_id":"AY692730","genbank_protein_id":"51012911","gene_card_id":"BDH2","chromosome_location":"chromosome 1","locus":"YAL061W","synonyms":[],"enzyme_classes":["1.1.1.303"],"go_classes":[{"category":"Component","description":" Not Available"},{"category":"Function","description":" zinc ion binding"},{"category":"Function","description":" catalytic activity"},{"category":"Function","description":" binding"},{"category":"Function","description":" ion binding"},{"category":"Function","description":" cation binding"},{"category":"Function","description":" metal ion binding"},{"category":"Function","description":" transition metal ion binding"},{"category":"Function","description":" oxidoreductase activity"},{"category":"Process","description":" metabolic process"},{"category":"Process","description":" oxidation reduction"}],"pfams":[{"name":"ADH_N","identifier":"PF08240"},{"name":"ADH_zinc_N","identifier":"PF00107"}],"pathways":[{"name":"Butanoate metabolism","kegg_map_id":"00650"}],"gene_sequence":"ATGAGAGCCTTAGCGTATTTCGGTAAAGGTAACATCAGATTCACCAACCATTTAAAGGAGCCACATATTGTGGCGCCCGATGAGCTTGTGATTGATATCGAATGGTGTGGTATTTGCGGTACGGACCTGCATGAGTACACAGATGGTCCTATCTTTTTCCCAGAAGATGGACACACACATGAGATTAGTCATAACCCATTGCCACAGGCGATGGGCCACGAAATGGCTGGTACCGTTTTGGAGGTGGGCCCTGGTGTGAAAAACTTGAAAGTGGGAGACAAGGTAGTTGTCGAGCCCACAGGTACATGCAGAGACCGGTATCGTTGGCCCCTGTCGCCAAACGTTGACAAGGAATGGTGCGCTGCTTGCAAAAAGGGCTACTATAACATTTGTTCATATTTGGGGCTTTGTGGTGCGGGTGTGCAGAGCGGTGGATTTGCAGAACGTGTTGTGATGAACGAATCTCACTGCTACAAAGTACCGGACTTCGTGCCCTTAGACGTTGCAGCTTTGATTCAACCGTTGGCTGTGTGCTGGCATGCAATTAGAGTCTGCGAGTTCAAAGCAGGCTCTACGGCTTTGATCATTGGTGCTGGCCCCATCGGACTGGGCACGATACTGGCGTTGAACGCTGCAGGTTGCAAGGACATCGTCGTTTCAGAGCCTGCCAAGGTAAGAAGAGAACTGGCTGAAAAAATGGGTGCCAGGGTTTACGACCCAACTGCGCACGCTGCCAAGGAGAGCATTGATTATCTGAGGTCGATTGCTGATGGTGGAGACGGCTTCGATTACACATTTGATTGCTCCGGGTTGGAAGTCACATTGAATGCTGCTATTCAGTGTCTCACTTTCAGAGGCACCGCAGTGAACTTGGCCATGTGGGGCCATCACAAGATACAGTTTTCTCCGATGGACATCACATTGCATGAAAGAAAGTACACAGGGTCCATGTGCTACACACACCACGATTTTGAGGCAGTAATAGAAGCTTTGGAAGAAGGCAGGATTGACATTGATAGAGCAAGACATATGATAACGGGCAGAGTCAACATTGAGGACGGCCTTGATGGCGCCATCATGAAGCTGATAAACGAGAAGGAGTCTACAATCAAGATTATTCTGACTCCAAACAATCACGGAGAGTTGAACAGGGAAGCCGATAATGAGAAGAAAGAAATTTCCGAGCTGAGCAGTCGGAAAGATCAAGAAAGACTACGAGAATCAATAAACGAGGCTAAACTGCGTCACACATGA","protein_sequence":"MRALAYFGKGNIRFTNHLKEPHIVAPDELVIDIEWCGICGTDLHEYTDGPIFFPEDGHTHEISHNPLPQAMGHEMAGTVLEVGPGVKNLKVGDKVVVEPTGTCRDRYRWPLSPNVDKEWCAACKKGYYNICSYLGLCGAGVQSGGFAERVVMNESHCYKVPDFVPLDVAALIQPLAVCWHAIRVCEFKAGSTALIIGAGPIGLGTILALNAAGCKDIVVSEPAKVRRELAEKMGARVYDPTAHAAKESIDYLRSIADGGDGFDYTFDCSGLEVTLNAAIQCLTFRGTAVNLAMWGHHKIQFSPMDITLHERKYTGSMCYTHHDFEAVIEALEEGRIDIDRARHMITGRVNIEDGLDGAIMKLINEKESTIKIILTPNNHGELNREADNEKKEISELSSRKDQERLRESINEAKLRHT"},{"created_at":"2011-05-27T01:46:39.000Z","updated_at":"2011-07-22T17:53:39.000Z","name":"Diacetyl reductase [(R)-acetoin forming]","uniprot_id":"P39714","uniprot_name":"BDH1_YEAST","enzyme":true,"transporter":false,"gene_name":"BDH1","num_residues":382,"molecular_weight":"41537.69922","theoretical_pi":"6.65","general_function":"Involved in zinc ion binding","specific_function":"Catalyzes the irreversible reduction of 2,3-butanediol to (S)-acetoin in the presence of NADH","reactions":[{"id":1126,"direction":"\u003c\u003e","locations":"cytoplasm","altext":null,"export":true,"pw_reaction_id":null,"source":null},{"id":2640,"direction":"\u003e","locations":"Cytoplasm. Nucleus","altext":"(R)-acetoin + NAD(+) = diacetyl + NADH.","export":false,"pw_reaction_id":null,"source":null}],"signal_regions":"None","transmembrane_regions":"None","pdb_id":null,"cellular_location":null,"genbank_gene_id":"U12980","genbank_protein_id":"595526","gene_card_id":"BDH1","chromosome_location":"chromosome 1","locus":"YAL060W","synonyms":[],"enzyme_classes":["1.1.1.303"],"go_classes":[{"category":"Component","description":" Not Available"},{"category":"Function","description":" zinc ion binding"},{"category":"Function","description":" catalytic activity"},{"category":"Function","description":" binding"},{"category":"Function","description":" ion binding"},{"category":"Function","description":" cation binding"},{"category":"Function","description":" metal ion binding"},{"category":"Function","description":" transition metal ion binding"},{"category":"Function","description":" oxidoreductase activity"},{"category":"Process","description":" metabolic process"},{"category":"Process","description":" oxidation reduction"}],"pfams":[{"name":"ADH_N","identifier":"PF08240"},{"name":"ADH_zinc_N","identifier":"PF00107"}],"pathways":[{"name":"Butanoate metabolism","kegg_map_id":"00650"}],"gene_sequence":"ATGAGAGCTTTGGCATATTTCAAGAAGGGTGATATTCACTTCACTAATGATATCCCTAGGCCAGAAATCCAAACCGACGATGAGGTTATTATCGACGTCTCTTGGTGTGGGATTTGTGGCTCGGATCTTCACGAGTACTTGGATGGTCCAATCTTCATGCCTAAAGATGGAGAGTGCCATAAATTATCCAACGCTGCTTTACCTCTGGCAATGGGCCATGAGATGTCAGGAATTGTTTCCAAGGTTGGTCCTAAAGTGACAAAGGTGAAGGTTGGCGACCACGTGGTCGTTGATGCTGCCAGCAGTTGTGCGGACCTGCATTGCTGGCCACACTCCAAATTTTACAATTCCAAACCATGTGATGCTTGTCAGAGGGGCAGTGAAAATCTATGTACCCACGCCGGTTTTGTAGGACTAGGTGTGATCAGTGGTGGCTTTGCTGAACAAGTCGTAGTCTCTCAACATCACATTATCCCGGTTCCAAAGGAAATTCCTCTAGATGTGGCTGCTTTAGTTGAGCCTCTTTCTGTCACCTGGCATGCTGTTAAGATTTCTGGTTTCAAAAAAGGCAGTTCAGCCTTGGTTCTTGGTGCAGGTCCCATTGGGTTGTGTACCATTTTGGTACTTAAGGGAATGGGGGCTAGTAAAATTGTAGTGTCTGAAATTGCAGAGAGAAGAATAGAAATGGCCAAGAAACTGGGCGTTGAGGTGTTCAATCCCTCCAAGCACGGTCATAAATCTATAGAGATACTACGTGGTTTGACCAAGAGCCATGATGGGTTTGATTACAGTTATGATTGTTCTGGTATTCAAGTTACTTTCGAAACCTCTTTGAAGGCATTAACATTCAAGGGGACAGCCACCAACATTGCAGTTTGGGGTCCAAAACCTGTCCCATTCCAACCAATGGATGTGACTCTCCAAGAGAAAGTTATGACTGGTTCGATCGGCTATGTTGTCGAAGCCTTCGAAGAAGTTGTTCGTGCCATCCACAACGGAGACATCGCCATGGAAGATTGTAAGCAACTAATCACTGGTAAGCAAAGGATTGAGGACGGTTGGGAAAAGGGATTCCAAGAGTTGATGGATCACAAGGAATCCAACGTTAAGATTCTATTGACGCCTAACAATCACGGTGAAATGAAGTAA","protein_sequence":"MRALAYFKKGDIHFTNDIPRPEIQTDDEVIIDVSWCGICGSDLHEYLDGPIFMPKDGECHKLSNAALPLAMGHEMSGIVSKVGPKVTKVKVGDHVVVDAASSCADLHCWPHSKFYNSKPCDACQRGSENLCTHAGFVGLGVISGGFAEQVVVSQHHIIPVPKEIPLDVAALVEPLSVTWHAVKISGFKKGSSALVLGAGPIGLCTILVLKGMGASKIVVSEIAERRIEMAKKLGVEVFNPSKHGHKSIEILRGLTKSHDGFDYSYDCSGIQVTFETSLKALTFKGTATNIAVWGPKPVPFQPMDVTLQEKVMTGSIGYVVEAFEEVVRAIHNGDIAMEDCKQLITGKQRIEDGWEKGFQELMDHKESNVKILLTPNNHGEMK"}]}