{"ymdb_id":"YMDB00499","created_at":"2011-05-29T18:23:56.000Z","updated_at":"2016-09-08T18:35:32.000Z","name":"3-methylbutanal","cas":"590-86-3","state":"Liquid","melting_point":"-51 oC","description":"3-Methylbutanal (isovaleraldehyde) is a leucine degradation product[Biocyc PWY-5076]. It has been suggested that 3-Methylbutanal is a signalling molecule involved in the filimentation of Saccharomyces cerevisiae.[PMID: 16999827]","experimental_water_solubility":"14 mg/mL at 20 oC [FALBE,J et al. (1985)]","experimental_logp_hydrophobicity":null,"location":"extracellular;mitochondrion;cytoplasm","synthesis_reference":"Roelen, O.  Synthesis of aldehydes and derivatives from olefins, carbon monoxide, and hydrogen.    Angew. Chem.  (1948),  A60  62.  CAN 44:46679  AN 1950:46679 ","chebi_id":"16638","hmdb_id":"HMDB06478","kegg_id":"C07329","pubchem_id":"7284","cs_id":"11065","foodb_id":null,"wikipedia_link":null,"biocyc_id":null,"iupac":"3-methylbutanal","traditional_iupac":"isovaleraldehyde","logp":"1.0501616416666666","pka":null,"alogps_solubility":"1.70e+01 g/l","alogps_logp":"1.29","alogps_logs":"-0.71","acceptor_count":"1","donor_count":"0","rotatable_bond_count":"2","polar_surface_area":"17.07","refractivity":"25.494799999999998","polarizability":"10.12084477416142","formal_charge":"0","physiological_charge":"0","pka_strongest_basic":"-6.950085545908737","pka_strongest_acidic":"18.56011290069315","bioavailability":"1","number_of_rings":"0","rule_of_five":"1","ghose_filter":"0","veber_rule":"1","mddr_like_rule":"0","synonyms":["\u0026beta;-Methylbutanal","1-Butanal, 3-methyl-","2-Methylbutanal-4","3-methyl-1-Butanal","3-methyl-Butanal","3-methyl-Butyraldehyde","3-Methylbutan-1-al","3-Methylbutanal","3-Methylbutyraldehyde","b-Methylbutanal","beta-methylbutanal","Butanal, 3-methyl-","Butyraldehyde, 3-methyl-","Isoamyl aldehyde","Isoamylaldehyde","Isopentaldehyde","Isopentanal","Isovaleral","Isovaleraldehyde","Isovaleric aldehyde","Isovalerylaldehyde","Methyl butanal"],"pathways":[{"name":"Leucine Degradation","kegg_map_id":null}],"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":12702265,"citation":"Leskovac, V., Trivic, S., Pericin, D. (2002). \"The three zinc-containing alcohol dehydrogenases from baker's yeast, Saccharomyces cerevisiae.\" FEMS Yeast Res 2:481-494."},{"pubmed_id":17287358,"citation":"Chi, A., Huttenhower, C., Geer, L. Y., Coon, J. J., Syka, J. E., Bai, D. L., Shabanowitz, J., Burke, D. J., Troyanskaya, O. G., Hunt, D. F. (2007). \"Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry.\" Proc Natl Acad Sci U S A 104:2193-2198."},{"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":12423374,"citation":"Larroy, C., Pares, X., Biosca, J. A. (2002). \"Characterization of a Saccharomyces cerevisiae NADP(H)-dependent alcohol dehydrogenase (ADHVII), a member of the cinnamyl alcohol dehydrogenase family.\" Eur J Biochem 269:5738-5745."},{"pubmed_id":12499363,"citation":"Dickinson, J. R., Salgado, L. E., Hewlins, M. J. (2003). \"The catabolism of amino acids to long chain and complex alcohols in Saccharomyces cerevisiae.\" J Biol Chem 278:8028-8034."},{"pubmed_id":11742541,"citation":"Larroy, C., Fernandez, M. R., Gonzalez, E., Pares, X., Biosca, J. A. (2002). \"Characterization of the Saccharomyces cerevisiae YMR318C (ADH6) gene product as a broad specificity NADPH-dependent alcohol dehydrogenase: relevance in aldehyde reduction.\" Biochem J 361:163-172."},{"pubmed_id":16999827,"citation":"Hauser, M., Horn, P., Tournu, H., Hauser, N. C., Hoheisel, J. D., Brown, A. J., Dickinson, J. R. (2007). \"A transcriptome analysis of isoamyl alcohol-induced filamentation in yeast reveals a novel role for Gre2p as isovaleraldehyde reductase.\" FEMS Yeast Res 7:84-92."}],"proteins":[{"created_at":"2011-05-24T20:23:50.000Z","updated_at":"2011-07-22T17:54:09.000Z","name":"Alcohol dehydrogenase 3, mitochondrial","uniprot_id":"P07246","uniprot_name":"ADH3_YEAST","enzyme":true,"transporter":false,"gene_name":"ADH3","num_residues":375,"molecular_weight":"40369.19922","theoretical_pi":"8.62","general_function":"Involved in zinc ion binding","specific_function":"An alcohol + NAD(+) = an aldehyde or ketone + NADH","reactions":[{"id":1293,"direction":"\u003e","locations":"mitochondrion","altext":null,"export":true,"pw_reaction_id":null,"source":null},{"id":1294,"direction":"\u003e","locations":"mitochondrion;cytoplasm","altext":null,"export":true,"pw_reaction_id":null,"source":null},{"id":1296,"direction":"\u003e","locations":"mitochondrion;cytoplasm","altext":null,"export":true,"pw_reaction_id":null,"source":null},{"id":1303,"direction":"\u003e","locations":"mitochondrion;cytoplasm","altext":null,"export":true,"pw_reaction_id":null,"source":null},{"id":1305,"direction":"\u003e","locations":"mitochondrion;cytoplasm","altext":null,"export":true,"pw_reaction_id":null,"source":null},{"id":1308,"direction":"\u003e","locations":"mitochondrion;cytoplasm","altext":null,"export":true,"pw_reaction_id":null,"source":null},{"id":2314,"direction":"\u003e","locations":"Mitochondrion matrix;Cytoplasm;Mitochondrion","altext":"An alcohol + NAD(+) = an aldehyde or ketone + NADH.","export":false,"pw_reaction_id":null,"source":null}],"signal_regions":"None","transmembrane_regions":"None","pdb_id":null,"cellular_location":"Mitochondrion matrix","genbank_gene_id":"AY692988","genbank_protein_id":"51013427","gene_card_id":"ADH3","chromosome_location":"chromosome 13","locus":"YMR083W","synonyms":["Alcohol dehydrogenase III","YADH-3"],"enzyme_classes":["1.1.1.1"],"go_classes":[{"category":"Component","description":" Not Available"},{"category":"Function","description":" metal ion binding"},{"category":"Function","description":" transition metal ion binding"},{"category":"Function","description":" oxidoreductase activity"},{"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":"Process","description":" oxidation reduction"},{"category":"Process","description":" metabolic process"}],"pfams":[{"name":"ADH_N","identifier":"PF08240"},{"name":"ADH_zinc_N","identifier":"PF00107"}],"pathways":[{"name":"Glycolysis / Gluconeogenesis","kegg_map_id":"00010"},{"name":"Fatty acid metabolism","kegg_map_id":"00071"},{"name":"Glycine, serine and threonine metabolism","kegg_map_id":"00260"},{"name":"Tyrosine metabolism","kegg_map_id":"00350"}],"gene_sequence":"ATGTTGAGAACGTCAACATTGTTCACCAGGCGTGTCCAACCAAGCCTATTTTCTAGAAACATTCTTAGATTGCAATCCACAGCTGCAATCCCTAAGACTCAAAAAGGTGTCATCTTTTATGAGAATAAGGGGAAGCTGCATTACAAAGATATCCCTGTCCCCGAGCCTAAGCCAAATGAAATTTTAATCAACGTTAAATATTCTGGTGTATGTCACACCGATTTACATGCTTGGCACGGCGATTGGCCATTACCTGTTAAACTACCATTAGTAGGTGGTCATGAAGGTGCTGGTGTAGTTGTCAAACTAGGTTCCAATGTCAAGGGCTGGAAAGTCGGTGATTTAGCAGGTATCAAATGGCTGAACGGTTCTTGTATGACATGCGAATTCTGTGAATCAGGTCATGAATCAAATTGTCCAGATGCTGATTTATCTGGTTACACTCATGATGGTTCTTTCCAACAATTTGCGACCGCTGATGCTATTCAAGCCGCCAAAATTCAACAGGGTACCGACTTGGCCGAAGTAGCCCCAATATTATGTGCTGGTGTTACTGTATATAAAGCACTAAAAGAGGCAGACTTGAAAGCTGGTGACTGGGTTGCCATCTCTGGTGCTGCAGGTGGCTTGGGTTCCTTGGCCGTTCAATATGCAACTGCGATGGGTTACAGAGTTCTAGGTATTGATGCAGGTGAGGAAAAGGAAAAACTTTTCAAGAAATTGGGGGGTGAAGTATTCATCGACTTTACTAAAACAAAGAATATGGTTTCTGACATTCAAGAAGCTACCAAAGGTGGCCCTCATGGTGTCATTAACGTTTCCGTTTCTGAAGCCGCTATTTCTCTATCTACGGAATATGTTAGACCATGTGGTACCGTCGTTTTGGTTGGTTTGCCCGCTAACGCCTACGTTAAATCAGAGGTATTCTCTCATGTGGTGAAGTCCATCAATATCAAGGGTTCTTATGTTGGTAACAGAGCTGATACGAGAGAAGCCTTAGACTTCTTTAGCAGAGGTTTGATCAAATCACCAATCAAAATTGTTGGATTATCTGAATTACCAAAGGTTTATGACTTGATGGAAAAGGGCAAGATTTTGGGTAGATACGTCGTCGATACTAGTAAATAA","protein_sequence":"MLRTSTLFTRRVQPSLFSRNILRLQSTAAIPKTQKGVIFYENKGKLHYKDIPVPEPKPNEILINVKYSGVCHTDLHAWHGDWPLPVKLPLVGGHEGAGVVVKLGSNVKGWKVGDLAGIKWLNGSCMTCEFCESGHESNCPDADLSGYTHDGSFQQFATADAIQAAKIQQGTDLAEVAPILCAGVTVYKALKEADLKAGDWVAISGAAGGLGSLAVQYATAMGYRVLGIDAGEEKEKLFKKLGGEVFIDFTKTKNMVSDIQEATKGGPHGVINVSVSEAAISLSTEYVRPCGTVVLVGLPANAYVKSEVFSHVVKSINIKGSYVGNRADTREALDFFSRGLIKSPIKIVGLSELPKVYDLMEKGKILGRYVVDTSK"},{"created_at":"2011-05-24T20:25:28.000Z","updated_at":"2011-07-22T17:54:08.000Z","name":"S-(hydroxymethyl)glutathione dehydrogenase","uniprot_id":"P32771","uniprot_name":"FADH_YEAST","enzyme":true,"transporter":false,"gene_name":"SFA1","num_residues":386,"molecular_weight":"41041.69922","theoretical_pi":"6.76","general_function":"Involved in zinc ion binding","specific_function":"Oxidizes long-chain alcohols and, in the presence of glutathione, is able to oxidize formaldehyde. Is responsible for yeast resistance to formaldehyde","reactions":[{"id":1291,"direction":"\u003c\u003e","locations":"cytoplasm","altext":null,"export":true,"pw_reaction_id":null,"source":null},{"id":1294,"direction":"\u003e","locations":"mitochondrion;cytoplasm","altext":null,"export":true,"pw_reaction_id":null,"source":null},{"id":1296,"direction":"\u003e","locations":"mitochondrion;cytoplasm","altext":null,"export":true,"pw_reaction_id":null,"source":null},{"id":1303,"direction":"\u003e","locations":"mitochondrion;cytoplasm","altext":null,"export":true,"pw_reaction_id":null,"source":null},{"id":1305,"direction":"\u003e","locations":"mitochondrion;cytoplasm","altext":null,"export":true,"pw_reaction_id":null,"source":null},{"id":1308,"direction":"\u003e","locations":"mitochondrion;cytoplasm","altext":null,"export":true,"pw_reaction_id":null,"source":null},{"id":1545,"direction":"\u003c\u003e","locations":"cytoplasm","altext":null,"export":true,"pw_reaction_id":null,"source":null},{"id":2317,"direction":"\u003e","locations":null,"altext":"S-(hydroxymethyl)glutathione + NAD(P)(+) = S-formylglutathione + NAD(P)H.","export":false,"pw_reaction_id":null,"source":null},{"id":2314,"direction":"\u003e","locations":"Mitochondrion matrix;Cytoplasm;Mitochondrion","altext":"An alcohol + NAD(+) = an aldehyde or ketone + NADH.","export":false,"pw_reaction_id":null,"source":null}],"signal_regions":"None","transmembrane_regions":"None","pdb_id":null,"cellular_location":null,"genbank_gene_id":"X68020","genbank_protein_id":"288591","gene_card_id":"SFA1","chromosome_location":"chromosome 4","locus":"YDL168W","synonyms":["Alcohol dehydrogenase SFA","Glutathione-dependent formaldehyde dehydrogenase","FALDH","FDH","FLD","GSH-FDH"],"enzyme_classes":["1.1.1.284","1.1.1.1","1.1.1.-"],"go_classes":[{"category":"Component","description":" Not Available"},{"category":"Function","description":" metal ion binding"},{"category":"Function","description":" transition metal ion binding"},{"category":"Function","description":" oxidoreductase activity"},{"category":"Function","description":" zinc ion binding"},{"category":"Function","description":" oxidoreductase activity, acting on CH-OH group of donors"},{"category":"Function","description":" oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor"},{"category":"Function","description":" S-(hydroxymethyl)glutathione dehydrogenase activity"},{"category":"Function","description":" catalytic activity"},{"category":"Function","description":" binding"},{"category":"Function","description":" ion binding"},{"category":"Function","description":" cation binding"},{"category":"Process","description":" oxidation reduction"},{"category":"Process","description":" small molecule metabolic process"},{"category":"Process","description":" alcohol metabolic process"},{"category":"Process","description":" monohydric alcohol metabolic process"},{"category":"Process","description":" metabolic process"},{"category":"Process","description":" ethanol metabolic process"},{"category":"Process","description":" ethanol oxidation"}],"pfams":[{"name":"ADH_N","identifier":"PF08240"},{"name":"ADH_zinc_N","identifier":"PF00107"}],"pathways":[{"name":"Methane metabolism","kegg_map_id":"00680"}],"gene_sequence":"ATGTCCGCCGCTACTGTTGGTAAACCTATTAAGTGCATTGCTGCTGTTGCGTATGATGCGAAGAAACCATTAAGTGTTGAAGAAATCACGGTAGACGCCCCAAAAGCGCACGAAGTACGTATCAAAATTGAATATACTGCTGTATGCCACACTGATGCGTACACTTTATCAGGCTCTGATCCAGAAGGACTTTTCCCTTGCGTTCTGGGCCACGAAGGAGCCGGTATCGTAGAATCTGTAGGCGATGATGTCATAACAGTTAAGCCTGGTGATCATGTTATTGCTTTGTACACTGCTGAGTGTGGCAAATGTAAGTTCTGTACTTCCGGTAAAACCAACTTATGTGGTGCTGTTAGAGCTACTCAAGGGAAAGGTGTAATGCCTGATGGGACCACAAGATTTCATAATGCGAAAGGTGAAGATATATACCATTTCATGGGTTGCTCTACTTTTTCCGAATATACTGTGGTGGCAGATGTCTCTGTGGTTGCCATCGATCCAAAAGCTCCCTTGGATGCTGCCTGTTTACTGGGTTGTGGTGTTACTACTGGTTTTGGGGCGGCTCTTAAGACAGCTAATGTGCAAAAAGGCGATACCGTTGCAGTATTTGGCTGCGGGACTGTAGGACTCTCCGTTATCCAAGGTGCAAAGTTAAGGGGCGCTTCCAAGATCATTGCCATTGACATTAACAATAAGAAAAAACAATATTGTTCTCAATTTGGTGCCACGGATTTTGTTAATCCCAAGGAAGATTTGGCCAAAGATCAAACTATCGTTGAAAAGTTAATTGAAATGACTGATGGGGGTCTGGATTTTACTTTTGACTGTACTGGTAATACCAAAATTATGAGAGATGCTTTGGAAGCCTGTCATAAAGGTTGGGGTCAATCTATTATCATTGGTGTGGCTGCCGCTGGTGAAGAAATTTCTACAAGGCCGTTCCAGCTGGTCACTGGTAGAGTGTGGAAAGGCTCTGCTTTTGGTGGCATCAAAGGTAGATCTGAAATGGGCGGTTTAATTAAAGACTATCAAAAAGGTGCCTTAAAAGTCGAAGAATTTATCACTCACAGGAGACCATTCAAAGAAATCAATCAAGCCTTTGAAGATTTGCATAACGGTGATTGCTTAAGAACCGTCTTGAAGTCTGATGAAATAAAATAG","protein_sequence":"MSAATVGKPIKCIAAVAYDAKKPLSVEEITVDAPKAHEVRIKIEYTAVCHTDAYTLSGSDPEGLFPCVLGHEGAGIVESVGDDVITVKPGDHVIALYTAECGKCKFCTSGKTNLCGAVRATQGKGVMPDGTTRFHNAKGEDIYHFMGCSTFSEYTVVADVSVVAIDPKAPLDAACLLGCGVTTGFGAALKTANVQKGDTVAVFGCGTVGLSVIQGAKLRGASKIIAIDINNKKKQYCSQFGATDFVNPKEDLAKDQTIVEKLIEMTDGGLDFTFDCTGNTKIMRDALEACHKGWGQSIIIGVAAAGEEISTRPFQLVTGRVWKGSAFGGIKGRSEMGGLIKDYQKGALKVEEFITHRRPFKEINQAFEDLHNGDCLRTVLKSDEIK"},{"created_at":"2011-05-24T20:29:06.000Z","updated_at":"2011-07-22T17:54:08.000Z","name":"Alcohol dehydrogenase 1","uniprot_id":"P00330","uniprot_name":"ADH1_YEAST","enzyme":true,"transporter":false,"gene_name":"ADH1","num_residues":348,"molecular_weight":"36849.0","theoretical_pi":"6.67","general_function":"Involved in zinc ion binding","specific_function":"This isozyme preferentially catalyzes the conversion of primary unbranched alcohols to their corresponding aldehydes. Also also shows activity toward secondary alcohols","reactions":[{"id":1291,"direction":"\u003c\u003e","locations":"cytoplasm","altext":null,"export":true,"pw_reaction_id":null,"source":null},{"id":1294,"direction":"\u003e","locations":"mitochondrion;cytoplasm","altext":null,"export":true,"pw_reaction_id":null,"source":null},{"id":1296,"direction":"\u003e","locations":"mitochondrion;cytoplasm","altext":null,"export":true,"pw_reaction_id":null,"source":null},{"id":1303,"direction":"\u003e","locations":"mitochondrion;cytoplasm","altext":null,"export":true,"pw_reaction_id":null,"source":null},{"id":1305,"direction":"\u003e","locations":"mitochondrion;cytoplasm","altext":null,"export":true,"pw_reaction_id":null,"source":null},{"id":1308,"direction":"\u003e","locations":"mitochondrion;cytoplasm","altext":null,"export":true,"pw_reaction_id":null,"source":null},{"id":2314,"direction":"\u003e","locations":"Mitochondrion matrix;Cytoplasm;Mitochondrion","altext":"An alcohol + NAD(+) = an aldehyde or ketone + NADH.","export":false,"pw_reaction_id":null,"source":null}],"signal_regions":"None","transmembrane_regions":"None","pdb_id":null,"cellular_location":"Cytoplasm","genbank_gene_id":"M38456","genbank_protein_id":"171025","gene_card_id":"ADH1","chromosome_location":"chromosome 15","locus":"YOL086C","synonyms":["Alcohol dehydrogenase I","YADH-1"],"enzyme_classes":["1.1.1.1"],"go_classes":[{"category":"Component","description":" Not Available"},{"category":"Function","description":" metal ion binding"},{"category":"Function","description":" transition metal ion binding"},{"category":"Function","description":" oxidoreductase activity"},{"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":"Process","description":" oxidation reduction"},{"category":"Process","description":" metabolic process"}],"pfams":[{"name":"ADH_N","identifier":"PF08240"},{"name":"ADH_zinc_N","identifier":"PF00107"}],"pathways":[{"name":"Glycolysis / Gluconeogenesis","kegg_map_id":"00010"},{"name":"Fatty acid metabolism","kegg_map_id":"00071"},{"name":"Glycine, serine and threonine metabolism","kegg_map_id":"00260"},{"name":"Tyrosine metabolism","kegg_map_id":"00350"}],"gene_sequence":"ATGTCTATCCCAGAAACTCAAAAAGGTGTTATCTTCTACGAATCCCACGGTAAATTGGAACACAAGGATATTCCAGTTCCAAAGCCAAAGGCCAACGAATTGTTGATCAACGTTAAGTACTCTGGTGTCTGTCACACCGACTTGCACGCTTGGCACGGTGACTGGCCATTGCCAGTTAAGCTACCATTAGTCGGTGGTCACGAAGGTGCCGGTGTCGTTGTCGGCATGGGTGAAAACGTTAAGGGCTGGAAGATCGGTGACTACGCCGGTATCAAATGGTTGAACGGTTCTTGTATGGCCTGTGAATACTGTGAATTGGGTAACGAATCCAACTGTCCTCACGCTGACTTGTCTGGTTACACCCACGACGGTTCTTTCCAACAATACGCTACCGCTGACGCTGTTCAAGCCGCTCACATTCCTCAAGGTACCGACTTGGCCCAAGTCGCCCCCATCTTGTGTGCTGGTATCACCGTCTACAAGGCTTTGAAGTCTGCTAACTTGATGGCCGGTCATTGGGTTGCCATTTCCGGTGCTGCCGGTGGTCTAGGTTCTTTGGCTGTTCAATACGCCAAGGCTATGGGTTACAGAGTCTTGGGTATTGACGGTGGTGAAGGTAAGGAAGAATTATTCAGATCCATCGGTGGTGAAGTCTTCATTGACTTCACTAAGGAAAAGGACATTGTCGGTGCTGTTCTAAAGGCCACTGACGGTGGTGCTCACGGTGTCATCAACGTTTCCGTTTCCGAAGCCGCTATTGAAGCTTCTACCAGATACGTTAGAGCTAACGGTACCACCGTTTTGGTCGGTATGCCAGCTGGTGCCAAGTGTTGTTCTGATGTCTTCAACCAAGTCGTCAAGTCCATCTCTATTGTTGGTTCTTACGTCGGTAACAGAGCCGACACCAGAGAAGCTTTGGACTTCTTCGCCAGAGGTTTGGTCAAGTCTCCAATCAAGGTTGTCGGCTTGTCTACCTTGCCAGAAATTTACGAAAAGATGGAAAAGGGTCAAATCGTTGGTAGATACGTTGTTGACACTTCTAAATAA","protein_sequence":"MSIPETQKGVIFYESHGKLEYKDIPVPKPKANELLINVKYSGVCHTDLHAWHGDWPLPVKLPLVGGHEGAGVVVGMGENVKGWKIGDYAGIKWLNGSCMACEYCELGNESNCPHADLSGYTHDGSFQQYATADAVQAAHIPQGTDLAQVAPILCAGITVYKALKSANLMAGHWVAISGAAGGLGSLAVQYAKAMGYRVLGIDGGEGKEELFRSIGGEVFIDFTKEKDIVGAVLKATDGGAHGVINVSVSEAAIEASTRYVRANGTTVLVGMPAGAKCCSDVFNQVVKSISIVGSYVGNRADTREALDFFARGLVKSPIKVVGLSTLPEIYEKMEKGQIVGRYVVDTSK"},{"created_at":"2011-05-24T20:30:23.000Z","updated_at":"2011-07-22T17:54:08.000Z","name":"Alcohol dehydrogenase 4","uniprot_id":"P10127","uniprot_name":"ADH4_YEAST","enzyme":true,"transporter":false,"gene_name":"ADH4","num_residues":382,"molecular_weight":"41141.69922","theoretical_pi":"6.09","general_function":"Involved in oxidoreductase activity","specific_function":"Reduces acetaldehyde to ethanol during glucose fermentation. Specific for ethanol. Shows drastically reduced activity towards primary alcohols from 4 carbon atoms upward. Isomers of aliphatic alcohol, as well as secondary alcohols and glycerol are not used at all","reactions":[{"id":1291,"direction":"\u003c\u003e","locations":"cytoplasm","altext":null,"export":true,"pw_reaction_id":null,"source":null},{"id":1294,"direction":"\u003e","locations":"mitochondrion;cytoplasm","altext":null,"export":true,"pw_reaction_id":null,"source":null},{"id":1296,"direction":"\u003e","locations":"mitochondrion;cytoplasm","altext":null,"export":true,"pw_reaction_id":null,"source":null},{"id":1303,"direction":"\u003e","locations":"mitochondrion;cytoplasm","altext":null,"export":true,"pw_reaction_id":null,"source":null},{"id":1305,"direction":"\u003e","locations":"mitochondrion;cytoplasm","altext":null,"export":true,"pw_reaction_id":null,"source":null},{"id":1308,"direction":"\u003e","locations":"mitochondrion;cytoplasm","altext":null,"export":true,"pw_reaction_id":null,"source":null},{"id":2314,"direction":"\u003e","locations":"Mitochondrion matrix;Cytoplasm;Mitochondrion","altext":"An alcohol + NAD(+) = an aldehyde or ketone + NADH.","export":false,"pw_reaction_id":null,"source":null}],"signal_regions":"None","transmembrane_regions":"None","pdb_id":null,"cellular_location":"Mitochondrion","genbank_gene_id":"X05992","genbank_protein_id":"3337","gene_card_id":"ADH4","chromosome_location":"chromosome 7","locus":"YGL256W","synonyms":["Alcohol dehydrogenase IV","ADHIV"],"enzyme_classes":["1.1.1.1"],"go_classes":[{"category":"Component","description":" Not Available"},{"category":"Function","description":" metal ion binding"},{"category":"Function","description":" oxidoreductase activity"},{"category":"Function","description":" catalytic activity"},{"category":"Function","description":" binding"},{"category":"Function","description":" ion binding"},{"category":"Function","description":" cation binding"},{"category":"Process","description":" oxidation reduction"},{"category":"Process","description":" metabolic process"}],"pfams":[{"name":"Fe-ADH","identifier":"PF00465"}],"pathways":[{"name":"Glycolysis / Gluconeogenesis","kegg_map_id":"00010"},{"name":"Fatty acid metabolism","kegg_map_id":"00071"},{"name":"Glycine, serine and threonine metabolism","kegg_map_id":"00260"},{"name":"Tyrosine 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dehydrogenase 5","uniprot_id":"P38113","uniprot_name":"ADH5_YEAST","enzyme":true,"transporter":false,"gene_name":"ADH5","num_residues":351,"molecular_weight":"37647.89844","theoretical_pi":"6.34","general_function":"Involved in zinc ion binding","specific_function":"An alcohol + NAD(+) = an aldehyde or ketone + NADH","reactions":[{"id":1291,"direction":"\u003c\u003e","locations":"cytoplasm","altext":null,"export":true,"pw_reaction_id":null,"source":null},{"id":1294,"direction":"\u003e","locations":"mitochondrion;cytoplasm","altext":null,"export":true,"pw_reaction_id":null,"source":null},{"id":1296,"direction":"\u003e","locations":"mitochondrion;cytoplasm","altext":null,"export":true,"pw_reaction_id":null,"source":null},{"id":1303,"direction":"\u003e","locations":"mitochondrion;cytoplasm","altext":null,"export":true,"pw_reaction_id":null,"source":null},{"id":1305,"direction":"\u003e","locations":"mitochondrion;cytoplasm","altext":null,"export":true,"pw_reaction_id":null,"source":null},{"id":1308,"direction":"\u003e","locations":"mitochondrion;cytoplasm","altext":null,"export":true,"pw_reaction_id":null,"source":null},{"id":2314,"direction":"\u003e","locations":"Mitochondrion matrix;Cytoplasm;Mitochondrion","altext":"An alcohol + NAD(+) = an aldehyde or ketone + 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metabolic process"}],"pfams":[{"name":"ADH_N","identifier":"PF08240"},{"name":"ADH_zinc_N","identifier":"PF00107"}],"pathways":[{"name":"Glycolysis / Gluconeogenesis","kegg_map_id":"00010"},{"name":"Fatty acid metabolism","kegg_map_id":"00071"},{"name":"Glycine, serine and threonine metabolism","kegg_map_id":"00260"},{"name":"Tyrosine 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Acts on a variety of primary unbranched aliphatic alcohols","reactions":[{"id":1291,"direction":"\u003c\u003e","locations":"cytoplasm","altext":null,"export":true,"pw_reaction_id":null,"source":null},{"id":1294,"direction":"\u003e","locations":"mitochondrion;cytoplasm","altext":null,"export":true,"pw_reaction_id":null,"source":null},{"id":1296,"direction":"\u003e","locations":"mitochondrion;cytoplasm","altext":null,"export":true,"pw_reaction_id":null,"source":null},{"id":1303,"direction":"\u003e","locations":"mitochondrion;cytoplasm","altext":null,"export":true,"pw_reaction_id":null,"source":null},{"id":1305,"direction":"\u003e","locations":"mitochondrion;cytoplasm","altext":null,"export":true,"pw_reaction_id":null,"source":null},{"id":1308,"direction":"\u003e","locations":"mitochondrion;cytoplasm","altext":null,"export":true,"pw_reaction_id":null,"source":null},{"id":2314,"direction":"\u003e","locations":"Mitochondrion matrix;Cytoplasm;Mitochondrion","altext":"An alcohol + NAD(+) = an aldehyde or ketone + NADH.","export":false,"pw_reaction_id":null,"source":null}],"signal_regions":"None","transmembrane_regions":"None","pdb_id":null,"cellular_location":"Cytoplasm","genbank_gene_id":"J01314","genbank_protein_id":"171021","gene_card_id":"ADH2","chromosome_location":"chromosome 13","locus":"YMR303C","synonyms":["Alcohol dehydrogenase II","YADH-2"],"enzyme_classes":["1.1.1.1"],"go_classes":[{"category":"Component","description":" Not Available"},{"category":"Function","description":" metal ion binding"},{"category":"Function","description":" transition metal ion binding"},{"category":"Function","description":" oxidoreductase activity"},{"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":"Process","description":" oxidation reduction"},{"category":"Process","description":" metabolic process"}],"pfams":[{"name":"ADH_N","identifier":"PF08240"},{"name":"ADH_zinc_N","identifier":"PF00107"}],"pathways":[{"name":"Glycolysis / Gluconeogenesis","kegg_map_id":"00010"},{"name":"Fatty acid metabolism","kegg_map_id":"00071"},{"name":"Glycine, serine and threonine metabolism","kegg_map_id":"00260"},{"name":"Tyrosine metabolism","kegg_map_id":"00350"}],"gene_sequence":"ATGTCTATTCCAGAAACTCAAAAAGCCATTATCTTCTACGAATCCAACGGCAAGTTGGAGCATAAGGATATCCCAGTTCCAAAGCCAAAGCCCAACGAATTGTTAATCAACGTCAAGTACTCTGGTGTCTGCCACACCGATTTGCACGCTTGGCATGGTGACTGGCCATTGCCAACTAAGTTACCATTAGTTGGTGGTCACGAAGGTGCCGGTGTCGTTGTCGGCATGGGTGAAAACGTTAAGGGCTGGAAGATCGGTGACTACGCCGGTATCAAATGGTTGAACGGTTCTTGTATGGCCTGTGAATACTGTGAATTGGGTAACGAATCCAACTGTCCTCACGCTGACTTGTCAGGTTACACCCACGACGGTTCTTTCCAAGAATACGCTACCGCTGACGCTGTTCAAGCCGCTCACATTCCTCAAGGTACTGACTTGGCTGAAGTCGCGCCAATCTTGTGTGCTGGTATCACCGTATACAAGGCTTTGAAGTCTGCCAACTTGAGAGCAGGCCACTGGGCGGCCATTTCTGGTGCTGCTGGTGGTCTAGGTTCTTTGGCTGTTCAATATGCTAAGGCGATGGGTTACAGAGTCTTAGGTATTGATGGTGGTCCAGGAAAGGAAGAATTGTTTACCTCGCTCGGTGGTGAAGTATTCATCGACTTCACCAAAGAGAAGGACATTGTTAGCGCAGTCGTTAAGGCTACCAACGGCGGTGCCCACGGTATCATCAATGTTTCCGTTTCCGAAGCCGCTATCGAAGCTTCTACCAGATACTGTAGGGCGAACGGTACTGTTGTCTTGGTTGGTTTGCCAGCCGGTGCAAAGTGCTCCTCTGATGTCTTCAACCACGTTGTCAAGTCTATCTCCATTGTCGGCTCTTACGTGGGGAACAGAGCTGATACCAGAGAAGCCTTAGATTTCTTTGCCAGAGGTCTAGTCAAGTCTCCAATAAAGGTAGTTGGCTTATCCAGTTTACCAGAAATTTACGAAAAGATGGAGAAGGGCCAAATTGCTGGTAGATACGTTGTTGACACTTCTAAATAA","protein_sequence":"MSIPETQKAIIFYESNGKLEHKDIPVPKPKPNELLINVKYSGVCHTDLHAWHGDWPLPTKLPLVGGHEGAGVVVGMGENVKGWKIGDYAGIKWLNGSCMACEYCELGNESNCPHADLSGYTHDGSFQEYATADAVQAAHIPQGTDLAEVAPILCAGITVYKALKSANLRAGHWAAISGAAGGLGSLAVQYAKAMGYRVLGIDGGPGKEELFTSLGGEVFIDFTKEKDIVSAVVKATNGGAHGIINVSVSEAAIEASTRYCRANGTVVLVGLPAGAKCSSDVFNHVVKSISIVGSYVGNRADTREALDFFARGLVKSPIKVVGLSSLPEIYEKMEKGQIAGRYVVDTSK"},{"created_at":"2011-05-26T23:22:53.000Z","updated_at":"2011-05-29T14:08:01.000Z","name":"NADPH-dependent methylglyoxal reductase GRE2","uniprot_id":"Q12068","uniprot_name":"GRE2_YEAST","enzyme":true,"transporter":false,"gene_name":"GRE2","num_residues":342,"molecular_weight":"38169.19922","theoretical_pi":"6.06","general_function":"Involved in catalytic activity","specific_function":"Catalyzes the irreversible reduction of the cytotoxic compound methylglyoxal (MG) to (R)-lactaldehyde as an alternative to detoxification of MG by glyoxalase I GLO1. 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NADPH.","export":false,"pw_reaction_id":null,"source":null},{"id":3900,"direction":"\u003c\u003e","locations":null,"altext":null,"export":true,"pw_reaction_id":"PW_R006417","source":"Smpdb"},{"id":3901,"direction":"\u003e","locations":null,"altext":null,"export":true,"pw_reaction_id":"PW_R006521","source":"Smpdb"},{"id":3902,"direction":"\u003e","locations":null,"altext":null,"export":true,"pw_reaction_id":"PW_R006526","source":"Smpdb"},{"id":3903,"direction":"\u003e","locations":null,"altext":null,"export":true,"pw_reaction_id":"PW_R006538","source":"Smpdb"},{"id":3904,"direction":"\u003c\u003e","locations":null,"altext":null,"export":true,"pw_reaction_id":"PW_R006558","source":"Smpdb"},{"id":3905,"direction":"\u003e","locations":null,"altext":null,"export":true,"pw_reaction_id":"PW_R006972","source":"Smpdb"},{"id":3906,"direction":"\u003c\u003e","locations":null,"altext":null,"export":true,"pw_reaction_id":"PW_R006976","source":"Smpdb"},{"id":3907,"direction":"\u003e","locations":null,"altext":null,"export":true,"pw_reaction_id":"PW_R006980","source":"Smpdb"}],"signal_regions":"None","transmembrane_regions":"None","pdb_id":null,"cellular_location":null,"genbank_gene_id":"X59720","genbank_protein_id":"1907243","gene_card_id":"ADH7","chromosome_location":"chromosome 3","locus":"YCR105W","synonyms":["NADP-dependent alcohol dehydrogenase VII","ADHVII"],"enzyme_classes":["1.1.1.2"],"go_classes":[{"category":"Component","description":" Not Available"},{"category":"Function","description":" metal ion binding"},{"category":"Function","description":" transition metal ion binding"},{"category":"Function","description":" oxidoreductase activity"},{"category":"Function","description":" zinc ion binding"},{"category":"Function","description":" cofactor binding"},{"category":"Function","description":" oxidoreductase activity, acting on CH-OH group of donors"},{"category":"Function","description":" oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor"},{"category":"Function","description":" catalytic activity"},{"category":"Function","description":" binding"},{"category":"Function","description":" ion binding"},{"category":"Function","description":" cation binding"},{"category":"Process","description":" oxidation 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phosphorylinositol ceramide synthase regulatory protein CSG2","uniprot_id":"P35206","uniprot_name":"CSG2_YEAST","enzyme":true,"transporter":false,"gene_name":"CSG2","num_residues":410,"molecular_weight":"45441.60156","theoretical_pi":"7.33","general_function":"Involved in enzyme regulator activity","specific_function":"Required for calcium regulation. May regulate calcium accumulation by a non-vacuole organelle. Also regulates the activity of CSH1 and SUR1 during mannosyl phosphorylinositol ceramide synthesis","reactions":[{"id":1295,"direction":"\u003e","locations":"cytoplasm","altext":null,"export":true,"pw_reaction_id":null,"source":null},{"id":1297,"direction":"\u003e","locations":"cytoplasm","altext":null,"export":true,"pw_reaction_id":null,"source":null},{"id":1304,"direction":"\u003e","locations":"cytoplasm","altext":null,"export":true,"pw_reaction_id":null,"source":null},{"id":1306,"direction":"\u003e","locations":"cytoplasm","altext":null,"export":true,"pw_reaction_id":null,"source":null}],"signal_regions":"1-17","transmembrane_regions":"51-71;142-161;168-187;198-217;246-265;286-305;325-344;356-374;386-404","pdb_id":null,"cellular_location":"Endoplasmic reticulum membrane; Multi-pass membrane protein","genbank_gene_id":"D28120","genbank_protein_id":"976270","gene_card_id":"CSG2","chromosome_location":"chromosome 2","locus":"YBR036C","synonyms":[],"enzyme_classes":[],"go_classes":[],"pfams":[],"pathways":[],"gene_sequence":"ATGTCTACCACACTACTTTGGTTTTCAAGTGTAATAGGCTACGTGATTCAAACAAAATGTTTGTCTAACATACAATCTAAAAAGGAAATCTCCGTGGGGCCCAATGGTACAATTGCAACGCCTGAAACTAACGGCGACAACGGAAACTCAAGTTCATTAACCTTCTATCTGACCTTTATGTATTTTGCTTCGTGGCTGCTCTTGGTGCCTGCATCTCGACTTTGGGAGAAGATGAGACCGATGTTTGTCTCTGACTCAGACTCGAACAGGAATTCTCAGTTTGACAACAACAACAGCGGGTCTGTGACAAACGAAGATGTCGATACGTTCTCGCACGTGTTGGATGATCCTCAACCACGGATTCCAGCCCAACAGCAGAAGCAAAAAATCATATCCGTGGCTACCTTCAAATATGTGGCTAAGCTAACAGTGCTGGCTCTCATAATGATTGTCGCTGATTTGACTTATAACATGGCTTTGTCATTGTCACCGGCATTTGATGTTGCTTTGATGCAAAATACTGCCATTTTCGAAATTGTCACTTTACTATATGGTGTTTGTGGAATCTCCAGGAAGAACTACGTTTTCCGTAATTTCCTCATCATGATGAACGCGGTCATTGGAATTTTGATCATCTCATACACGAAGGCTACCTGTGACATGCTTGCCGGAAAGCTGTCCGTCAACCCTAACACGGGTGAACTTTCTGACCCATTCTTGTTTGATAGGTTGAAAGGTGCTCTGATTTGCGGCCTTGGTGCTTTGATTATGGGTCCTTTTGCCGTGTTATGGAACCGTTGGTTTTGCAGTAACATTTCCAAGAACGAAAATTCTGCTGTAGTCTTGGTTAAGCAGAGCACCCACATGGCCCTAATCGGTATTATTGGCATGGTAATACTTTTGCCATTTATTCCTAAATTTCCCTCCCGTGAGTCTGTGGAATCCATTTCGTTGTTCTATAATGACAAGAGCTTTTGGTTCTCTCTACTAGGCTCGATTATCTTTGGTTCCTTGCCGAGCTTGATTTCGATATTAGAGTTGAATCGCAAGGCCCCTGCTGAGTATTTGACGACGTGCAACCTGGGAGCTATTATCTTTATGGGGTTAGCTGAGTGGGTTTGCGAACCTACGCAAACCACAATTGTGAGATGGGAAGTCATAGGATACATAATGCTAACGGTAAGTTTGTTGGTCCTATCAGTAACACTCGGGGAAGGTAAATACCACCATTAG","protein_sequence":"MSTTLLWFSSVIGYVIQTKCLSNIQSKKEISVGPNGTIATPETNGDNGNSSSLTFYLTFMYFASWLLLVPASRLWEKMRPMFVSDSDSNRNSQFDNNNSGSVTNEDVDTFSHVLDDPQPRIPAQQQKQKIISVATFKYVAKLTVLALIMIVADLTYNMALSLSPAFDVALMQNTAIFEIVTLLYGVCGISRKNYVFRNFLIMMNAVIGILIISYTKATCDMLAGKLSVNPNTGELSDPFLFDRLKGALICGLGALIMGPFAVLWNRWFCSNISKNENSAVVLVKQSTHMALIGIIGMVILLPFIPKFPSRESVESISLFYNDKSFWFSLLGSIIFGSLPSLISILELNRKAPAEYLTTCNLGAIIFMGLAEWVCEPTQTTIVRWEVIGYIMLTVSLLVLSVTLGEGKYHH"},{"created_at":"2011-05-27T02:09:02.000Z","updated_at":"2011-07-22T17:53:49.000Z","name":"Transaminated amino acid decarboxylase","uniprot_id":"Q06408","uniprot_name":"ARO10_YEAST","enzyme":true,"transporter":false,"gene_name":"ARO10","num_residues":635,"molecular_weight":"71383.79688","theoretical_pi":"6.51","general_function":"Involved in magnesium ion binding","specific_function":"One of five 2-oxo acid decarboxylases (PDC1, PDC5, PDC6, ARO10, and THI3) involved in amino acid catabolism. The enzyme catalyzes the decarboxylation of amino acids, which, in a first step, have been transaminated to the corresponding 2-oxo acids (alpha-keto-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, phenylalanine, tryptophan, (and probably tyrosine), but also isoleucine, whereas leucine is a low efficiency and valine and pyruvate are no substrates. In analogy to the pyruvate decarboxylases the enzyme may in a side-reaction catalyze condensation (or carboligation) reactions leading to the formation of 2-hydroxy ketone, collectively called acyloins","reactions":[{"id":1186,"direction":"\u003e","locations":"cytoplasm","altext":null,"export":true,"pw_reaction_id":null,"source":null},{"id":1197,"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":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":2321,"direction":"\u003e","locations":"Cytoplasm. Nucleus;Cytoplasm","altext":"Phenylpyruvate = phenylacetaldehyde + 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":14461,"direction":"\u003e","locations":null,"altext":null,"export":true,"pw_reaction_id":"PW_R006975","source":"Smpdb"}],"signal_regions":"None","transmembrane_regions":"None","pdb_id":null,"cellular_location":"Cytoplasm","genbank_gene_id":"U28373","genbank_protein_id":"849201","gene_card_id":"ARO10","chromosome_location":"chromosome 4","locus":"YDR380W","synonyms":["Transaminated branched-chain amino acid decarboxylase"],"enzyme_classes":["4.1.1.-","4.1.1.43"],"go_classes":[{"category":"Component","description":" Not Available"},{"category":"Function","description":" binding"},{"category":"Function","description":" ion binding"},{"category":"Function","description":" cation binding"},{"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":" lyase activity"},{"category":"Function","description":" carbon-carbon lyase activity"},{"category":"Function","description":" carboxy-lyase activity"},{"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":"Leucine Degradation","kegg_map_id":null}],"gene_sequence":"ATGGCACCTGTTACAATTGAAAAGTTCGTAAATCAAGAAGAACGACACCTTGTTTCCAACCGATCAGCAACAATTCCGTTTGGTGAATACATATTTAAAAGATTGTTGTCCATCGATACGAAATCAGTTTTCGGTGTTCCTGGTGACTTCAACTTATCTCTATTAGAATATCTCTATTCACCTAGTGTTGAATCAGCTGGCCTAAGATGGGTCGGCACGTGTAATGAACTGAACGCCGCTTATGCGGCCGACGGATATTCCCGTTACTCTAATAAGATTGGCTGTTTAATAACCACGTATGGCGTTGGTGAATTAAGCGCCTTGAACGGTATAGCCGGTTCGTTCGCTGAAAATGTCAAAGTTTTGCACATTGTTGGTGTGGCCAAGTCCATAGATTCGCGTTCAAGTAACTTTAGTGATCGGAACCTACATCATTTGGTCCCACAGCTACATGATTCAAATTTTAAAGGGCCAAATCATAAAGTATATCATGATATGGTAAAAGATAGAGTCGCTTGCTCGGTAGCCTACTTGGAGGATATTGAAACTGCATGTGACCAAGTCGATAATGTTATCCGCGATATTTACAAGTATTCTAAACCTGGTTATATTTTTGTTCCTGCAGATTTTGCGGATATGTCTGTTACATGTGATAATTTGGTTAATGTTCCACGTATATCTCAACAAGATTGTATAGTATACCCTTCTGAAAACCAATTGTCTGACATAATCAACAAGATTACTAGTTGGATATATTCCAGTAAAACACCTGCGATCCTTGGAGACGTACTGACTGATAGGTATGGTGTGAGTAACTTTTTGAACAAGCTTATCTGCAAAACTGGGATTTGGAATTTTTCCACTGTTATGGGAAAATCTGTAATTGATGAGTCAAACCCAACTTATATGGGTCAATATAATGGTAAAGAAGGTTTAAAACAAGTCTATGAACATTTTGAACTGTGCGACTTGGTCTTGCATTTTGGAGTCGACATCAATGAAATTAATAATGGGCATTATACTTTTACTTATAAACCAAATGCTAAAATCATTCAATTTCATCCGAATTATATTCGCCTTGTGGACACTAGGCAGGGCAATGAGCAAATGTTCAAAGGAATCAATTTTGCCCCTATTTTAAAAGAACTATACAAGCGCATTGACGTTTCTAAACTTTCTTTGCAATATGATTCAAATGTAACTCAATATACGAACGAAACAATGCGGTTAGAAGATCCTACCAATGGACAATCAAGCATTATTACACAAGTTCACTTACAAAAGACGATGCCTAAATTTTTGAACCCTGGTGATGTTGTCGTTTGTGAAACAGGCTCTTTTCAATTCTCTGTTCGTGATTTCGCGTTTCCTTCGCAATTAAAATATATATCGCAAGGATTTTTCCTTTCCATTGGCATGGCCCTTCCTGCCGCCCTAGGTGTTGGAATTGCCATGCAAGACCACTCAAACGCTCACATCAATGGTGGCAACGTAAAAGAGGACTATAAGCCAAGATTAATTTTGTTTGAAGGTGACGGTGCAGCACAGATGACAATCCAAGAACTGAGCACCATTCTGAAGTGCAATATTCCACTAGAAGTTATCATTTGGAACAATAACGGCTACACTATTGAAAGAGCCATCATGGGCCCTACCAGGTCGTATAACGACGTTATGTCTTGGAAATGGACCAAACTATTTGAAGCATTCGGAGACTTCGACGGAAAGTATACTAATAGCACTCTCATTCAATGTCCCTCTAAATTAGCACTGAAATTGGAGGAGCTTAAGAATTCAAACAAAAGAAGCGGGATAGAACTTTTAGAAGTCAAATTAGGCGAATTGGATTTCCCCGAACAGCTAAAGTGCATGGTTGAAGCAGCGGCACTTAAAAGAAATAAAAAATAG","protein_sequence":"MAPVTIEKFVNQEERHLVSNRSATIPFGEYIFKRLLSIDTKSVFGVPGDFNLSLLEYLYSPSVESAGLRWVGTCNELNAAYAADGYSRYSNKIGCLITTYGVGELSALNGIAGSFAENVKVLHIVGVAKSIDSRSSNFSDRNLHHLVPQLHDSNFKGPNHKVYHDMVKDRVACSVAYLEDIETACDQVDNVIRDIYKYSKPGYIFVPADFADMSVTCDNLVNVPRISQQDCIVYPSENQLSDIINKITSWIYSSKTPAILGDVLTDRYGVSNFLNKLICKTGIWNFSTVMGKSVIDESNPTYMGQYNGKEGLKQVYEHFELCDLVLHFGVDINEINNGHYTFTYKPNAKIIQFHPNYIRLVDTRQGNEQMFKGINFAPILKELYKRIDVSKLSLQYDSNVTQYTNETMRLEDPTNGQSSIITQVHLQKTMPKFLNPGDVVVCETGSFQFSVRDFAFPSQLKYISQGFFLSIGMALPAALGVGIAMQDHSNAHINGGNVKEDYKPRLILFEGDGAAQMTIQELSTILKCNIPLEVIIWNNNGYTIERAIMGPTRSYNDVMSWKWTKLFEAFGDFDGKYTNSTLIQCPSKLALKLEELKNSNKRSGIELLEVKLGELDFPEQLKCMVEAAALKRNKK"},{"created_at":"2011-05-27T02:09:59.000Z","updated_at":"2011-07-22T17:54:08.000Z","name":"NADP-dependent alcohol dehydrogenase 6","uniprot_id":"Q04894","uniprot_name":"ADH6_YEAST","enzyme":true,"transporter":false,"gene_name":"ADH6","num_residues":360,"molecular_weight":"39617.30078","theoretical_pi":"6.73","general_function":"Involved in zinc ion binding","specific_function":"NADP-dependent alcohol dehydrogenase with a broad substrate specificity","reactions":[{"id":1295,"direction":"\u003e","locations":"cytoplasm","altext":null,"export":true,"pw_reaction_id":null,"source":null},{"id":1297,"direction":"\u003e","locations":"cytoplasm","altext":null,"export":true,"pw_reaction_id":null,"source":null},{"id":1304,"direction":"\u003e","locations":"cytoplasm","altext":null,"export":true,"pw_reaction_id":null,"source":null},{"id":1306,"direction":"\u003e","locations":"cytoplasm","altext":null,"export":true,"pw_reaction_id":null,"source":null},{"id":2660,"direction":"\u003e","locations":"","altext":"An alcohol + NADP(+) = an aldehyde + NADPH.","export":false,"pw_reaction_id":null,"source":null},{"id":3860,"direction":"\u003e","locations":null,"altext":null,"export":true,"pw_reaction_id":"PW_R006381","source":"Smpdb"},{"id":3900,"direction":"\u003c\u003e","locations":null,"altext":null,"export":true,"pw_reaction_id":"PW_R006417","source":"Smpdb"},{"id":3901,"direction":"\u003e","locations":null,"altext":null,"export":true,"pw_reaction_id":"PW_R006521","source":"Smpdb"},{"id":3902,"direction":"\u003e","locations":null,"altext":null,"export":true,"pw_reaction_id":"PW_R006526","source":"Smpdb"},{"id":3903,"direction":"\u003e","locations":null,"altext":null,"export":true,"pw_reaction_id":"PW_R006538","source":"Smpdb"},{"id":3904,"direction":"\u003c\u003e","locations":null,"altext":null,"export":true,"pw_reaction_id":"PW_R006558","source":"Smpdb"},{"id":3905,"direction":"\u003e","locations":null,"altext":null,"export":true,"pw_reaction_id":"PW_R006972","source":"Smpdb"},{"id":3906,"direction":"\u003c\u003e","locations":null,"altext":null,"export":true,"pw_reaction_id":"PW_R006976","source":"Smpdb"},{"id":3907,"direction":"\u003e","locations":null,"altext":null,"export":true,"pw_reaction_id":"PW_R006980","source":"Smpdb"}],"signal_regions":"None","transmembrane_regions":"None","pdb_id":"1Q1N","cellular_location":null,"genbank_gene_id":"Z54141","genbank_protein_id":"984691","gene_card_id":"ADH6","chromosome_location":"chromosome 13","locus":"YMR318C","synonyms":["NADP-dependent alcohol dehydrogenase VI","ScADHVI"],"enzyme_classes":["1.1.1.2"],"go_classes":[{"category":"Component","description":" Not Available"},{"category":"Function","description":" metal ion binding"},{"category":"Function","description":" transition metal ion binding"},{"category":"Function","description":" oxidoreductase activity"},{"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":"Process","description":" oxidation reduction"},{"category":"Process","description":" metabolic process"}],"pfams":[{"name":"ADH_N","identifier":"PF08240"},{"name":"ADH_zinc_N","identifier":"PF00107"}],"pathways":[{"name":"Glycolysis / Gluconeogenesis","kegg_map_id":"00010"},{"name":"Glycerolipid metabolism","kegg_map_id":"00561"},{"name":"Ethanol fermentation","kegg_map_id":null},{"name":"Glycerol metabolism","kegg_map_id":null},{"name":"Isoleucine degradation","kegg_map_id":null},{"name":"Leucine 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":"ATGTCTTATCCTGAGAAATTTGAAGGTATCGCTATTCAATCACACGAAGATTGGAAAAACCCAAAGAAGACAAAGTATGACCCAAAACCATTTTACGATCATGACATTGACATTAAGATCGAAGCATGTGGTGTCTGCGGTAGTGATATTCATTGTGCAGCTGGTCATTGGGGCAATATGAAGATGCCGCTAGTCGTTGGTCATGAAATCGTTGGTAAAGTTGTCAAGCTAGGGCCCAAGTCAAACAGTGGGTTGAAAGTCGGTCAACGTGTTGGTGTAGGTGCTCAAGTCTTTTCATGCTTGGAATGTGACCGTTGTAAGAATGATAATGAACCATACTGCACCAAGTTTGTTACCACATACAGTCAGCCTTATGAAGACGGCTATGTGTCGCAGGGTGGCTATGCAAACTACGTCAGAGTTCATGAACATTTTGTGGTGCCTATCCCAGAGAATATTCCATCACATTTGGCTGCTCCACTATTATGTGGTGGTTTGACTGTGTACTCTCCATTGGTTCGTAACGGTTGCGGTCCAGGTAAAAAAGTTGGTATAGTTGGTCTTGGTGGTATCGGCAGTATGGGTACATTGATTTCCAAAGCCATGGGGGCAGAGACGTATGTTATTTCTCGTTCTTCGAGAAAAAGAGAAGATGCAATGAAGATGGGCGCCGATCACTACATTGCTACATTAGAAGAAGGTGATTGGGGTGAAAAGTACTTTGACACCTTCGACCTGATTGTAGTCTGTGCTTCCTCCCTTACCGACATTGACTTCAACATTATGCCAAAGGCTATGAAGGTTGGTGGTAGAATTGTCTCAATCTCTATACCAGAACAACACGAAATGTTATCGCTAAAGCCATATGGCTTAAAGGCTGTCTCCATTTCTTACAGTGCTTTAGGTTCCATCAAAGAATTGAACCAACTCTTGAAATTAGTCTCTGAAAAAGATATCAAAATTTGGGTGGAAACATTACCTGTTGGTGAAGCCGGCGTCCATGAAGCCTTCGAAAGGATGGAAAAGGGTGACGTTAGATATAGATTTACCTTAGTCGGCTACGACAAAGAATTTTCAGACTAG","protein_sequence":"MSYPEKFEGIAIQSHEDWKNPKKTKYDPKPFYDHDIDIKIEACGVCGSDIHCAAGHWGNMKMPLVVGHEIVGKVVKLGPKSNSGLKVGQRVGVGAQVFSCLECDRCKNDNEPYCTKFVTTYSQPYEDGYVSQGGYANYVRVHEHFVVPIPENIPSHLAAPLLCGGLTVYSPLVRNGCGPGKKVGIVGLGGIGSMGTLISKAMGAETYVISRSSRKREDAMKMGADHYIATLEEGDWGEKYFDTFDLIVVCASSLTDIDFNIMPKAMKVGGRIVSISIPEQHEMLSLKPYGLKAVSISYSALGSIKELNQLLKLVSEKDIKIWVETLPVGEAGVHEAFERMEKGDVRYRFTLVGYDKEFSD"},{"created_at":"2011-05-27T08:04:35.000Z","updated_at":"2011-07-22T17:53:49.000Z","name":"Thiamine metabolism regulatory protein THI3","uniprot_id":"Q07471","uniprot_name":"THI3_YEAST","enzyme":true,"transporter":false,"gene_name":"THI3","num_residues":609,"molecular_weight":"68365.79688","theoretical_pi":"6.33","general_function":"Involved in magnesium ion binding","specific_function":"One of five 2-oxo acid decarboxylases (PDC1, PDC5, PDC6, ARO10, and THI3) involved in amino acid catabolism. The enzyme catalyzes the decarboxylation of amino acids, which, in a first step, have been transaminated to the corresponding 2-oxo acids (alpha-keto-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 leucine and isoleucine, whereas valine, aromatic amino acids, and pyruvate are no substrates. In analogy to the pyruvate decarboxylases the enzyme may in a side-reaction catalyze condensation (or carboligation) reactions leading to the formation of 2-hydroxy ketone, collectively called acyloins. The enzyme is also positively regulating the thiamine metabolism by a molecular mechanism that may involve thiamine concentration sensing and signal transmission","reactions":[{"id":1186,"direction":"\u003e","locations":"cytoplasm","altext":null,"export":true,"pw_reaction_id":null,"source":null},{"id":1197,"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":14461,"direction":"\u003e","locations":null,"altext":null,"export":true,"pw_reaction_id":"PW_R006975","source":"Smpdb"}],"signal_regions":"None","transmembrane_regions":"None","pdb_id":null,"cellular_location":"Nucleus","genbank_gene_id":"Z74128","genbank_protein_id":"1431100","gene_card_id":"THI3","chromosome_location":"chromosome 4","locus":"YDL080C","synonyms":["Keto isocaproate decarboxylase KID1"],"enzyme_classes":["4.1.1.-"],"go_classes":[{"category":"Component","description":" Not Available"},{"category":"Function","description":" binding"},{"category":"Function","description":" ion binding"},{"category":"Function","description":" cation binding"},{"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":" lyase activity"},{"category":"Function","description":" carbon-carbon lyase activity"},{"category":"Function","description":" carboxy-lyase activity"},{"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":"Leucine Degradation","kegg_map_id":null}],"gene_sequence":"ATGAATTCTAGCTATACACAGAGATATGCACTGCCGAAGTGTATAGCAATATCAGATTATCTTTTCCATCGGCTCAACCAGCTGAACATACATACCATATTTGGACTCTCCGGAGAATTTAGCATGCCGTTGCTGGATAAACTATACAACATTCCGAACTTACGATGGGCCGGTAATTCTAATGAGTTAAATGCTGCCTACGCAGCAGATGGATACTCACGACTAAAAGGCTTGGGATGTCTCATAACAACCTTTGGTGTAGGCGAATTATCGGCAATCAATGGCGTGGCCGGATCTTACGCTGAACATGTAGGAATACTTCACATAGTGGGTATGCCGCCAACAAGTGCACAAACGAAACAACTACTACTGCATCATACTCTGGGCAATGGTGATTTCACGGTATTTCATAGAATAGCCAGTGATGTAGCATGCTATACAACATTGATTATTGACTCTGAATTATGTGCCGACGAAGTCGATAAGTGCATCAAAAAGGCTTGGATAGAACAGAGGCCAGTATACATGGGCATGCCTGTCAACCAGGTAAATCTCCCGATTGAATCAGCAAGGCTTAATACACCTCTGGATTTACAATTGCATAAAAACGACCCAGACGTAGAGAAAGAAGTTATTTCTCGAATATTGAGTTTTATATACAAAAGCCAGAATCCGGCAATCATCGTAGATGCATGTACTAGTCGACAGAATTTAATCGAGGAGACTAAAGAGCTTTGTAATAGGCTTAAATTTCCAGTTTTTGTTACACCTATGGGTAAGGGTACAGTAAACGAAACAGACCCGCAATTTGGGGGCGTATTCACGGGCTCGATATCAGCCCCAGAAGTAAGAGAAGTAGTTGATTTTGCCGATTTTATCATCGTCATTGGTTGCATGCTCTCCGAATTCAGCACGTCAACTTTCCACTTCCAATATAAAACTAAGAATTGTGCGCTACTATATTCTACATCTGTGAAATTGAAAAATGCCACATATCCTGACTTGAGCATTAAATTACTACTACAGAAAATATTAGCAAATCTTGATGAATCTAAACTGTCTTACCAACCAAGCGAACAACCCAGTATGATGGTTCCAAGACCTTACCCAGCAGGAAATGTCCTCTTGAGACAAGAATGGGTCTGGAATGAAATATCCCATTGGTTCCAACCAGGTGACATAATCATAACAGAAACTGGTGCTTCTGCATTTGGAGTTAACCAGACCAGATTTCCGGTAAATACACTAGGTATTTCGCAAGCTCTTTGGGGATCTGTCGGATATACAATGGGGGCGTGTCTTGGGGCAGAATTTGCTGTTCAAGAGATAAACAAGGATAAATTCCCCGCAACTAAACATAGAGTTATTCTGTTTATGGGTGACGGTGCTTTCCAATTGACAGTTCAAGAATTATCCACAATTGTTAAGTGGGGATTGACACCTTATATTTTTGTGATGAATAACCAAGGTTACTCTGTGGACAGGTTTTTGCATCACAGGTCAGATGCTAGTTATTACGATATCCAACCTTGGAACTACTTGGGATTATTGCGAGTATTTGGTTGCACGAACTACGAAACGAAAAAAATTATTACTGTTGGAGAATTCAGATCCATGATCAGTGACCCAAACTTTGCGACCAATGACAAAATTCGGATGATAGAGATTATGCTACCACCAAGGGATGTTCCACAGGCTCTGCTTGACAGGTGGGTGGTAGAAAAAGAACAGAGCAAACAAGTGCAAGAGGAGAACGAAAATTCTAGCGCAGTAAATACGCCAACTCCAGAATTCCAACCACTTCTAAAAAAAAATCAAGTTGGATACTGA","protein_sequence":"MNSSYTQRYALPKCIAISDYLFHRLNQLNIHTIFGLSGEFSMPLLDKLYNIPNLRWAGNSNELNAAYAADGYSRLKGLGCLITTFGVGELSAINGVAGSYAEHVGILHIVGMPPTSAQTKQLLLHHTLGNGDFTVFHRIASDVACYTTLIIDSELCADEVDKCIKKAWIEQRPVYMGMPVNQVNLPIESARLNTPLDLQLHKNDPDVEKEVISRILSFIYKSQNPAIIVDACTSRQNLIEETKELCNRLKFPVFVTPMGKGTVNETDPQFGGVFTGSISAPEVREVVDFADFIIVIGCMLSEFSTSTFHFQYKTKNCALLYSTSVKLKNATYPDLSIKLLLQKILANLDESKLSYQPSEQPSMMVPRPYPAGNVLLRQEWVWNEISHWFQPGDIIITETGASAFGVNQTRFPVNTLGISQALWGSVGYTMGACLGAEFAVQEINKDKFPATKHRVILFMGDGAFQLTVQELSTIVKWGLTPYIFVMNNQGYSVDRFLHHRSDASYYDIQPWNYLGLLRVFGCTNYETKKIITVGEFRSMISDPNFATNDKIRMIEIMLPPRDVPQALLDRWVVEKEQSKQVQEENENSSAVNTPTPEFQPLLKKNQVGY"}]}