{"ymdb_id":"YMDB00106","created_at":"2011-05-29T15:57:15.000Z","updated_at":"2016-09-08T18:35:02.000Z","name":"2-Isopropylmalic acid","cas":"49601-06-1","state":"Solid","melting_point":"144-146 oC","description":"2-Isopropylmalic acid is an alpha-hydroxy organic acid and is an intermediate of luecine biosynthesis. Yeast cells naturally secret this compound into their surrounding. It is thought that 2-Isopropylmalic acid secretion chelates aluminum ions and prevents them from entering cells, resulting in aluminum tolerance. [PMID: 17916978]","experimental_water_solubility":null,"experimental_logp_hydrophobicity":null,"location":"Cytoplasm;Extracellular;Mitochondrion","synthesis_reference":"Schloss J V; Magolda R; Emptage M  Synthesis of alpha-isopropylmalate, beta-isopropylmalate, and dimethylcitraconate.    Methods in enzymology  (1988),  166 92-6. ","chebi_id":"35128","hmdb_id":"HMDB00402","kegg_id":"C02504","pubchem_id":"5280523","cs_id":"4444155","foodb_id":"FDB011983","wikipedia_link":null,"biocyc_id":null,"iupac":"(2S)-2-hydroxy-2-(propan-2-yl)butanedioic acid","traditional_iupac":"2-isopropyl-malic acid","logp":"0.20661967933333347","pka":"5.566000838313116","alogps_solubility":"1.81e+02 g/l","alogps_logp":"-0.29","alogps_logs":"0.01","acceptor_count":"5","donor_count":"3","rotatable_bond_count":"4","polar_surface_area":"94.83","refractivity":"38.5841","polarizability":"16.372264381734986","formal_charge":"0","physiological_charge":"-2","pka_strongest_basic":"-4.140578200901909","pka_strongest_acidic":"3.629835264652623","bioavailability":"1","number_of_rings":"0","rule_of_five":"1","ghose_filter":"0","veber_rule":"0","mddr_like_rule":"0","synonyms":["(2S)-2-hydroxy-2-(propan-2-yl)butanedioic acid","(2S)-2-Hydroxy-2-isopropylsuccinic acid","(2S)-2-Isopropylmalate","(3S)-3-carboxy-3-hydroxy-4-methylpentanoic acid","(3S)-3-carboxy-3-hydroxyisocaproic acid","2-Hydroxy-2-isopropylsuccinate","2-Hydroxy-2-isopropylsuccinic acid","2-Isopropyl-2-hydroxybutanedioate","2-Isopropyl-2-hydroxybutanedioic acid","2-isopropyl-Malic acid","2-Isopropylmalate","2-Isopropylmalic acid","3-Carboxy-3-hydroxy-4-methylpentanoate","3-Carboxy-3-hydroxyisocaproate","3-Carboxy-3-hydroxyisocaproic acid","3-hydroxy-4-methyl-3-carboxypentanoate","a-Isopropylmalate","a-Isopropylmalic acid","alpha-Isopropylmalate","alpha-Isopropylmalic acid"],"pathways":[{"name":"Pyruvate metabolism","kegg_map_id":"00620"},{"name":"Valine, leucine and isoleucine biosynthesis","kegg_map_id":"00290"},{"name":"Leucine Biosynthesis","kegg_map_id":null}],"growth_conditions":[],"references":[{"pubmed_id":21051339,"citation":"UniProt Consortium (2011). \"Ongoing and future developments at the Universal Protein Resource.\" Nucleic Acids Res 39:D214-D219."},{"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":15833351,"citation":"Kobayashi, A., Edo, H., Furihata, K., Yoshimura, E. (2005). \"Secretion of an aluminum chelator, 2-isopropylmalic acid, by the budding yeast, Saccharomyces cerevisiae.\" J Inorg Biochem 99:1260-1263."},{"pubmed_id":null,"citation":"Yannai S. Dictionary of food compounds with CD-ROM: additives, flavors, and ingredients. Chapman \u0026 Hall/CRC; 2004."},{"pubmed_id":6090272,"citation":"Chang, L. F., Cunningham, T. S., Gatzek, P. R., Chen, W. J., Kohlhaw, G. B. (1984). \"Cloning and characterization of yeast Leu4, one of two genes responsible for alpha-isopropylmalate synthesis.\" Genetics 108:91-106."},{"pubmed_id":17916978,"citation":"Suzuki, T., Tamura, S., Nakanishi, H., Tashiro, M., Nishizawa, N. K., Yoshimura, E. (2007). \"Reduction of aluminum toxicity by 2-isopropylmalic acid in the budding yeast Saccharomyces cerevisiae.\" Biol Trace Elem Res 120:257-263."},{"pubmed_id":17439666,"citation":"Castrillo, J. I., Zeef, L. A., Hoyle, D. C., Zhang, N., Hayes, A., Gardner, D. C., Cornell, M. J., Petty, J., Hakes, L., Wardleworth, L., Rash, B., Brown, M., Dunn, W. B., Broadhurst, D., O'Donoghue, K., Hester, S. S., Dunkley, T. P., Hart, S. R., Swainston, N., Li, P., Gaskell, S. J., Paton, N. W., Lilley, K. S., Kell, D. B., Oliver, S. G. (2007). \"Growth control of the eukaryote cell: a systems biology study in yeast.\" J Biol 6:4."}],"proteins":[{"created_at":"2011-05-24T21:21:31.000Z","updated_at":"2011-07-22T17:53:43.000Z","name":"2-isopropylmalate synthase 2, mitochondrial","uniprot_id":"Q12166","uniprot_name":"LEU9_YEAST","enzyme":true,"transporter":false,"gene_name":"LEU9","num_residues":604,"molecular_weight":"67199.60156","theoretical_pi":"6.75","general_function":"Involved in 2-isopropylmalate synthase activity","specific_function":"Catalyzes the condensation of the acetyl group of acetyl-CoA with 3-methyl-2-oxobutanoate (2-oxoisovalerate) to form 3-carboxy-3-hydroxy-4-methylpentanoate (2-isopropylmalate). Redundant to LEU4, responsible of about 20% of alpha-IPMS activity. Involved in leucine synthesis","reactions":[{"id":1148,"direction":"\u003e","locations":"mitochondrion;cytoplasm","altext":null,"export":true,"pw_reaction_id":null,"source":null},{"id":2382,"direction":"\u003e","locations":"Mitochondrion. Cytoplasm;Mitochondrion","altext":"Acetyl-CoA + 3-methyl-2-oxobutanoate + H(2)O = (2S)-2-isopropylmalate + CoA.","export":false,"pw_reaction_id":null,"source":null},{"id":14128,"direction":"\u003c\u003e","locations":null,"altext":null,"export":true,"pw_reaction_id":"PW_R006565","source":"Smpdb"}],"signal_regions":"None","transmembrane_regions":"None","pdb_id":null,"cellular_location":"Mitochondrion","genbank_gene_id":"X94335","genbank_protein_id":"1262141","gene_card_id":"LEU9","chromosome_location":"chromosome 15","locus":"YOR108W","synonyms":["Alpha-IPM synthase 2","Alpha-isopropylmalate synthase 2","Alpha-isopropylmalate synthase II"],"enzyme_classes":["2.3.3.13"],"go_classes":[{"category":"Component","description":" Not Available"},{"category":"Function","description":" transferase activity"},{"category":"Function","description":" transferase activity, transferring acyl groups"},{"category":"Function","description":" transferase activity, transferring acyl groups, acyl groups converted into alkyl on transfer"},{"category":"Function","description":" 2-isopropylmalate synthase activity"},{"category":"Function","description":" catalytic activity"},{"category":"Process","description":" metabolic process"},{"category":"Process","description":" cellular metabolic process"},{"category":"Process","description":" cellular amino acid and derivative metabolic process"},{"category":"Process","description":" cellular amino acid metabolic process"},{"category":"Process","description":" organic acid metabolic process"},{"category":"Process","description":" oxoacid metabolic process"},{"category":"Process","description":" carboxylic acid metabolic process"},{"category":"Process","description":" branched chain family amino acid metabolic process"},{"category":"Process","description":" leucine metabolic process"},{"category":"Process","description":" leucine biosynthetic process"}],"pfams":[{"name":"HMGL-like","identifier":"PF00682"},{"name":"LeuA_dimer","identifier":"PF08502"}],"pathways":[{"name":"Valine, leucine and isoleucine biosynthesis","kegg_map_id":"00290"},{"name":"Pyruvate metabolism","kegg_map_id":"00620"}],"gene_sequence":"ATGGTAAAACATTCGTTCATAGCGCTAGCTGAGCATGCTAGTAAACTAAGAAGGTCTATCCCACCCGTCAAACTGACTTATAAAAATATGCTACGGGACCCATCGGTAAAATATAGGGCGTTTGCTCCACCAAAAATGGTCAAGAGGATTTGGCCTGACAAAACTATTCAAAAGGCTCCACGTTGGCTGTCTACTGACTTGAGGGACGGTAATCAATCTTTACCGGACCCAATGTCTGTGGCTCAAAAGAAAGAATATTTCCACAAGTTGATCAACATCGGTTTCAAAGAAATCGAAGTGTCTTTCCCCTCTGCATCTCAAACAGATTTCGACTTCACCAGGTATGCTGTAGAAAACGCTCCAGATGATGTTGGTATTCAATGTCTTGTCCAATCTAGAGAACACTTGATTAAAAGAACCGTGGAAGCATTGACTGGTGCTAAAAGGGCTACCATACATACTTACTTGGCCACAAGTGACATGTTCCGAGAAATTGTCTTCAATATGTCTAGAGAGGAAGCTATTTCTAAAGCTGTAGAAGCCACCAAACTGGTTAGGAAACTAACCAAGGATGACCCTTCCCAGCAAGCTACTCGTTGGTCCTATGAGTTTTCTCCCGAATGTTTCAGTGATACGCCAGGTGAATTTGCTGTAGAAATTTGTGAAGCTGTTAAAAAGGCTTGGGAACCTACCGAGGAAAATCCGATCATTTTCAACTTACCAGCTACTGTAGAAGTTGCCTCTCCAAATGTTTACGCTGATCAAATTGAGTACTTCTCTACCCACATTACTGAGCGTGAGAAGGTCTGTATTTCTACGCATTGTCACAATGACCGTGGTTGCGGTGTCGCCGCCACAGAATTAGGTATGCTTGCAGGCGCTGATCGTGTAGAAGGTTGTCTATTTGGTAATGGTGAACGTACAGGTAATGTTGATTTGGTTACAGTTGCCATGAATATGTATACCCAAGGTGTTTCTCCTAATTTAGATTTCTCAGATTTAACTTCAATTTCTGAAATTGTCCATCGCTGTAACAAGATTCCAATTCCCCCAAGAGCCCCATATGGCGGTGAATTGGTTGTTTCTGCCTTTTCTGGTTCTCATCAGGATGCAATTAAGAAGGGATTTGCAATCCAAAACAAGAAACAGGCTCAAGGAGAAACTCGGTGGAGAATTCCATACTTACCATTGGATCCAAAGGATATTGGACGTGATTACGAAGCCGTCATCAGAGTCAACTCTCAATCCGGTAAGGGTGGTGCTGCTTGGGTTATTATGAGATCTCTAGGATTAGATGTACCAAGACCAATGCAAGTTGATTTCTCCAATACTCTACAGAAAAATGCAGATGCCTTAGGAAGAGAGTTAAAATCCGAAGAGATTACAAAATTGTTCAAAGAAACTTACAACTACAACAACAATGAACATATATACGTCACCTTGTTGAATTACGAAGTTAAGAAATTGAACCCAGAGCGTAGAGCTTTAGTGGGCCAGGTAGAAATCAACGATAAGGTTGTCAACATCGAAGGCTACGGAAATGGTCCTATCTCTTCTTTGGTGGATGCGCTATCCAATTTACTGAATGTTAAGTTGAGCGTTCAAAACTACTCTGAACATTCCTTGGGTTCTGGTTCTGCAACCCAAGCGGCATCTTTCATAAATCTTTCCTACATAAAGGACATCAATAATCATGCTACTAGTAATATGTGGGGTGTTGGTGTCTCCGAAGACACTGGGGATGCATCTATTAAGGCGGTATTTGCTACTGTCAATAATATTATTCATTCCGGGGATGTTCTACTGGCAGAGTAA","protein_sequence":"MVKHSFIALAEHASKLRRSIPPVKLTYKNMLRDPSVKYRAFAPPKMVKRIWPDKTIQKAPRWLSTDLRDGNQSLPDPMSVAQKKEYFHKLINIGFKEIEVSFPSASQTDFDFTRYAVENAPDDVGIQCLVQSREHLIKRTVEALTGAKRATIHTYLATSDMFREIVFNMSREEAISKAVEATKLVRKLTKDDPSQQATRWSYEFSPECFSDTPGEFAVEICEAVKKAWEPTEENPIIFNLPATVEVASPNVYADQIEYFSTHITEREKVCISTHCHNDRGCGVAATELGMLAGADRVEGCLFGNGERTGNVDLVTVAMNMYTQGVSPNLDFSDLTSISEIVHRCNKIPIPPRAPYGGELVVSAFSGSHQDAIKKGFAIQNKKQAQGETRWRIPYLPLDPKDIGRDYEAVIRVNSQSGKGGAAWVIMRSLGLDVPRPMQVDFSNTLQKNADALGRELKSEEITKLFKETYNYNNNEHIYVTLLNYEVKKLNPERRALVGQVEINDKVVNIEGYGNGPISSLVDALSNLLNVKLSVQNYSEHSLGSGSATQAASFINLSYIKDINNHATSNMWGVGVSEDTGDASIKAVFATVNNIIHSGDVLLAE"},{"created_at":"2011-05-24T21:47:11.000Z","updated_at":"2011-07-22T17:53:43.000Z","name":"2-isopropylmalate synthase","uniprot_id":"P06208","uniprot_name":"LEU1_YEAST","enzyme":true,"transporter":false,"gene_name":"LEU4","num_residues":619,"molecular_weight":"68408.29688","theoretical_pi":"5.85","general_function":"Involved in 2-isopropylmalate synthase activity","specific_function":"Catalyzes the condensation of the acetyl group of acetyl-CoA with 3-methyl-2-oxobutanoate (2-oxoisovalerate) to form 3-carboxy-3-hydroxy-4-methylpentanoate (2-isopropylmalate)","reactions":[{"id":1148,"direction":"\u003e","locations":"mitochondrion;cytoplasm","altext":null,"export":true,"pw_reaction_id":null,"source":null},{"id":2382,"direction":"\u003e","locations":"Mitochondrion. Cytoplasm;Mitochondrion","altext":"Acetyl-CoA + 3-methyl-2-oxobutanoate + H(2)O = (2S)-2-isopropylmalate + CoA.","export":false,"pw_reaction_id":null,"source":null},{"id":14128,"direction":"\u003c\u003e","locations":null,"altext":null,"export":true,"pw_reaction_id":"PW_R006565","source":"Smpdb"}],"signal_regions":"None","transmembrane_regions":"None","pdb_id":null,"cellular_location":"Mitochondrion. Cytoplasm","genbank_gene_id":"M12893","genbank_protein_id":"171841","gene_card_id":"LEU4","chromosome_location":"chromosome 14","locus":"YNL104C","synonyms":["Alpha-IPM synthase","Alpha-isopropylmalate synthase"],"enzyme_classes":["2.3.3.13"],"go_classes":[{"category":"Component","description":" Not Available"},{"category":"Function","description":" transferase activity"},{"category":"Function","description":" transferase activity, transferring acyl groups"},{"category":"Function","description":" transferase activity, transferring acyl groups, acyl groups converted into alkyl on transfer"},{"category":"Function","description":" 2-isopropylmalate synthase activity"},{"category":"Function","description":" catalytic activity"},{"category":"Process","description":" metabolic process"},{"category":"Process","description":" cellular metabolic process"},{"category":"Process","description":" cellular amino acid and derivative metabolic process"},{"category":"Process","description":" cellular amino acid metabolic process"},{"category":"Process","description":" organic acid metabolic process"},{"category":"Process","description":" oxoacid metabolic process"},{"category":"Process","description":" carboxylic acid metabolic process"},{"category":"Process","description":" branched chain family amino acid metabolic process"},{"category":"Process","description":" leucine metabolic process"},{"category":"Process","description":" leucine biosynthetic process"}],"pfams":[{"name":"HMGL-like","identifier":"PF00682"},{"name":"LeuA_dimer","identifier":"PF08502"}],"pathways":[{"name":"Valine, leucine and isoleucine biosynthesis","kegg_map_id":"00290"},{"name":"Pyruvate metabolism","kegg_map_id":"00620"}],"gene_sequence":"ATGGTTAAAGAGAGTATTATTGCTCTTGCTGAGCATGCGGCCTCCAGAGCCTCAAGAGTTATTCCTCCAGTGAAGCTAGCCTATAAAAATATGCTTAAGGACCCTTCCTCCAAGTACAAGCCATTTAACGCTCCAAAGCTATCTAATAGAAAGTGGCCGGATAACCGGATCACGAGGGCTCCTCGTTGGTTATCAACAGATTTGAGAGATGGTAACCAATCTCTGCCGGATCCCATGTCAGTGGAACAAAAGAAAGAATACTTTCACAAGCTGGTCAATATTGGGTTCAAAGAAATCGAGGTTTCCTTCCCCTCTGCATCTCAAACAGATTTCGACTTCACTAGATATGCTGTAGAAAACGCCCCAGACGATGTTAGTATTCAATGTCTTGTCCAATCTAGAGAACACTTGATTAAGAGAACGGTGGAAGCATTAACAGGTGCTAAAAAGGCTACTATACATACTTACTTGGCAACAAGTGATATGTTCCGTGAAATTGTTTTTAATATGTCTAGAGAGGAAGCTATTTCCAAGGCAGTAGAGGCCACCAAACTAGTTAGGAAACTAACTAAGGATGACCCTTCCCAACAAGCCACTCGTTGGTCCTATGAGTTTTCCCCCGAATGTTTCAGTGATACTCCAGGTGAATTTGCTGTAGAAATTTGCGAAGCTGTTAAGAAGGCTTGGGAACCTACCGAGGAAAATCCAATCATTTTCAACTTACCTGCTACCGTAGAAGTTGCCTCTCCAAATGTTTATGCTGATCAGATTGAATACTTCGCTACCCATATTACTGAGCGTGAGAAGGTTTGCATCTCTACACATTGTCACAATGACCGTGGTTGCGGTGTCGCCGCCACAGAGTTAGGTATGCTTGCAGGTGCCGACCGTGTAGAAGGATGTCTCTTTGGTAATGGTGAACGTACAGGTAATGTGGACTTGGTTACTGTTGCTATGAATATGTATACCCAAGGTGTTTCTCCTAATTTGGATTTCTCTGACTTGACCTCTGTCCTAGATGTGGTTGAGCGTTGTAATAAGATCCCAGTATCGCAAAGAGCACCATACGGCGGTGACTTGGTCGTTTGTGCCTTTTCCGGTTCTCACCAAGACGCCATTAAGAAGGGTTTCAACTTACAAAACAAGAAGCGTGCTCAAGGTGAAACTCAATGGAGAATCCCATACTTGCCATTGGATCCAAAGGACATTGGCCGTGATTACGAAGCTGTCATCAGAGTCAACTCTCAGTCTGGTAAAGGTGGTGCCGCTTGGGTTATTTTGAGATCTTTGGGTTTGGATCTACCAAGAAACATGCAAATCGAATTTTCTAGCGCCGTTCAAGACCATGCTGACTCCTTGGGTAGAGAACTAAAATCAGATGAGATTTCCAAGTTATTCAAAGAGGCTTACAACTACAATGACGAACAGTACCAAGCTATTAGTTTAGTCAATTATAATGTTGAAAAATTCGGCACTGAACGTAGAGTGTTCACTGGTCAAGTCAAAGTAGGCGACCAGATCGTCGATATTGAAGGTACAGGTAATGGTCCAATCTCTTCTTTGGTCGACGCCCTATCAAACTTGTTGAACGTGAGATTTGCCGTAGCAAACTACACAGAGCATTCTCTAGGTTCTGGTTCTTCTACGCAAGCTGCTTCTTACATCCATCTATCGTATAGGCGTAATGCCGACAACGAAAAGGCCTACAAATGGGGTGTAGGTGTCTCCGAAGATGTCGGTGATTCTTCAGTGAGAGCCATCTTTGCCACCATTAACAATATTATCCATTCTGGTGATGTGTCCATTCCATCTTTGGCCGAGGTCGAAGGTAAGAATGCTGCGGCATCTGGCTCTGCATAA","protein_sequence":"MVKESIIALAEHAASRASRVIPPVKLAYKNMLKDPSSKYKPFNAPKLSNRKWPDNRITRAPRWLSTDLRDGNQSLPDPMSVEQKKEYFHKLVNIGFKEIEVSFPSASQTDFDFTRYAVENAPDDVSIQCLVQSREHLIKRTVEALTGAKKATIHTYLATSDMFREIVFNMSREEAISKAVEATKLVRKLTKDDPSQQATRWSYEFSPECFSDTPGEFAVEICEAVKKAWEPTEENPIIFNLPATVEVASPNVYADQIEYFATHITEREKVCISTHCHNDRGCGVAATELGMLAGADRVEGCLFGNGERTGNVDLVTVAMNMYTQGVSPNLDFSDLTSVLDVVERCNKIPVSQRAPYGGDLVVCAFSGSHQDAIKKGFNLQNKKRAQGETQWRIPYLPLDPKDIGRDYEAVIRVNSQSGKGGAAWVILRSLGLDLPRNMQIEFSSAVQDHADSLGRELKSDEISKLFKEAYNYNDEQYQAISLVNYNVEKFGTERRVFTGQVKVGDQIVDIEGTGNGPISSLVDALSNLLNVRFAVANYTEHSLGSGSSTQAASYIHLSYRRNADNEKAYKWGVGVSEDVGDSSVRAIFATINNIIHSGDVSIPSLAEVEGKNAAASGSA"},{"created_at":"2011-05-26T19:31:00.000Z","updated_at":"2011-07-22T17:53:47.000Z","name":"3-isopropylmalate dehydratase","uniprot_id":"P07264","uniprot_name":"LEUC_YEAST","enzyme":true,"transporter":false,"gene_name":"LEU1","num_residues":779,"molecular_weight":"85793.70313","theoretical_pi":"5.69","general_function":"Involved in 3-isopropylmalate dehydratase activity","specific_function":"Catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate","reactions":[{"id":1147,"direction":"\u003c\u003e","locations":"cytoplasm","altext":null,"export":true,"pw_reaction_id":null,"source":null},{"id":1182,"direction":"\u003c\u003e","locations":"cytoplasm","altext":null,"export":true,"pw_reaction_id":null,"source":null},{"id":2574,"direction":"\u003e","locations":null,"altext":"(2R,3S)-3-isopropylmalate = (2S)-2-isopropylmaleate + H(2)O.","export":false,"pw_reaction_id":null,"source":null},{"id":2575,"direction":"\u003e","locations":null,"altext":"(2S)-2-isopropylmaleate + H(2)O = (2S)-2-isopropylmalate.","export":false,"pw_reaction_id":null,"source":null}],"signal_regions":"None","transmembrane_regions":"None","pdb_id":null,"cellular_location":null,"genbank_gene_id":"Z72531","genbank_protein_id":"1322463","gene_card_id":"LEU1","chromosome_location":"chromosome 7","locus":"YGL009C","synonyms":["Alpha-IPM isomerase","IPMI","Isopropylmalate isomerase"],"enzyme_classes":["4.2.1.33"],"go_classes":[{"category":"Component","description":" 3-isopropylmalate dehydratase complex"},{"category":"Component","description":" macromolecular complex"},{"category":"Component","description":" protein complex"},{"category":"Function","description":" lyase activity"},{"category":"Function","description":" 3-isopropylmalate dehydratase activity"},{"category":"Function","description":" binding"},{"category":"Function","description":" metal cluster binding"},{"category":"Function","description":" iron-sulfur cluster binding"},{"category":"Function","description":" carbon-oxygen lyase activity"},{"category":"Function","description":" hydro-lyase activity"},{"category":"Function","description":" 4 iron, 4 sulfur cluster binding"},{"category":"Function","description":" catalytic activity"},{"category":"Process","description":" metabolic process"},{"category":"Process","description":" leucine biosynthetic process"},{"category":"Process","description":" cellular metabolic process"},{"category":"Process","description":" cellular amino acid and derivative metabolic process"},{"category":"Process","description":" cellular amino acid metabolic process"},{"category":"Process","description":" cellular amino acid biosynthetic process"},{"category":"Process","description":" branched chain family amino acid metabolic process"},{"category":"Process","description":" leucine metabolic process"}],"pfams":[{"name":"Aconitase","identifier":"PF00330"},{"name":"Aconitase_C","identifier":"PF00694"}],"pathways":[{"name":"Valine, leucine and isoleucine biosynthesis","kegg_map_id":"00290"},{"name":"Citric Acid Cycle 1434561204","kegg_map_id":null},{"name":"TCA Cycle","kegg_map_id":null}],"gene_sequence":"ATGGTTTACACTCCATCCAAGGGTCCAAGAACTCTTTACGATAAGGTTTTTGATGCACATGTTGTCCATCAAGATGAAAATGGTTCCTTTTTGTTGTATATCGACAGACACTTGGTTCATGAAGTCACCTCTCCACAAGCTTTCGAAGGCCTAGAAAATGCCGGCAGAAAGGTCAGAAGAGTTGATTGTACTCTAGCTACTGTAGATCATAATATTCCAACTGAATCAAGAAAGAATTTCAAATCACTAGACACATTTATCAAGCAAACTGATTCGCGTTTACAAGTCAAAACTTTAGAGAATAATGTTAAACAGTTCGGCGTTCCATATTTCGGTATGAGTGATGCCAGACAAGGTATCGTCCACACCATCGGTCCCGAAGAAGGTTTCACTTTACCAGGTACCACTGTTGTTTGTGGTGACTCTCATACCTCTACTCACGGTGCCTTTGGTTCGCTGGCCTTTGGTATTGGTACTTCTGAAGTTGAACACGTCTTGGCCACTCAAACAATTATCCAAGCTAAATCGAAAAACATGAGAATTACTGTTAATGGTAAGCTATCACCTGGTATCACATCTAAAGATTTGATTTTGTATATTATTGGTCTGATAGGTACTGCAGGTGGTACTGGTTGCGTTATTGAATTCGCAGGTGAAGCCATTGAAGCTCTTTCTATGGAAGCACGTATGTCCATGTGTAACATGGCCATCGAAGCTGGTGCAAGAGCAGGTATGATTAAACCAGACGAAACTACTTTCCAATACACCAAAGGCAGACCTTTGGCTCCAAAAGGTGCCGAATGGGAAAAGGCTGTTGCCTACTGGAAAACTTTGAAAACAGACGAAGGTGCCAAATTTGACCACGAAATCAACATTGAAGCTGTCGACGTGATTCCAACTATTACATGGGGTACTTCTCCTCAAGATGCCTTACCAATTACTGGTTCCGTACCAGATCCAAAAAATGTTACAGACCCAATAAAGAAATCTGGTATGGAAAGAGCCTTAGCCTATATGGGTTTGGAACCTAACACACCGCTAAAGAGCATCAAAGTAGATAAAGTCTTTATTGGATCTTGTACCAATGGCCGTATTGAAGATTTAAGAAGTGCTGCAGCTGTAGTTAGGGGTCAAAAATTGGCTAGTAACATCAAATTAGCTATGGTTGTTCCGGGATCTGGTTTGGTCAAAAAACAAGCCGAAGCAGAAGGTTTGGACAAGATTTTCCAAGAAGCTGGTTTTGAATGGAGAGAAGCTGGTTGTTCAATATGTTTAGGTATGAACCCTGATATTTTGGATGCCTATGAACGTTGTGCTTCTACTTCCAACAGAAATTTCGAAGGTCGTCAAGGTGCCTTGTCTCGTACACATCTAATGTCCCCAGCCATGGCGGCTGCTGCAGGTATCGCAGGTCACTTCGTAGATATTAGAGAATTCGAATATAAGGATCAAGACCAAAGTAGTCCAAAGGTTGAGGTCACTTCCGAAGATGAAAAAGAGCTTGAAAGTGCTGCTTACGATCACGCTGAACCTGTCCAACCCGAAGACGCTCCCCAAGATATTGCCAATGATGAATTAAAAGATATTCCAGTGAAGTCAGATGATACACCTGCTAAACCTAGCTCTTCCGGCATGAAGCCATTTTTGACTTTGGAAGGTATTAGCGCACCATTAGATAAGGCCAATGTTGATACAGACGCTATTATCCCAAAGCAATTTTTAAAGACAATTAAGAGAACGGGTTTGAAAAAAGGGTTGTTTTATGAATGGCGTTTCCGTAAAGACGATCAAGGTAAGGATCAAGAAACCGATTTTGTATTAAATGTTGAACCTTGGAGGGAAGCTGAAATATTGGTTGTTACTGGTGACAATTTCGGATGTGGTTCTTCCAGAGAACACGCACCATGGGCTCTAAAAGACTTTGGTATAAAATCCATCATTGCACCTTCTTACGGTGATATTTTCTACAACAACTCTTTCAAGAACGGCTTATTACCTATTAGATTGGATCAACAAATAATCATTGACAAATTGATCCCTATTGCTAATAAGGGTGGTAAGCTCTGCGTCGATTTACCAAATCAAAAAATTTTGGATTCCGATGGCAATGTGCTCGTTGATCATTTTGAAATAGAACCTTTCAGAAAGCACTGCCTAGTTAACGGTCTTGATGATATTGGTATTACATTGCAAAAGGAAGAATACATTTCCAGATACGAAGCTTTGAGAAGAGAGAAATACTCATTCTTGGAAGGTGGATCAAAATTATTAAAATTTGACAACGTTCCAAAAAGAAAAGCTGTTACAACTACTTTCGATAAAGTCCACCAGGATTGGTAG","protein_sequence":"MVYTPSKGPRTLYDKVFDAHVVHQDENGSFLLYIDRHLVHEVTSPQAFEGLENAGRKVRRVDCTLATVDHNIPTESRKNFKSLDTFIKQTDSRLQVKTLENNVKQFGVPYFGMSDARQGIVHTIGPEEGFTLPGTTVVCGDSHTSTHGAFGSLAFGIGTSEVEHVLATQTIIQAKSKNMRITVNGKLSPGITSKDLILYIIGLIGTAGGTGCVIEFAGEAIEALSMEARMSMCNMAIEAGARAGMIKPDETTFQYTKGRPLAPKGAEWEKAVAYWKTLKTDEGAKFDHEINIEAVDVIPTITWGTSPQDALPITGSVPDPKNVTDPIKKSGMERALAYMGLEPNTPLKSIKVDKVFIGSCTNGRIEDLRSAAAVVRGQKLASNIKLAMVVPGSGLVKKQAEAEGLDKIFQEAGFEWREAGCSICLGMNPDILDAYERCASTSNRNFEGRQGALSRTHLMSPAMAAAAGIAGHFVDIREFEYKDQDQSSPKVEVTSEDEKELESAAYDHAEPVQPEDAPQDIANDELKDIPVKSDDTPAKPSSSGMKPFLTLEGISAPLDKANVDTDAIIPKQFLKTIKRTGLKKGLFYEWRFRKDDQGKDQETDFVLNVEPWREAEILVVTGDNFGCGSSREHAPWALKDFGIKSIIAPSYGDIFYNNSFKNGLLPIRLDQQIIIDKLIPIANKGGKLCVDLPNQKILDSDGNVLVDHFEIEPFRKHCLVNGLDDIGITLQKEEYISRYEALRREKYSFLEGGSKLLKFDNVPKRKAVTTTFDKVHQDW"}]}