{"ymdb_id":"YMDB00385","created_at":"2011-05-29T18:11:39.000Z","updated_at":"2016-10-18T17:11:28.000Z","name":"Formic acid","cas":"64-18-6","state":"Liquid","melting_point":"8.4 oC","description":"Formic acid (methanoic acid) is the simplest carboxylic acid. It is an intermediate in normal metabolism and occurs naturally, most notably in the venom of bee and ant stings.  Esters, salts, and the anion derived from formic acid are referred to as formates.","experimental_water_solubility":"1000 mg/mL at 25 oC [RIDDICK,JA et al. (1986)]","experimental_logp_hydrophobicity":"-0.54 [HANSCH,C ET AL. (1995)]","location":"Cytoplasm;Extracellular;Mitochondrion","synthesis_reference":" Finholt, Albert E.; Jacobson, Eugene C. The reduction of carbon dioxide to formic acid with lithium aluminum hydride. Journal of the American Chemical Society (1952), 74 3943-4.","chebi_id":"30751","hmdb_id":"HMDB00142","kegg_id":"C00058","pubchem_id":"284","cs_id":"278","foodb_id":null,"wikipedia_link":"Formic_acid","biocyc_id":"FORMATE","iupac":"formic acid","traditional_iupac":"formic acid","logp":"-0.2720444223333333","pka":null,"alogps_solubility":"4.77e+02 g/l","alogps_logp":"-0.47","alogps_logs":"1.02","acceptor_count":"2","donor_count":"1","rotatable_bond_count":"0","polar_surface_area":"37.3","refractivity":"8.1532","polarizability":"3.374057914916533","formal_charge":"0","physiological_charge":"-1","pka_strongest_basic":null,"pka_strongest_acidic":"4.2691179843154865","bioavailability":"1","number_of_rings":"0","rule_of_five":"1","ghose_filter":"0","veber_rule":"1","mddr_like_rule":"0","synonyms":["Add-F","Amasil","Ameisensaeure","Ameisensaure","Aminate","Aminic acid","Bilorin","Collo-Bueglatt","Collo-Didax","FMT","Formate","formic acid","Formira","Formisoton","Formylate","Formylic acid","HCO2 anion","HCOOH","Hydrogen carboxylate","Hydrogen carboxylic acid","hydrogencarboxylic acid","Kwas metaniowy","Kyselina mravenci","Methanoate","Methanoic acid","Methanoic acid monomer","Mierenzuur","Myrmicyl","Sodium Formate","Sybest","Trisodium phosphonoformate hexahydrate","Wonderbond Hardener M 600L"],"pathways":[{"name":"Glyoxylate and dicarboxylate metabolism","kegg_map_id":"00630"},{"name":"Pyruvate metabolism","kegg_map_id":"00620"},{"name":"Nitrogen metabolism","kegg_map_id":"00910"},{"name":"Methane metabolism","kegg_map_id":"00680"},{"name":"Cholesterol biosynthesis and metabolism CE(10:0)","kegg_map_id":null},{"name":"Cholesterol biosynthesis and metabolism CE(12:0)","kegg_map_id":null},{"name":"Cholesterol biosynthesis and metabolism CE(14:0)","kegg_map_id":null},{"name":"Cholesterol biosynthesis and metabolism CE(16:0)","kegg_map_id":null},{"name":"Cholesterol biosynthesis and metabolism CE(18:0)","kegg_map_id":null},{"name":"Methionine metabolism and salvage","kegg_map_id":null},{"name":"NAD metabolism","kegg_map_id":null},{"name":"One Carbon Pool by Folate I","kegg_map_id":null},{"name":"Steroid biosynthesis","kegg_map_id":"00100"},{"name":"Tryptophan metabolism","kegg_map_id":"00380"},{"name":"glycine metabolism","kegg_map_id":null},{"name":"purine nucleotides de novo biosynthesis","kegg_map_id":null},{"name":"Riboflavin metabolism","kegg_map_id":"00740"},{"name":"serine metabolism","kegg_map_id":null},{"name":"tetrahydrofolate biosynthesis","kegg_map_id":null}],"growth_conditions":[{"growth_media":"YEB media with 0.5 mM glucose","concentration":"14745.0","concentration_units":"\u0026#181;M","error":"737.0"}],"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":12595523,"citation":"Jin, C., Barrientos, A., Tzagoloff, A. (2003). \"Yeast dihydroxybutanone phosphate synthase, an enzyme of the riboflavin biosynthetic pathway, has a second unrelated function in expression of mitochondrial respiration.\" J Biol Chem 278:14698-14703."},{"pubmed_id":14506228,"citation":"Subhi, A. L., Diegelman, P., Porter, C. W., Tang, B., Lu, Z. J., Markham, G. D., Kruger, W. D. (2003). \"Methylthioadenosine phosphorylase regulates ornithine decarboxylase by production of downstream metabolites.\" J Biol Chem 278:49868-49873."},{"pubmed_id":12062417,"citation":"Panozzo, C., Nawara, M., Suski, C., Kucharczyka, R., Skoneczny, M., Becam, A. M., Rytka, J., Herbert, C. J. (2002). \"Aerobic and anaerobic NAD+ metabolism in Saccharomyces cerevisiae.\" FEBS Lett 517:97-102."},{"pubmed_id":10622712,"citation":"Lamb, D. C., Kelly, D. E., Manning, N. J., Kaderbhai, M. A., Kelly, S. L. (1999). \"Biodiversity of the P450 catalytic cycle: yeast cytochrome b5/NADH cytochrome b5 reductase complex efficiently drives the entire sterol 14-demethylation (CYP51) reaction.\" FEBS Lett 462:283-288."}],"proteins":[{"created_at":"2011-05-24T19:55:26.000Z","updated_at":"2011-05-27T14:55:59.000Z","name":"Probable kynurenine--oxoglutarate transaminase BNA3","uniprot_id":"P47039","uniprot_name":"BNA3_YEAST","enzyme":true,"transporter":false,"gene_name":"BNA3","num_residues":444,"molecular_weight":"50081.89844","theoretical_pi":"6.53","general_function":"Involved in 1-aminocyclopropane-1-carboxylate synthase activity","specific_function":"Catalyzes the irreversible transamination of the L- tryptophan metabolite L-kynurenine to form kynurenic acid (KA)","reactions":[{"id":1756,"direction":"\u003e","locations":"cytoplasm","altext":null,"export":true,"pw_reaction_id":null,"source":null},{"id":2282,"direction":"\u003e","locations":"Cytoplasm. Mitochondrion","altext":"L-kynurenine + 2-oxoglutarate = 4-(2-aminophenyl)-2,4-dioxobutanoate + L-glutamate.","export":false,"pw_reaction_id":null,"source":null},{"id":3723,"direction":"\u003e","locations":null,"altext":null,"export":true,"pw_reaction_id":"PW_R006249","source":"Smpdb"}],"signal_regions":"None","transmembrane_regions":"None","pdb_id":null,"cellular_location":"Cytoplasm. Mitochondrion","genbank_gene_id":"Z49335","genbank_protein_id":"1008205","gene_card_id":"BNA3","chromosome_location":"chromosome 10","locus":"YJL060W","synonyms":["Biosynthesis of nicotinic acid protein 3","Kynurenine aminotransferase"],"enzyme_classes":["2.6.1.7"],"go_classes":[{"category":"Component","description":" Not Available"},{"category":"Function","description":" pyridoxal phosphate binding"},{"category":"Function","description":" carbon-sulfur lyase activity"},{"category":"Function","description":" 1-aminocyclopropane-1-carboxylate synthase activity"},{"category":"Function","description":" catalytic activity"},{"category":"Function","description":" transferase activity"},{"category":"Function","description":" lyase activity"},{"category":"Function","description":" binding"},{"category":"Function","description":" transferase activity, transferring nitrogenous groups"},{"category":"Function","description":" cofactor binding"},{"category":"Process","description":" metabolic process"},{"category":"Process","description":" biosynthetic process"}],"pfams":[{"name":"Aminotran_1_2","identifier":"PF00155"}],"pathways":[{"name":"Tryptophan metabolism","kegg_map_id":"00380"},{"name":"L-alanine metabolism","kegg_map_id":null}],"gene_sequence":"ATGAAACAACGATTCATTCGTCAATTTACGAACCTAATGTCTACTTCGAGACCGAAAGTTGTTGCCAACAAATATTTCACTTCTAACACTGCCAAAGATGTTTGGTCGCTAACCAATGAAGCCGCTGCAAAAGCTGCCAATAACTCCAAAAACCAAGGCCGTGAACTTATTAATTTAGGCCAAGGCTTTTTTTCATATTCCCCTCCTCAATTCGCCATTAAGGAGGCTCAGAAAGCCCTAGACATTCCAATGGTCAATCAATATTCTCCAACTAGAGGTCGACCTTCATTAATTAATTCCTTGATTAAGTTGTATTCTCCTATTTATAACACAGAATTGAAAGCGGAAAATGTTACCGTAACAACAGGTGCCAATGAAGGTATACTTTCTTGCTTGATGGGGCTTTTGAACGCTGGCGACGAGGTTATTGTTTTTGAACCTTTCTTTGACCAATATATTCCAAATATCGAACTTTGCGGTGGTAAAGTTGTTTACGTCCCCATAAATCCTCCAAAGGAATTGGATCAAAGGAATACTAGAGGTGAAGAATGGACCATTGACTTTGAGCAGTTCGAAAAAGCGATTACATCCAAGACAAAAGCTGTCATTATCAATACCCCTCACAACCCAATTGGTAAAGTTTTCACGCGCGAGGAATTAACCACTTTAGGTAACATTTGCGTCAAGCACAACGTTGTGATTATATCTGATGAAGTCTATGAACACCTTTACTTCACTGATTCTTTCACTAGAATTGCCACACTCTCTCCAGAAATTGGGCAACTAACCTTAACGGTCGGTTCTGCCGGTAAATCGTTTGCTGCTACTGGTTGGAGAATTGGTTGGGTCTTATCCTTGAACGCAGAGTTGTTAAGTTATGCAGCTAAGGCACATACAAGAATTTGTTTTGCATCTCCATCCCCTCTACAGGAAGCTTGTGCAAACTCTATTAACGACGCTTTAAAAATTGGGTATTTTGAAAAAATGAGACAGGAATATATCAACAAATTCAAAATTTTCACATCGATCTTTGATGAATTGGGACTACCATATACAGCTCCAGAGGGTACATATTTTGTCCTCGTTGATTTCTCTAAAGTGAAAATTCCCGAGGACTATCCCTACCCAGAGGAGATCCTGAATAAGGGAAAAGATTTTCGCATTTCTCACTGGTTGATCAATGAATTAGGTGTGGTTGCCATTCCACCAACTGAATTCTATATCAAAGAGCACGAAAAGGCTGCTGAGAATTTGTTAAGGTTTGCAGTTTGTAAAGATGATGCTTATCTAGAAAATGCCGTAGAGAGATTAAAACTACTCAAGGACTACTTATAA","protein_sequence":"MKQRFIRQFTNLMSTSRPKVVANKYFTSNTAKDVWSLTNEAAAKAANNSKNQGRELINLGQGFFSYSPPQFAIKEAQKALDIPMVNQYSPTRGRPSLINSLIKLYSPIYNTELKAENVTVTTGANEGILSCLMGLLNAGDEVIVFEPFFDQYIPNIELCGGKVVYVPINPPKELDQRNTRGEEWTIDFEQFEKAITSKTKAVIINTPHNPIGKVFTREELTTLGNICVKHNVVIISDEVYEHLYFTDSFTRIATLSPEIGQLTLTVGSAGKSFAATGWRIGWVLSLNAELLSYAAKAHTRICFASPSPLQEACANSINDALKIGYFEKMRQEYINKFKIFTSIFDELGLPYTAPEGTYFVLVDFSKVKIPEDYPYPEEILNKGKDFRISHWLINELGVVAIPPTEFYIKEHEKAAENLLRFAVCKDDAYLENAVERLKLLKDYL"},{"created_at":"2011-05-24T20:03:33.000Z","updated_at":"2011-05-27T14:55:59.000Z","name":"Lanosterol 14-alpha demethylase","uniprot_id":"P10614","uniprot_name":"CP51_YEAST","enzyme":true,"transporter":false,"gene_name":"ERG11","num_residues":530,"molecular_weight":"60719.80078","theoretical_pi":"8.95","general_function":"Involved in iron ion binding","specific_function":"Catalyzes C14-demethylation of lanosterol which is critical for ergosterol biosynthesis. It transforms lanosterol into 4,4'-dimethyl cholesta-8,14,24-triene-3-beta-ol","reactions":[{"id":2295,"direction":"\u003e","locations":"Membrane; Single-pass membrane protein","altext":"Obtusifoliol + 3 O(2) + 3 NADPH = 4-alpha-methyl-5-alpha-ergosta-8,14,24(28)-trien-3-beta-ol + formate + 3 NADP(+) + 4 H(2)O.","export":false,"pw_reaction_id":null,"source":null},{"id":14387,"direction":"\u003e","locations":null,"altext":null,"export":true,"pw_reaction_id":"PW_R006897","source":"Smpdb"}],"signal_regions":"None","transmembrane_regions":"21-41","pdb_id":null,"cellular_location":"Membrane; Single-pass membrane protein","genbank_gene_id":"M18109","genbank_protein_id":"170946","gene_card_id":"ERG11","chromosome_location":"chromosome 8","locus":"YHR007C","synonyms":["CYPLI","Cytochrome P450 51","Cytochrome P450-14DM","Cytochrome P450-LIA1","Sterol 14-alpha demethylase"],"enzyme_classes":["1.14.13.70"],"go_classes":[{"category":"Component","description":" Not Available"},{"category":"Function","description":" oxidoreductase activity"},{"category":"Function","description":" heme binding"},{"category":"Function","description":" electron carrier activity"},{"category":"Function","description":" monooxygenase activity"},{"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":" iron ion binding"},{"category":"Process","description":" Not Available"}],"pfams":[{"name":"p450","identifier":"PF00067"}],"pathways":[{"name":"Steroid biosynthesis","kegg_map_id":"00100"},{"name":"Cholesterol biosynthesis and metabolism CE(10:0)","kegg_map_id":null},{"name":"Cholesterol biosynthesis and metabolism CE(12:0)","kegg_map_id":null},{"name":"Cholesterol biosynthesis and metabolism CE(14:0)","kegg_map_id":null},{"name":"Cholesterol biosynthesis and metabolism CE(16:0)","kegg_map_id":null},{"name":"Cholesterol biosynthesis and metabolism CE(18:0)","kegg_map_id":null}],"gene_sequence":"ATGTCTGCTACCAAGTCAATCGTTGGAGAGGCATTGGAATACGTAAACATTGGTTTAAGTCATTTCTTGGCTTTACCATTGGCCCAAAGAATCTCTTTGATCATAATAATTCCTTTCATTTACAATATTGTATGGCAATTACTATATTCTTTGAGAAAGGACCGTCCACCTCTAGTGTTTTACTGGATTCCATGGGTCGGTAGTGCTGTTGTGTACGGTATGAAGCCATACGAGTTTTTCGAAGAATGTCAAAAGAAATACGGTGATATTTTTTCATTCGTTTTGTTAGGAAGAGTCATGACTGTGTATTTAGGACCAAAGGGTCACGAATTTGTCTTCAACGCTAAGTTGGCAGATGTTTCAGCAGAAGCTGCTTACGCTCATTTGACTACTCCAGTTTTCGGTAAAGGTGTTATTTACGATTGTCCAAATTCTAGATTGATGGAGCAAAAGAAGTTTGTTAAGGGTGCTCTAACCAAAGAAGCCTTCAAGAGCTACGTTCCATTGATTGCTGAAGAAGTGTACAAGTACTTCAGAGACTCCAAAAACTTCCGTTTGAATGAAAGAACTACTGGTACTATTGACGTGATGGTTACTCAACCTGAAATGACTATTTTCACCGCTTCAAGATCATTATTGGGTAAGGAAATGAGAGCAAAATTGGATACCGATTTTGCTTACTTGTACAGTGATTTGGATAAGGGTTTCACTCCAATCAACTTCGTCTTCCCTAACTTACCATTGGAACACTATAGAAAGAGAGATCACGCTCAAAAGGCTATCTCCGGTACTTACATGTCTTTGATTAAGGAAAGAAGAAAGAACAACGACATTCAAGACAGAGATTTGATCGATTCCTTGATGAAGAACTCTACCTACAAGGATGGTGTGAAGATGACTGATCAAGAAATCGCTAACTTGTTAATTGGTGTCTTAATGGGTGGTCAACATACTTCTGCTGCCACTTCTGCTTGGATTTTGTTGCACTTGGCTGAAAGACCAGATGTCCAACAAGAATTGTACGAAGAACAAATGCGTGTTTTGGATGGTGGTAAGAAGGAATTGACCTACGATTTATTACAAGAAATGCCATTGTTGAACCAAACTATTAAGGAAACTCTAAGAATGCACCATCCATTGCACTCTTTGTTCCGTAAGGTTATGAAAGATATGCACGTTCCAAACACTTCTTATGTCATCCCAGCAGGTTATCACGTTTTGGTTTCTCCAGGTTACACTCATTTAAGAGACGAATACTTCCCTAATGCTCACCAATTCAACATTCACCGTTGGAACAAAGATTCTGCCTCCTCTTATTCCGTCGGTGAAGAAGTCGATTACGGTTTCGGTGCCATTTCTAAGGGTGTCAGCTCTCCATACTTACCTTTCGGTGGTGGTAGACACAGATGTATCGGTGAACACTTTGCTTACTGTCAGCTAGGTGTTCTAATGTCCATTTTTATCAGAACATTAAAATGGCATTACCCAGAGGGTAAGACCGTTCCACCTCCTGACTTTACATCTATGGTTACTCTTCCAACCGGTCCAGCCAAGATCATCTGGGAAAAGAGAAATCCAGAACAAAAGATCTAA","protein_sequence":"MSATKSIVGEALEYVNIGLSHFLALPLAQRISLIIIIPFIYNIVWQLLYSLRKDRPPLVFYWIPWVGSAVVYGMKPYEFFEECQKKYGDIFSFVLLGRVMTVYLGPKGHEFVFNAKLADVSAEAAYAHLTTPVFGKGVIYDCPNSRLMEQKKFVKGALTKEAFKSYVPLIAEEVYKYFRDSKNFRLNERTTGTIDVMVTQPEMTIFTASRSLLGKEMRAKLDTDFAYLYSDLDKGFTPINFVFPNLPLEHYRKRDHAQKAISGTYMSLIKERRKNNDIQDRDLIDSLMKNSTYKDGVKMTDQEIANLLIGVLMGGQHTSAATSAWILLHLAERPDVQQELYEEQMRVLDGGKKELTYDLLQEMPLLNQTIKETLRMHHPLHSLFRKVMKDMHVPNTSYVIPAGYHVLVSPGYTHLRDEYFPNAHQFNIHRWNKDSASSYSVGEEVDYGFGAISKGVSSPYLPFGGGRHRCIGEHFAYCQLGVLMSIFIRTLKWHYPEGKTVPPPDFTSMVTLPTGPAKIIWEKRNPEQKI"},{"created_at":"2011-05-24T20:34:21.000Z","updated_at":"2011-05-29T14:01:21.000Z","name":"Enolase-phosphatase E1","uniprot_id":"P32626","uniprot_name":"ENOPH_YEAST","enzyme":true,"transporter":false,"gene_name":"UTR4","num_residues":227,"molecular_weight":"25187.19922","theoretical_pi":"5.3","general_function":"Involved in catalytic activity","specific_function":"Bifunctional enzyme that catalyzes the enolization of 2,3-diketo-5-methylthiopentyl-1-phosphate (DK-MTP-1-P) into the intermediate 2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate (HK-MTPenyl-1-P), which is then dephosphorylated to form the acireductone 1,2-dihydroxy-3-keto-5-methylthiopentene (DHK-MTPene)","reactions":[{"id":2327,"direction":"\u003e","locations":"Cytoplasm. Nucleus","altext":"5-(methylthio)-2,3-dioxopentyl phosphate + H(2)O = 1,2-dihydroxy-5-(methylthio)pent-1-en-3-one + phosphate.","export":false,"pw_reaction_id":null,"source":null},{"id":2328,"direction":"\u003e","locations":"Cytoplasmic;Cytoplasm. Nucleus","altext":"2-Phosphoglycolate + H2O = glycolate + phosphate","export":false,"pw_reaction_id":null,"source":null},{"id":3792,"direction":null,"locations":null,"altext":null,"export":true,"pw_reaction_id":"PW_R006311","source":"Smpdb"}],"signal_regions":"None","transmembrane_regions":"None","pdb_id":null,"cellular_location":"Cytoplasm. Nucleus","genbank_gene_id":"U18779","genbank_protein_id":"603641","gene_card_id":"UTR4","chromosome_location":"chromosome 5","locus":"YEL038W","synonyms":["2,3-diketo-5-methylthio-1-phosphopentane phosphatase","Unknown transcript 4 protein"],"enzyme_classes":["3.1.3.77","3.1.3.18"],"go_classes":[{"category":"Component","description":" Not Available"},{"category":"Function","description":" metal ion binding"},{"category":"Function","description":" hydrolase activity"},{"category":"Function","description":" hydrolase activity, acting on ester bonds"},{"category":"Function","description":" phosphoric ester hydrolase activity"},{"category":"Function","description":" phosphatase activity"},{"category":"Function","description":" phosphoglycolate phosphatase activity"},{"category":"Function","description":" acireductone synthase activity"},{"category":"Function","description":" catalytic activity"},{"category":"Function","description":" binding"},{"category":"Function","description":" ion binding"},{"category":"Function","description":" cation binding"},{"category":"Process","description":" cellular amino acid biosynthetic process"},{"category":"Process","description":" amino acid salvage"},{"category":"Process","description":" metabolic process"},{"category":"Process","description":" L-methionine salvage from methylthioadenosine"},{"category":"Process","description":" cellular metabolic process"},{"category":"Process","description":" cellular amino acid and derivative metabolic process"},{"category":"Process","description":" cellular amino acid metabolic process"}],"pfams":[{"name":"Hydrolase","identifier":"PF00702"}],"pathways":[{"name":"Cysteine and methionine metabolism","kegg_map_id":"00270"},{"name":"Methionine metabolism and salvage","kegg_map_id":null}],"gene_sequence":"ATGGTCATTGGGCAAAAGGTCCTGCTAGCTCGTATACCAAAAATGGGAGACAATTACTCGACTTACTTGCTTGATATTGAAGGGACAGTGTGCCCGATCTCGTTCGTGAAGGAGACTTTATTCCCTTATTTCACGAATAAAGTGCCGCAATTGGTTCAACAGGATACAAGGGACTCCCCGGTTTCCAACATTCTGTCGCAGTTTCACATCGACAATAAGGAGCAGTTGCAGGCGCATATTTTGGAGTTGGTGGCCAAGGATGTGAAGGATCCAATCTTGAAACAGTTGCAAGGCTACGTCTGGGCTCACGGATACGAATCTGGGCAGATTAAGGCGCCCGTTTATGCAGATGCTATTGACTTTATCAAGAGGAAGAAGCGTGTGTTTATCTACTCTAGTGGATCTGTAAAGGCACAGAAATTGCTGTTCGGGTATGTTCAGGATCCCAACGCGCCTGCGCATGATTCGTTGGATTTGAATTCTTATATAGATGGTTATTTCGACATCAACACTTCTGGAAAGAAAACCGAAACACAGTCTTACGCCAACATCTTGCGGGATATCGGTGCGAAGGCTAGCGAGGTACTGTTCTTGAGCGATAATCCATTGGAATTGGACGCAGCGGCCGGCGTTGGAATAGCTACTGGGTTAGCTTCCCGACCTGGTAATGCACCTGTCCCCGATGGGCAAAAGTACCAGGTATACAAGAATTTTGAAACTCTTTAA","protein_sequence":"MGDNYSTYLLDIEGTVCPISFVKETLFPYFTNKVPQLVQQDTRDSPVSNILSQFHIDNKEQLQAHILELVAKDVKDPILKQLQGYVWAHGYESGQIKAPVYADAIDFIKRKKRVFIYSSGSVKAQKLLFGYVQDPNAPAHDSLDLNSYIDGYFDINTSGKKTETQSYANILRDIGAKASEVLFLSDNPLELDAAAGVGIATGLASRPGNAPVPDGQKYQVYKNFETL"},{"created_at":"2011-05-26T16:59:39.000Z","updated_at":"2011-05-27T15:01:01.000Z","name":"Phosphoribosylaminoimidazole carboxylase","uniprot_id":"P21264","uniprot_name":"PUR6_YEAST","enzyme":true,"transporter":false,"gene_name":"ADE2","num_residues":571,"molecular_weight":"62338.69922","theoretical_pi":"7.36","general_function":"Involved in phosphoribosylaminoimidazole carboxylase activity","specific_function":"5-amino-1-(5-phospho-D-ribosyl)imidazole-4- carboxylate = 5-amino-1-(5-phospho-D-ribosyl)imidazole + CO(2)","reactions":[{"id":1884,"direction":"\u003c\u003e","locations":"cytoplasm","altext":null,"export":true,"pw_reaction_id":null,"source":null},{"id":2456,"direction":"\u003e","locations":null,"altext":"5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate = 5-amino-1-(5-phospho-D-ribosyl)imidazole + CO(2).","export":false,"pw_reaction_id":null,"source":null},{"id":14240,"direction":"\u003e","locations":null,"altext":null,"export":true,"pw_reaction_id":"PW_R006683","source":"Smpdb"},{"id":14241,"direction":"\u003e","locations":null,"altext":null,"export":true,"pw_reaction_id":"PW_R006686","source":"Smpdb"},{"id":14242,"direction":"\u003e","locations":null,"altext":null,"export":true,"pw_reaction_id":"PW_R006799","source":"Smpdb"}],"signal_regions":"None","transmembrane_regions":"None","pdb_id":null,"cellular_location":null,"genbank_gene_id":"M59824","genbank_protein_id":"171003","gene_card_id":"ADE2","chromosome_location":"chromosome 15","locus":"YOR128C","synonyms":["AIR carboxylase","AIRC"],"enzyme_classes":["4.1.1.21"],"go_classes":[{"category":"Component","description":" Not Available"},{"category":"Function","description":" adenyl ribonucleotide binding"},{"category":"Function","description":" ATP binding"},{"category":"Function","description":" phosphoribosylaminoimidazole carboxylase activity"},{"category":"Function","description":" lyase activity"},{"category":"Function","description":" catalytic activity"},{"category":"Function","description":" carbon-carbon lyase activity"},{"category":"Function","description":" carboxy-lyase activity"},{"category":"Function","description":" binding"},{"category":"Function","description":" nucleoside binding"},{"category":"Function","description":" purine nucleoside binding"},{"category":"Function","description":" adenyl nucleotide binding"},{"category":"Process","description":" nucleoside phosphate metabolic process"},{"category":"Process","description":" nucleotide metabolic process"},{"category":"Process","description":" purine nucleotide metabolic process"},{"category":"Process","description":" purine nucleotide biosynthetic process"},{"category":"Process","description":" purine nucleoside monophosphate biosynthetic process"},{"category":"Process","description":" purine ribonucleoside monophosphate biosynthetic process"},{"category":"Process","description":" IMP biosynthetic process"},{"category":"Process","description":" 'de novo' IMP biosynthetic process"},{"category":"Process","description":" metabolic process"},{"category":"Process","description":" nitrogen compound metabolic process"},{"category":"Process","description":" cellular nitrogen compound metabolic process"},{"category":"Process","description":" nucleobase, nucleoside, nucleotide and nucleic acid metabolic process"},{"category":"Process","description":" nucleobase, nucleoside and nucleotide metabolic process"}],"pfams":[{"name":"AIRC","identifier":"PF00731"},{"name":"ATP-grasp","identifier":"PF02222"}],"pathways":[{"name":"Purine metabolism","kegg_map_id":"00230"},{"name":"One Carbon Pool by Folate 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biosynthesis","kegg_map_id":null}],"gene_sequence":"ATGTTGTCGAGACTATCTTTATTGAGTAACTCGAGGGCGTTCCAACAGGCCAGATGGCGCATTTACCGCTTAAAAGTTTCGCCAACTGTGCATGCTTCTCAATACCATATTCTTTCTGGTAGGAAACTTGCTCAATCTATTCGAGAAAAAGCCAATGATGAGATACAAGCCATTAAGCTTAAGCATCCTAATTTCAAGCCTACCTTGAAAATCATTCAAGTCGGGGCCAGACCAGACTCATCTACGTACGTGAGGATGAAATTGAAAGCTTCAAAGGACAGCAATGTAGACTGTATCATAGAGAAGTTACCAGCAGAAATCACTGAAGTTGAGCTTTTGAAGAAAATTAGTGACATCAATGATGATGACTCTATCCATGGGTTGCTAATTCAACTACCTCTACCGCGTCACTTGGATGAAACCACGATTACAAACGCTGTGGACTTTAAAAAGGACGTTGATGGGTTCCACAGATATAATGCTGGTGAATTGGCTAAAAAAGGAGGGAAACCATACTTCATACCATGTACTCCTTATGGTTGCATGAAATTACTTGAAGAAGCTCATGTTAAGTTAGATGGTAAGAACGCCGTCGTGTTAGGCAGATCAAGTATCGTCGGAAATCCAATTGCTTCGTTGTTGAAAAATGCGAATGCCACTGTTACTGTCTGTCATAGTCATACAAGGAACATTGCAGAAGTGGTCTCCCAAGCTGATATAGTTATCGCAGCTTGCGGTATTCCTCAATACGTTAAATCAGACTGGATTAAAGAAGGCGCCGTGGTTATTGATGTAGGTATCAACTACGTACCTGATATCAGTAAGAAAAGTGGGCAAAAATTAGTTGGTGATGTTGATTTTGATTCTGTAAAGGAAAAGACATCTTATATTACCCCTGTTCCTGGTGGAGTGGGTCCAATGACTGTCGCTATGCTTGTTTCCAATGTACTATTAGCTGCTAAAAGGCAATTCGTGGAATCTGAAAAGCTTCCAGTTATCAAACCTCTTCCATTACACTTAGAAAGTCCAGTGCCTTCAGATATTGATATATCAAGAGCTCAGAGTCCTAAGCATATCAAGCAAGTTGCCGAGGAGTTGGGAATCCACTCTCACGAATTAGAATTATACGGCCACTATAAGGCAAAAATTTCTCCAAATATTTTTAAAAGATTAGAATCTAGAGAAAACGGTAAGTACGTCCTTGTTGCAGGTATTACTCCGACTCCATTGGGTGAAGGTAAATCCACTACGACTATGGGGTTGGTGCAGGCTTTATCCGCTCATTTAGGGAAACCATCCATCGCGAACGTTAGACAACCATCTCTTGGCCCAACCCTGGGTGTCAAAGGTGGTGCTGCTGGTGGTGGTTATGCCCAAGTTATTCCTATGGACGAGTTCAATTTACATTTGACCGGGGATATTCATGCTATCAGCGCTGCGAACAATCTTCTTGCAGCAGCTATCGACACTAGAATGTTCCATGAAGCCACTCAGAAGAATGATAGTACATTTTACAAGAGACTAGTTCCAAGAAAAAAAGGCATCAGAAAGTTTACCCCATCCATGCAGAGAAGGCTTAAAAGATTGGATATTGAAAAAGAAGACCCTGATGCTTTAACACCTGAAGAAGTCAAAAGATTTGCTAGATTGAACATAAATCCCGATACTATCACTATCAGAAGAGTTGTCGACATCAATGACAGGATGTTAAGACAAATTACCATTGGCGAAGCCGCTACGGAGAAGGGTTTTACAAGGACCACTGGATTCGATATCACTGTTGCCTCTGAATTAATGGCCATTTTAGCTCTATCTAAAAGCTTACACGAGATGAAGGAACGTATTGGACGCATGGTTATTGGTGCTGATTATGATAACAAACCAGTAACAGTAGAAGATATTGGCTGTACCGGTGCTCTGACTGCATTATTACGTGACGCTATAAAGCCTAACTTAATGCAAACTTTGGAAGGGACCCCCGTAATGGTTCACGCTGGTCCTTTCGCCAACATCTCCATCGGCGCATCATCAGTAATTGCAGACTTAATGGCATTGAAGCTTGTTGGTTCAGAAAAGAACCCGTTAAATGACAAGAACATCCATGAACCTGGTTATGTAGTTACTGAAGCAGGATTCGATTTTGCCATGGGTGGTGAAAGATTCTTTGATATCAAATGTCGTTCCTCTGGATTGGTGCCAGATGCAGTTGTCTTAGTCGCAACCGTAAGAGCTTTGAAATCTCATGGAGGTGCTCCAAATGTTAAGCCCGGACAATCATTACCAAAAGAATACACAGAGGAAAACATCGATTTTGTTGCCAAGGGTGTTAGTAATTTGGTTAAGCAGATTGAAAACATCAAAACGTTTGGAATACCAGTCGTTGTAGCAATCAACAGATTTGAAACAGACTCACAGGCAGAGATTGAGGTAATCAAGAAAGCAGCCTTGAATGCTGGCGCATCTCATGCCGTTACTTCTAATCACTGGATGGAAGGTGGTAAAGGTGCAGTAGAATTAGCACATGCTGTGGTAGATGCAACGAAAGAACCAAAGAACTTTAACTTTTTGTACGACGTCAATAGCTCCATCGAGGACAAGCTTACCAGCATCGTCCAAAAAATGTATGGTGGGGCAAAAATCGAAGTATCACCAGAAGCCCAAAAAAAGATAGACACCTACAAAAAACAAGGCTTCGGTAATCTTCCCATCTGTATTGCTAAGACACAATATTCATTATCCCATGATCCATCATTAAAGGGTGTTCCTAGAGGTTTTACGTTCCCCATCAGGGATGTGAGAGCTTCAATAGGTGCAGGTTATTTATACGCTTTGGCTGCAGAAATTCAAACCATACCGGGTCTATCGACATATGCTGGTTACATGGCAGTAGAAGTCGACGACGACGGTGAAATTGAAGGTCTATTTTAA","protein_sequence":"MLSRLSLLSNSRAFQQARWRIYRLKVSPTVHASQYHILSGRKLAQSIREKANDEIQAIKLKHPNFKPTLKIIQVGARPDSSTYVRMKLKASKDSNVDCIIEKLPAEITEVELLKKISDINDDDSIHGLLIQLPLPRHLDETTITNAVDFKKDVDGFHRYNAGELAKKGGKPYFIPCTPYGCMKLLEEAHVKLDGKNAVVLGRSSIVGNPIASLLKNANATVTVCHSHTRNIAEVVSQADIVIAACGIPQYVKSDWIKEGAVVIDVGINYVPDISKKSGQKLVGDVDFDSVKEKTSYITPVPGGVGPMTVAMLVSNVLLAAKRQFVESEKLPVIKPLPLHLESPVPSDIDISRAQSPKHIKQVAEELGIHSHELELYGHYKAKISPNIFKRLESRENGKYVLVAGITPTPLGEGKSTTTMGLVQALSAHLGKPSIANVRQPSLGPTLGVKGGAAGGGYAQVIPMDEFNLHLTGDIHAISAANNLLAAAIDTRMFHEATQKNDSTFYKRLVPRKKGIRKFTPSMQRRLKRLDIEKEDPDALTPEEVKRFARLNINPDTITIRRVVDINDRMLRQITIGEAATEKGFTRTTGFDITVASELMAILALSKSLHEMKERIGRMVIGADYDNKPVTVEDIGCTGALTALLRDAIKPNLMQTLEGTPVMVHAGPFANISIGASSVIADLMALKLVGSEKNPLNDKNIHEPGYVVTEAGFDFAMGGERFFDIKCRSSGLVPDAVVLVATVRALKSHGGAPNVKPGQSLPKEYTEENIDFVAKGVSNLVKQIENIKTFGIPVVVAINRFETDSQAEIEVIKKAALNAGASHAVTSNHWMEGGKGAVELAHAVVDATKEPKNFNFLYDVNSSIEDKLTSIVQKMYGGAKIEVSPEAQKKIDTYKKQGFGNLPICIAKTQYSLSHDPSLKGVPRGFTFPIRDVRASIGAGYLYALAAEIQTIPGLSTYAGYMAVEVDDDGEIEGLF"},{"created_at":"2011-05-26T17:53:55.000Z","updated_at":"2011-05-27T15:01:02.000Z","name":"C-1-tetrahydrofolate 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diphosphate.","export":false,"pw_reaction_id":null,"source":null},{"id":14108,"direction":"\u003e","locations":null,"altext":null,"export":true,"pw_reaction_id":"PW_R006539","source":"Smpdb"}],"signal_regions":"None","transmembrane_regions":"None","pdb_id":null,"cellular_location":"Cytoplasmic","genbank_gene_id":"X74738","genbank_protein_id":"511141","gene_card_id":"RIB1","chromosome_location":"chromosome 2","locus":"YBL033C","synonyms":["GTP cyclohydrolase II"],"enzyme_classes":["3.5.4.25"],"go_classes":[{"category":"Component","description":" Not Available"},{"category":"Function","description":" hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amidines"},{"category":"Function","description":" cyclohydrolase activity"},{"category":"Function","description":" GTP cyclohydrolase activity"},{"category":"Function","description":" GTP cyclohydrolase II activity"},{"category":"Function","description":" catalytic activity"},{"category":"Function","description":" hydrolase activity"},{"category":"Function","description":" hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds"},{"category":"Process","description":" riboflavin metabolic process"},{"category":"Process","description":" riboflavin biosynthetic process"},{"category":"Process","description":" metabolic process"},{"category":"Process","description":" nitrogen compound metabolic process"}],"pfams":[{"name":"GTP_cyclohydro2","identifier":"PF00925"}],"pathways":[{"name":"Riboflavin 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hydrolase","uniprot_id":"P40363","uniprot_name":"SFGH_YEAST","enzyme":true,"transporter":false,"gene_name":null,"num_residues":299,"molecular_weight":"33934.0","theoretical_pi":"6.7","general_function":"Involved in carboxylesterase activity","specific_function":"Serine hydrolase involved in the detoxification of formaldehyde","reactions":[{"id":1958,"direction":"\u003c\u003e","locations":"cytoplasm","altext":null,"export":true,"pw_reaction_id":null,"source":null},{"id":2702,"direction":"\u003e","locations":"Cytoplasm","altext":"S-formylglutathione + H(2)O = glutathione + formate.","export":false,"pw_reaction_id":null,"source":null},{"id":2703,"direction":"\u003e","locations":"Cytoplasm","altext":"4-methylumbelliferyl acetate + H2O = 4-methylumbelliferone + acetate","export":false,"pw_reaction_id":null,"source":null}],"signal_regions":"None","transmembrane_regions":"None","pdb_id":"1PV1","cellular_location":"Cytoplasm","genbank_gene_id":"X88851","genbank_protein_id":"895893","gene_card_id":null,"chromosome_location":null,"locus":"YJL068C","synonyms":["FGH"],"enzyme_classes":["3.1.2.12","3.1.1.56"],"go_classes":[{"category":"Component","description":" vesicle"},{"category":"Component","description":" cytoplasmic vesicle"},{"category":"Component","description":" cytoplasmic membrane-bounded vesicle"},{"category":"Component","description":" organelle"},{"category":"Function","description":" thiolester hydrolase activity"},{"category":"Function","description":" S-formylglutathione hydrolase activity"},{"category":"Function","description":" catalytic activity"},{"category":"Function","description":" hydrolase activity"},{"category":"Function","description":" hydrolase activity, acting on ester bonds"},{"category":"Function","description":" carboxylesterase activity"},{"category":"Process","description":" Not Available"}],"pfams":[{"name":"Esterase","identifier":"PF00756"}],"pathways":[{"name":"Methane 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4-phosphate.","export":false,"pw_reaction_id":null,"source":null},{"id":14111,"direction":"\u003e","locations":null,"altext":null,"export":true,"pw_reaction_id":"PW_R006542","source":"Smpdb"}],"signal_regions":"None","transmembrane_regions":"None","pdb_id":null,"cellular_location":null,"genbank_gene_id":"AY557810","genbank_protein_id":"45269511","gene_card_id":"RIB3","chromosome_location":"chromosome 4","locus":"YDR487C","synonyms":["DHBP synthase"],"enzyme_classes":["4.1.99.12"],"go_classes":[{"category":"Component","description":" Not Available"},{"category":"Function","description":" 3,4-dihydroxy-2-butanone-4-phosphate synthase activity"},{"category":"Function","description":" catalytic activity"},{"category":"Function","description":" lyase activity"},{"category":"Function","description":" carbon-carbon lyase activity"},{"category":"Process","description":" riboflavin metabolic process"},{"category":"Process","description":" riboflavin biosynthetic process"},{"category":"Process","description":" metabolic process"},{"category":"Process","description":" nitrogen compound metabolic process"}],"pfams":[{"name":"DHBP_synthase","identifier":"PF00926"}],"pathways":[{"name":"Riboflavin metabolism","kegg_map_id":"00740"}],"gene_sequence":"ATGTTTACACCAATTGATCAAGCTATAGAACACTTCAAGCAGAATAAGTTTGTAATTGTTATGGACGATGCCGGTCGTGAAAATGAAGGTGATCTTATTTGCGCTGCTGAAAATGTCAGCACTGAACAAATGGCCTTTCTTGTACGCCATTCCTCAGGCTACGTCTGTGCACCTATGACGAATGCCATTGCTGATAAGTTGGACCTTCCACTACTGAGAACAGGCATGAAGTTTGAATCCAATGATGACGACAGGCATGGAACTGCATACACAATAACTGTAGATGTAGCCCAAGGCACTACCACAGGTATTTCTGCTCACGACAGGTCGATGACTTGTAGGGCTCTTGCAGACTCTTCCTCTACGCCAAAATCATTTTTAAAACCAGGGCACATCTGTCCCTTGAGAGCCGCTGATGGCGGTGTTTTGCAGAGAAGAGGCCACACTGAGGCCGGTGTCGATTTGTGTAAACTAAGTGGACTAAGTCCCGTCGCTGTTATTGGCGAATTGGTTAACGATGACGAACAAGGAACTATGATGAGATTAAATGACTGCCAAGCGTTTGGTAAGAAACATGGCATTCCTTTGATCTCCATCGAAGAATTGGCCCAATATTTGAAGAAATAA","protein_sequence":"MFTPIDQAIEHFKQNKFVIVMDDAGRENEGDLICAAENVSTEQMAFLVRHSSGYVCAPMTNAIADKLDLPLLRTGMKFESNDDDRHGTAYTITVDVAQGTTTGISAHDRSMTCRALADSSSTPKSFLKPGHICPLRAADGGVLQRRGHTEAGVDLCKLSGLSPVAVIGELVNDDEQGTMMRLNDCQAFGKKHGIPLISIEELAQYLKK"},{"created_at":"2011-05-27T05:24:20.000Z","updated_at":"2011-05-27T15:01:24.000Z","name":"Probable kynurenine formamidase","uniprot_id":"Q04066","uniprot_name":"BNA7_YEAST","enzyme":true,"transporter":false,"gene_name":"BNA7","num_residues":261,"molecular_weight":"29991.0","theoretical_pi":"4.98","general_function":"Involved in hydrolase activity","specific_function":"Catalyzes the hydrolysis of N-formyl-L-kynurenine to L- kynurenine, the second step in the conversion of tryptophan to nicotinic acid, NAD(H) and NADP(H)","reactions":[{"id":2770,"direction":"\u003e","locations":"Cytoplasmic","altext":"N-formyl-L-kynurenine + H(2)O = formate + L-kynurenine.","export":false,"pw_reaction_id":null,"source":null},{"id":4188,"direction":"\u003e","locations":null,"altext":null,"export":true,"pw_reaction_id":"PW_R006488","source":"Smpdb"}],"signal_regions":"None","transmembrane_regions":"None","pdb_id":"1VKH","cellular_location":"Cytoplasmic","genbank_gene_id":"U33007","genbank_protein_id":"927719","gene_card_id":"BNA7","chromosome_location":"chromosome 4","locus":"YDR428C","synonyms":["Biosynthesis of nicotinic acid protein 7","Probable N-formylkynurenine formamidase"],"enzyme_classes":["3.5.1.9"],"go_classes":[{"category":"Component","description":" Not Available"},{"category":"Function","description":" catalytic activity"},{"category":"Function","description":" hydrolase activity"},{"category":"Process","description":" metabolic process"}],"pfams":[{"name":"Abhydrolase_3","identifier":"PF07859"}],"pathways":[{"name":"Tryptophan metabolism","kegg_map_id":"00380"},{"name":"Glyoxylate and dicarboxylate metabolism","kegg_map_id":"00630"},{"name":"NAD 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cyclohydrolase 1","uniprot_id":"P51601","uniprot_name":"GCH1_YEAST","enzyme":true,"transporter":false,"gene_name":"FOL2","num_residues":243,"molecular_weight":"27768.80078","theoretical_pi":"7.25","general_function":"Involved in GTP cyclohydrolase I activity","specific_function":"GTP + H(2)O = formate + 2-amino-4-hydroxy-6- (erythro-1,2,3-trihydroxypropyl)-dihydropteridine triphosphate","reactions":[{"id":1616,"direction":"\u003e","locations":"cytoplasm","altext":null,"export":true,"pw_reaction_id":null,"source":null},{"id":2802,"direction":"\u003e","locations":"Cytoplasmic","altext":"GTP + H(2)O = formate + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)-dihydropteridine triphosphate.","export":false,"pw_reaction_id":null,"source":null},{"id":4140,"direction":"\u003e","locations":null,"altext":null,"export":true,"pw_reaction_id":"PW_R006439","source":"Smpdb"}],"signal_regions":"None","transmembrane_regions":"None","pdb_id":null,"cellular_location":"Cytoplasmic","genbank_gene_id":"AY692993","genbank_protein_id":"51013437","gene_card_id":"FOL2","chromosome_location":"chromosome 7","locus":"YGR267C","synonyms":["GTP cyclohydrolase I","GTP-CH-I"],"enzyme_classes":["3.5.4.16"],"go_classes":[{"category":"Component","description":" cell part"},{"category":"Component","description":" intracellular part"},{"category":"Component","description":" cytoplasm"},{"category":"Function","description":" hydrolase activity"},{"category":"Function","description":" hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds"},{"category":"Function","description":" hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amidines"},{"category":"Function","description":" cyclohydrolase activity"},{"category":"Function","description":" GTP cyclohydrolase activity"},{"category":"Function","description":" GTP cyclohydrolase I activity"},{"category":"Function","description":" catalytic activity"},{"category":"Process","description":" cellular aromatic compound metabolic process"},{"category":"Process","description":" folic acid and derivative metabolic process"},{"category":"Process","description":" folic acid and derivative biosynthetic process"},{"category":"Process","description":" tetrahydrofolate biosynthetic process"},{"category":"Process","description":" metabolic process"},{"category":"Process","description":" cellular metabolic process"}],"pfams":[{"name":"GTP_cyclohydroI","identifier":"PF01227"}],"pathways":[{"name":"Folate biosynthesis","kegg_map_id":"00790"},{"name":"tetrahydrofolate 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Nucleus","altext":"1,2-dihydroxy-5-(methylthio)pent-1-en-3-one + O(2) = 3-(methylthio)propanoate + formate + CO.","export":false,"pw_reaction_id":null,"source":null},{"id":3791,"direction":"\u003e","locations":null,"altext":null,"export":true,"pw_reaction_id":"PW_R006310","source":"Smpdb"}],"signal_regions":"None","transmembrane_regions":"None","pdb_id":null,"cellular_location":"Cell membrane; Peripheral membrane protein; Cytoplasmic side. Nucleus","genbank_gene_id":"AY558584","genbank_protein_id":"45271058","gene_card_id":"ADI1","chromosome_location":null,"locus":null,"synonyms":["Acireductone dioxygenase","ARD"],"enzyme_classes":[],"go_classes":[{"category":"Function","description":"oxidoreductase activity"},{"category":"Function","description":"dioxygenase activity"},{"category":"Function","description":"binding"},{"category":"Function","description":"ion binding"},{"category":"Function","description":"cation binding"},{"category":"Function","description":"metal ion binding"},{"category":"Function","description":"catalytic activity"},{"category":"Process","description":"oxidation reduction"},{"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":"amino acid salvage"},{"category":"Process","description":"L-methionine salvage from methylthioadenosine"},{"category":"Process","description":"metabolic process"}],"pfams":[{"name":"ARD","identifier":"PF03079"}],"pathways":[{"name":"Methionine metabolism and salvage","kegg_map_id":null}],"gene_sequence":"ATGGTTAAGGTATATATTCATGACAACAAGGTTGACTCCGATTATCGCGCACCCCACAATTCTGGAACAGAACTTTCCCTGGATGAATTAGCCAAGTTAGGAGTGATTTATAAATACTGTGCAAATGAGGAAGAAGTGAATGAAATTGCTAGGCAAAGAGAATATAAAAATAGAGATGTGGTCAACATCTGCGAAGGTTCCTTCAAAAGTGAAGCAGAGTTTAATGAAAAACTAGCAACATTCTACCAAGAGCATTTACATGAAGACGAAGAAATAAGATACTGTCTCGAGGGTGCTGGATACTTTGACGTCAGGGATGCTTCCACACCAGAGAACTGGATTAGGTGTTTGGTAGAGTCAGGTGATTTACTGATTCTTCCACCAGGCATCTATCATCGTTTCACCTTGACAACTAGCAACCACATCAAGGCCTTGAGACTGTTTAAGGACGAGCCCAAATGGCAAGCTATCAACAGGTCAAATCAGGCTGATTCATTGCCTGTACGCAAGGACTACATTGCCCTGATCAATCAGTACTAA","protein_sequence":"MVKVYIHDNKVDSDYRAPHNSGTELSLDELAKLGVIYKYCANEEEVNEIARQREYKNRDVVNICEGSFKSEAEFNEKLATFYQEHLHEDEEIRYCLEGAGYFDVRDASTPENWIRCLVESGDLLILPPGIYHRFTLTTSNHIKALRLFKDEPKWQAINRSNQADSLPVRKDYIALINQY"}]}