{"ymdb_id":"YMDB00773","created_at":"2011-05-29T18:51:50.000Z","updated_at":"2016-09-08T18:35:53.000Z","name":"5,6,7,8-tetrahydrofolyl-L-glutamic acid","cas":null,"state":"Solid","melting_point":null,"description":"5,6,7,8-Tetrahydrofolyl-L-glutamic acid (THF-L-glutamate) is involved in the folate biosynthesis pathway. [KEGG]","experimental_water_solubility":null,"experimental_logp_hydrophobicity":null,"location":"cytoplasm","synthesis_reference":null,"chebi_id":"27650","hmdb_id":"HMDB06825","kegg_id":"C09332","pubchem_id":"442163","cs_id":"21864891","foodb_id":null,"wikipedia_link":null,"biocyc_id":null,"iupac":"(2S)-2-[(4S)-4-[(4-{[(2-amino-4-oxo-3,4,5,6,7,8-hexahydropteridin-6-yl)methyl]amino}phenyl)formamido]-4-carboxybutanamido]pentanedioic acid","traditional_iupac":"(2S)-2-[(4S)-4-[(4-{[(2-amino-4-oxo-5,6,7,8-tetrahydro-3H-pteridin-6-yl)methyl]amino}phenyl)formamido]-4-carboxybutanamido]pentanedioic acid","logp":"-4.290524407861601","pka":"3.519522535908951","alogps_solubility":"3.28e-01 g/l","alogps_logp":"-1.99","alogps_logs":"-3.24","acceptor_count":"14","donor_count":"10","rotatable_bond_count":"14","polar_surface_area":"273.67","refractivity":"149.67440000000002","polarizability":"57.43950903005329","formal_charge":"0","physiological_charge":"-3","pka_strongest_basic":"4.661484623798026","pka_strongest_acidic":"2.406415000414595","bioavailability":"0","number_of_rings":"3","rule_of_five":"0","ghose_filter":"0","veber_rule":"0","mddr_like_rule":"1","synonyms":["Tetrahydrofolyl-[Glu](2)","Tetrahydrofolyl-[Glu](n+1)","Tetrahydropteroyl-[gamma-Glu]n","Tetrahydropteroyl-[gamma-Glu]n+1","THF-L-glutamate","THF-L-glutamic acid","THF-polyglutamate"],"pathways":[{"name":"Folate biosynthesis","kegg_map_id":"00790"}],"growth_conditions":[],"references":[{"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":10799479,"citation":"Cherest, H., Thomas, D., Surdin-Kerjan, Y. (2000). \"Polyglutamylation of folate coenzymes is necessary for methionine biosynthesis and maintenance of intact mitochondrial genome in Saccharomyces cerevisiae.\" J Biol Chem 275:14056-14063."}],"proteins":[{"created_at":"2011-05-27T17:52:41.000Z","updated_at":"2011-05-29T05:06:52.000Z","name":"Folylpolyglutamate synthase","uniprot_id":"Q08645","uniprot_name":"FOLE_YEAST","enzyme":true,"transporter":false,"gene_name":"MET7","num_residues":548,"molecular_weight":"62150.89844","theoretical_pi":"9.24","general_function":"Coenzyme transport and metabolism","specific_function":"Conversion of folates to polyglutamate derivatives","reactions":[{"id":1996,"direction":"\u003c\u003e","locations":"cytoplasm","altext":null,"export":true,"pw_reaction_id":null,"source":null},{"id":2486,"direction":"\u003e","locations":"Cytoplasm;Mitochondrion. Cytoplasm;Mitochondrion","altext":"ATP + tetrahydropteroyl-(gamma-Glu)(n) + L-glutamate = ADP + phosphate + tetrahydropteroyl-(gamma-Glu)(n+1).","export":false,"pw_reaction_id":null,"source":null}],"signal_regions":"None","transmembrane_regions":"None","pdb_id":null,"cellular_location":"Mitochondrion. Cytoplasm","genbank_gene_id":"AY692818","genbank_protein_id":"51013087","gene_card_id":"MET7","chromosome_location":"chromosome 15","locus":"YOR241W","synonyms":["Folylpoly-gamma-glutamate synthetase","FPGS","Tetrahydrofolylpolyglutamate synthase","Tetrahydrofolate synthase"],"enzyme_classes":["6.3.2.17"],"go_classes":[{"category":"Component","description":" Not Available"},{"category":"Function","description":" ligase activity"},{"category":"Function","description":" ligase activity, forming carbon-nitrogen bonds"},{"category":"Function","description":" binding"},{"category":"Function","description":" nucleoside binding"},{"category":"Function","description":" purine nucleoside binding"},{"category":"Function","description":" adenyl nucleotide binding"},{"category":"Function","description":" adenyl ribonucleotide binding"},{"category":"Function","description":" ATP binding"},{"category":"Function","description":" acid-amino acid ligase activity"},{"category":"Function","description":" tetrahydrofolylpolyglutamate synthase activity"},{"category":"Function","description":" catalytic activity"},{"category":"Process","description":" biosynthetic process"},{"category":"Process","description":" cellular metabolic process"},{"category":"Process","description":" cellular aromatic compound metabolic process"},{"category":"Process","description":" folic acid and derivative metabolic process"},{"category":"Process","description":" metabolic process"},{"category":"Process","description":" folic acid and derivative biosynthetic process"}],"pfams":[],"pathways":[{"name":"Folate biosynthesis","kegg_map_id":"00790"}],"gene_sequence":"ATGCATAAAGGAAAAAAAAATTACCCTAATTTGATTACTTCGTTTCGGATGAATTTGAAAAAAATCATATTGAACCATGACCGATTTAGCCATCCAGAAAGATGGAAAACAAACGCACTCTTAAGGTTCACCTTCGTGTATATAAAATTTCTCTTCGACTTGATGATAATCAAAAATCCATTAAGGATGGTTGGAAAAACTTATCGAGACGCTGTTACTGCGCTAAACTCTTTGCAGTCCAATTATGCCAACATCATGGCTATCCGTCAAACTGGTGATCGTAAAAACACTATGACATTATTGGAAATGCATGAATGGTCTCGAAGAATTGGTTACTCTGCATCGGATTTCAATAAATTAAATATTGTTCATATCACTGGAACAAAAGGTAAAGGTTCTACTGCCGCATTTACTTCATCAATTCTAGGACAATATAAAGAACAATTACCACGTATCGGGCTATATACGTCTCCACATCTTAAGTCAGTGAGAGAAAGAATAAGAATAAATGGGGAGCCAATTTCTGAAGAAAAATTTGCGAAGTACTTCTTTGAGGTTTGGGACCGTCTAGATAGTACAACCTCTTCTTTGGATAAATTCCCGCACATGATCCCGGGAAGTAAGCCTGGCTATTTCAAGTTCCTCACATTGCTTTCATTTCACACTTTTATACAAGAGGACTGCAAAAGCTGTGTCTACGAAGTCGGCGTCGGAGGTGAATTGGATAGCACTAATATAATTGAAAAGCCAATTGTCTGCGGTGTTACACTATTAGGAATAGACCATACTTTCATGCTTGGTGATACTATTGAAGAAATTGCTTGGAATAAGGGAGGAATTTTCAAATCTGGAGCACCAGCATTCACCGTTGAGAAACAACCTCCTCAGGGATTAACAATATTGAAAGAAAGAGCTGAGGAGCGCAAAACAACGCTAACAGAAGTACCCCCATTTAAACAGTTGGAAAATGTCAAGCTTGGAATTGCTGGCGAGTTTCAAAAAAGTAACGCCTCCCTTGCCGTTATGCTGGCTTCTGAGATCTTGCATACGTCCAATATATTGGAGGAGAAGATCAAATGCAGTTCGAATGCATCGATTCCAGAAAAATTCATAATCGGTCTACAAAATACTAAGTGGGAAGGCAGATGTCAAGTACTAGAAAAGGGAAAAAACGTTTGGTACATTGATGGTGCTCACACCAAAGATAGTATGGTAGCTGCATCAACATGGTTCAGAGATATGGTTCGATTGTCGAAGAGAAAGAAGATCTTGCTCTTCAACCAACAAAGCAGAGATGCCAACGCTCTTGTGAATAACCTGTACTCATCTGTTTCGCCAGAAATAACGTTCGATGATGTGATATTTACTACTAATGTCACTTGGAAATCAGGCTCATACAGCGCTGACCTCGTTTCCATGAACACTTCTCAAGAAGATGTAGAAAAATTGAAAGTCCAGGAGTCATTAGTCAAGAATTGGAACAAAATAGACGATAATCGTGCTAAAACGCATGTAACGGCTAGTATAGAGGAAGCAAATGAATTGATTGAAACGCTATACGATGAACCTGCTGATATATTTGTAACTGGTTCATTACATCTTGTTGGCGGATTATTGGTCGTTTTTGATAGAATAGATGTAAAGTAA","protein_sequence":"MHKGKKNYPNLITSFRMNLKKIILNHDRFSHPERWKTNALLRFTFVYIKFLFDLMIIKNPLRMVGKTYRDAVTALNSLQSNYANIMAIRQTGDRKNTMTLLEMHEWSRRIGYSASDFNKLNIVHITGTKGKGSTAAFTSSILGQYKEQLPRIGLYTSPHLKSVRERIRINGEPISEEKFAKYFFEVWDRLDSTTSSLDKFPHMIPGSKPGYFKFLTLLSFHTFIQEDCKSCVYEVGVGGELDSTNIIEKPIVCGVTLLGIDHTFMLGDTIEEIAWNKGGIFKSGAPAFTVEKQPPQGLTILKERAEERKTTLTEVPPFKQLENVKLGIAGEFQKSNASLAVMLASEILHTSNILEEKIKCSSNASIPEKFIIGLQNTKWEGRCQVLEKGKNVWYIDGAHTKDSMVAASTWFRDMVRLSKRKKILLFNQQSRDANALVNNLYSSVSPEITFDDVIFTTNVTWKSGSYSADLVSMNTSQEDVEKLKVQESLVKNWNKIDDNRAKTHVTASIEEANELIETLYDEPADIFVTGSLHLVGGLLVVFDRIDVK"}]}