{"ymdb_id":"YMDB00516","created_at":"2011-05-29T18:25:41.000Z","updated_at":"2016-09-08T18:35:34.000Z","name":"5-Formyltetrahydrofolic acid","cas":"58-05-9","state":"Solid","melting_point":"245 oC","description":"5-Formyltetrahydrofolate (N5-Formyl-THF) is a folate coenzyme. Tetrahydrofolate (vitamin B9) and its derivatives, commonly termed folates, are essential cofactors that facilitate the transfer of one-carbon units from donor molecules into important biosynthetic pathways leading to methionine, purine, and pyrimidine biosynthesis. Folates also mediate the interconversion of serine and glycine, and play a role in histidine catabolism. Although 5-Formyl-tetrahydrofolate is the most stable derivative of the reduced folates, it is the only folate derivative that does not serve as a cofactor in C1-metabolism. [Biocyc PWY-2201] [PMID: 11923304]","experimental_water_solubility":null,"experimental_logp_hydrophobicity":null,"location":"Cytoplasm, Mitochondrion","synthesis_reference":null,"chebi_id":"15640","hmdb_id":"HMDB01562","kegg_id":"C03479","pubchem_id":"54575","cs_id":"131714","foodb_id":null,"wikipedia_link":"Folinate","biocyc_id":"5-FORMYL-THF","iupac":"(2S)-2-{[4-({[(6S)-2-amino-5-formyl-4-oxo-1,4,5,6,7,8-hexahydropteridin-6-yl]methyl}amino)phenyl]formamido}pentanedioic acid","traditional_iupac":"(2S)-2-{[4-({[(6S)-2-amino-5-formyl-4-oxo-1,6,7,8-tetrahydropteridin-6-yl]methyl}amino)phenyl]formamido}pentanedioic acid","logp":"-2.6744360693430935","pka":"4.2084919432830645","alogps_solubility":"3.00e-01 g/l","alogps_logp":"-1.06","alogps_logs":"-3.20","acceptor_count":"12","donor_count":"7","rotatable_bond_count":"9","polar_surface_area":"215.55","refractivity":"126.46200000000002","polarizability":"46.34154214681111","formal_charge":"0","physiological_charge":"-2","pka_strongest_basic":"2.807468599105256","pka_strongest_acidic":"3.4734158052231012","bioavailability":"0","number_of_rings":"3","rule_of_five":"0","ghose_filter":"0","veber_rule":"0","mddr_like_rule":"1","synonyms":["(6R,S)-5-Formyltetrahydrofolate","(6S)-5-formyltetrahydrofolate","(6S)-5-HCO-H4folate","[(6S)-5-formyl-5,6,7,8-tetrahydropteroyl]glutamate","10-Formyl-7,8-dihydrofolate","10-Formyl-7,8-dihydrofolic acid","5-Formyl-5,6,7,8-tetrahydrofolate","5-Formyl-5,6,7,8-tetrahydrofolic acid","5-Formyltetrahydrofolate","5-formyltetrahydrofolic acid","5-Formyltetrahydropteroylglutamate","5-Formyltetrahydropteroylglutamic acid","folinate","folinic acid","Folinic acid-SF","l-Leucovorin","l(-)-5-formyl-5,6,7,8-tetrahydrofolic acid","Leucal","Leucovorin","Levoleucovorin","N-(5-formyl-5,6,7,8-tetrahydropteroyl)-L-glutamic acid","N5-Formyl-5,6,7,8-tetrahydrofolate","N5-Formyl-5,6,7,8-tetrahydrofolic acid","N5-Formyltetrahydrofolate","N5-Formyltetrahydrofolic acid","Welcovorin"],"pathways":[{"name":"One carbon pool by folate","kegg_map_id":"00670"}],"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."}],"proteins":[{"created_at":"2011-05-27T01:31:06.000Z","updated_at":"2011-07-22T17:53:51.000Z","name":"5-formyltetrahydrofolate cyclo-ligase","uniprot_id":"P40099","uniprot_name":"FTHC_YEAST","enzyme":true,"transporter":false,"gene_name":"FAU1","num_residues":211,"molecular_weight":"24058.5","theoretical_pi":"7.14","general_function":"Involved in ATP binding","specific_function":"Utilizes 5-formyltetrahydrofolate (folinic acid) as substrate in an alternative way of folate biosynthesis","reactions":[{"id":1216,"direction":"\u003e","locations":"mitochondrion;cytoplasm","altext":null,"export":true,"pw_reaction_id":null,"source":null},{"id":2627,"direction":"\u003e","locations":"Mitochondrion","altext":"ATP + 5-formyltetrahydrofolate = ADP + phosphate + 5,10-methenyltetrahydrofolate.","export":false,"pw_reaction_id":null,"source":null}],"signal_regions":"None","transmembrane_regions":"None","pdb_id":null,"cellular_location":"Mitochondrion","genbank_gene_id":"U18922","genbank_protein_id":"603424","gene_card_id":"FAU1","chromosome_location":"chromosome 5","locus":"YER183C","synonyms":["5,10-methenyl-tetrahydrofolate synthetase","MTHFS","Methenyl-THF synthetase"],"enzyme_classes":["6.3.3.2"],"go_classes":[{"category":"Component","description":" Not Available"},{"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":" cyclo-ligase activity"},{"category":"Function","description":" catalytic activity"},{"category":"Function","description":" 5-formyltetrahydrofolate cyclo-ligase activity"},{"category":"Function","description":" ligase activity"},{"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":" folic acid and derivative biosynthetic process"},{"category":"Process","description":" metabolic process"}],"pfams":[{"name":"5-FTHF_cyc-lig","identifier":"PF01812"}],"pathways":[{"name":"One carbon pool by folate","kegg_map_id":"00670"}],"gene_sequence":"ATGGCCACTAAGCAATTACTGAGACGTCAAATCAAAAGGGTAATAAATGCTCTTGACTACGATATTATCGCTGCAGAGTCGCATACTATTTCTCAAGCAGTACGCTCATTGATCGCTTCCGCCAATTCTAGGCGTGTAGCGTGTTATATGAGCATGGATAAAGGAGAAGTAACGACTGGAGAAATCATTAAGAATTTATTTCAAGATGGCCAGGAGGTCTTTCTGCCAAGATGTACTCATACTTCTGAATCGAAACACTTCAAATTACGGGAAGATCATCATCCACATTTAATATTCCATCGAATGAGTAGTTTGAAAATGGTTCGTGATTTGAAGCCTCAAGGTCCATATCAACTAAAAGAGCCTGAACCGCATATTGAGGAATCAGATATTCTAGATGTCGTATTGGTGCCTGGAGTGGCGTTTGATATTAAAACTGGTGCAAGGATGGGTCACGGTGCTGGGTATTATGACGATTTTTTCCAACGGTATAAGATACTGCATGAAGGCCAAAAGCCCCTCCTAGTTGGACTATGTCTTATGGAACAGGTGGCCTCTCCAATTCCTTTAGAAAAACATGATTATTCCATGGATTGTATAGTATGCGGAGATGGATCCATACATTGGTTTCAATAA","protein_sequence":"MATKQLLRRQIKRVINALDYDIIAAESHTISQAVRSLIASANSRRVACYMSMDKGEVTTGEIIKNLFQDGQEVFLPRCTHTSESKHFKLREDHHPHLIFHRMSSLKMVRDLKPQGPYQLKEPEPHIEESDILDVVLVPGVAFDIKTGARMGHGAGYYDDFFQRYKILHEGQKPLLVGLCLMEQVASPIPLEKHDYSMDCIVCGDGSIHWFQ"},{"created_at":"2011-05-27T03:11:47.000Z","updated_at":"2011-05-27T15:01:19.000Z","name":"Pyruvate dehydrogenase E1 component subunit alpha, mitochondrial","uniprot_id":"P16387","uniprot_name":"ODPA_YEAST","enzyme":true,"transporter":false,"gene_name":"PDA1","num_residues":420,"molecular_weight":"46342.69922","theoretical_pi":"8.24","general_function":"Involved in oxidoreductase activity, acting on the aldehyde or oxo group of donors, disulfide as acceptor","specific_function":"The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2)","reactions":[{"id":2710,"direction":"\u003e","locations":"Mitochondrion matrix","altext":"Pyruvate + [dihydrolipoyllysine-residue acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine + CO(2).","export":false,"pw_reaction_id":null,"source":null}],"signal_regions":"None","transmembrane_regions":"None","pdb_id":null,"cellular_location":"Mitochondrion matrix","genbank_gene_id":"M29582","genbank_protein_id":"172108","gene_card_id":"PDA1","chromosome_location":"chromosome 5","locus":"YER178W","synonyms":["Pyruvate dehydrogenase complex component E1 alpha","PDHE1-A"],"enzyme_classes":["1.2.4.1"],"go_classes":[{"category":"Component","description":" organelle"},{"category":"Component","description":" membrane-bounded organelle"},{"category":"Component","description":" intracellular membrane-bounded organelle"},{"category":"Function","description":" oxidoreductase activity, acting on the aldehyde or oxo group of donors"},{"category":"Function","description":" oxidoreductase activity, acting on the aldehyde or oxo group of donors, disulfide as acceptor"},{"category":"Function","description":" catalytic activity"},{"category":"Function","description":" pyruvate dehydrogenase activity"},{"category":"Function","description":" pyruvate dehydrogenase (acetyl-transferring) activity"},{"category":"Function","description":" oxidoreductase activity"},{"category":"Process","description":" oxidation reduction"},{"category":"Process","description":" small molecule metabolic process"},{"category":"Process","description":" alcohol metabolic process"},{"category":"Process","description":" monosaccharide metabolic process"},{"category":"Process","description":" hexose metabolic process"},{"category":"Process","description":" glucose metabolic process"},{"category":"Process","description":" glucose catabolic process"},{"category":"Process","description":" glycolysis"},{"category":"Process","description":" metabolic process"}],"pfams":[{"name":"E1_dh","identifier":"PF00676"}],"pathways":[{"name":"Glycolysis / Gluconeogenesis","kegg_map_id":"00010"},{"name":"Citrate cycle (TCA cycle)","kegg_map_id":"00020"},{"name":"Valine, leucine and isoleucine biosynthesis","kegg_map_id":"00290"},{"name":"Pyruvate metabolism","kegg_map_id":"00620"},{"name":"Butanoate metabolism","kegg_map_id":"00650"}],"gene_sequence":"ATGCTTGCTGCTTCATTCAAACGCCAACCATCACAATTGGTCCGCGGGTTAGGAGCTGTTCTTCGCACTCCCACCAGGATAGGTCATGTTCGTACCATGGCAACTTTAAAAACAACTGATAAGAAGGCCCCTGAGGACATCGAGGGCTCGGACACAGTGCAAATTGAGTTGCCTGAATCTTCCTTCGAGTCGTATATGCTAGAGCCTCCAGACTTGTCTTATGAGAGTTCGAAAGCGACCTTGTTACAGATGTATAAAGATATGGTCATCATCAGAAGAATGGAGATGGCTTGTGACGCCTTGTACAAGGCCAAGAAAATCAGAGGTTTTTGCCATCTATCTGTTGGTCAGGAGGCCATTGCTGTCGGTATCGAGAATGCCATCACAAAATTGGATTCCATCATCACATCTTACAGATGTCACGGTTTCACTTTTATGAGAGGTGCCTCAGTGAAAGCCGTTCTGGCTGAATTAATGGGTAGAAGAGCCGGTGTCTCTTATGGTAAGGGTGGTTCCATGCACCTTTACGCTCCAGGCTTCTATGGTGGTAATGGTATCGTGGGTGCCCAGGTTCCTTTAGGTGCAGGTTTAGCTTTTGCTCACCAATACAAGAACGAGGACGCCTGCTCTTTCACTTTGTATGGTGATGGTGCCTCTAATCAAGGTCAAGTTTTTGAATCTTTCAACATGGCCAAATTATGGAATTTGCCGGTCGTGTTTTGCTGTGAGAACAACAAGTACGGTATGGGTACCGCCGCTTCAAGATCCTCCGCGATGACTGAATATTTCAAGCGTGGTCAATATATTCCAGGTTTAAAAGTTAACGGTATGGATATTCTAGCTGTCTACCAAGCATCCAAGTTTGCTAAGGACTGGTGTCTATCCGGCAAAGGTCCTCTCGTTCTAGAATATGAAACCTATAGGTACGGTGGCCATTCTATGTCTGATCCCGGTACTACCTACAGAACTAGAGACGAGATTCAGCATATGAGATCCAAGAACGATCCAATTGCTGGTCTTAAGATGCATTTGATTGATCTAGGTATTGCCACTGAAGCTGAAGTCAAAGCTTACGACAAGTCCGCTAGAAAATACGTTGACGAACAAGTTGAATTAGCTGATGCTGCTCCTCCTCCAGAAGCCAAATTATCCATCTTGTTTGAAGACGTCTACGTGAAAGGTACAGAAACTCCAACCCTAAGAGGTAGGATCCCTGAAGATACTTGGGACTTCAAAAAGCAAGGTTTTGCCTCTAGGGATTAA","protein_sequence":"MLAASFKRQPSQLVRGLGAVLRTPTRIGHVRTMATLKTTDKKAPEDIEGSDTVQIELPESSFESYMLEPPDLSYETSKATLLQMYKDMVIIRRMEMACDALYKAKKIRGFCHLSVGQEAIAVGIENAITKLDSIITSYRCHGFTFMRGASVKAVLAELMGRRAGVSYGKGGSMHLYAPGFYGGNGIVGAQVPLGAGLAFAHQYKNEDACSFTLYGDGASNQGQVFESFNMAKLWNLPVVFCCENNKYGMGTAASRSSAMTEYFKRGQYIPGLKVNGMDILAVYQASKFAKDWCLSGKGPLVLEYETYRYGGHSMSDPGTTYRTRDEIQHMRSKNDPIAGLKMHLIDLGIATEAEVKAYDKSARKYVDEQVELADAAPPPEAKLSILFEDVYVKGTETPTLRGRIPEDTWDFKKQGFASRD"}]}