{"ymdb_id":"YMDB00493","created_at":"2011-05-29T18:23:21.000Z","updated_at":"2016-09-08T18:35:32.000Z","name":"4-Aminobenzoic acid","cas":"150-13-0","state":"Solid","melting_point":"188.5 oC","description":"4-Aminobenzoic acid (p-aminobenzoate) is a precursor in the tetrahydrofolate biosynthesis pathway; it is synthetised from chorismate. Tetrahydrofolate (vitamin B9) is the parent structure of the large family of folates coenzymes. 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. [Biocyc PWY-6543 and PWY-6614]","experimental_water_solubility":"6.11 mg/mL at 30 oC [YALKOWSKY,SH \u0026 HE,Y (2003)]","experimental_logp_hydrophobicity":"0.83 [HANSCH,C ET AL. (1995)]","location":"Cytoplasm, Extracellular, Mitochondrion","synthesis_reference":"Sato, Ryu; Kimura, Koichi; Takahashi, Akira.  Preparation of p-aminobenzoic acid from styrene polymers.    Jpn. Kokai Tokkyo Koho  (2007),     13pp.","chebi_id":"30753","hmdb_id":"HMDB01392","kegg_id":"C00568","pubchem_id":"978","cs_id":"953","foodb_id":null,"wikipedia_link":"4-Aminobenzoic_acid","biocyc_id":"P-AMINO-BENZOATE","iupac":"4-aminobenzoic acid","traditional_iupac":"sunbrella","logp":"0.8019027699999998","pka":null,"alogps_solubility":"4.41e+00 g/l","alogps_logp":"0.78","alogps_logs":"-1.49","acceptor_count":"3","donor_count":"2","rotatable_bond_count":"1","polar_surface_area":"63.32","refractivity":"38.0146","polarizability":"13.44348919384024","formal_charge":"0","physiological_charge":"-1","pka_strongest_basic":"2.6912772144052126","pka_strongest_acidic":"4.769893805764377","bioavailability":"1","number_of_rings":"1","rule_of_five":"1","ghose_filter":"0","veber_rule":"0","mddr_like_rule":"0","synonyms":["1-Amino-4-carboxybenzene","4-Amino-benzoic acid","4-Aminobenzoate","4-Aminobenzoesaeure","4-Aminobenzoic acid","4-aminobenzoic acid, ion(1-)","4-Carboxyaniline","4-Carboxyphenylamine","ABEE","acido p-aminobenzoico","acidum paraminobenzoicum","Actipol","Amben","Aminobenzoate","Aminobenzoic acid","Aminobenzoic acid, para","Aniline-4-carboxylate","Aniline-4-carboxylic acid","Anti-Chromotrichia factor","Anticanitic vitamin","Anticantic vitamin","Antichromotrichia factor","Bacterial vitamin H1","Benzoic acid, 4-amino-","Benzoic acid, p-amino-","Chromotrichia factor","gamma-Aminobenzoate","gamma-Aminobenzoic acid","Hachemina","Kyselina p-aminobenzoova","p-amino-Benzoate","p-amino-Benzoic acid","p-Aminobenzoate","p-Aminobenzoesaeure","p-Aminobenzoic acid","p-Carboxyaniline","p-Carboxyphenylamine","PAB","PABA","Pabacyd","Pabafilm","Pabagel","Pabamine","Pabanol","Papacidum","para-aminobenzoate","para-Aminobenzoic acid","Paraminol","Paranate","Potaba","Romavit","Rvpaba","RVPaba Lipstick","Sunbrella","Super Shade by Coppertone","Trichochromogenic factor","Trochromogenic factor","Vitamin BX","Vitamin H'"],"pathways":[{"name":"Folate biosynthesis","kegg_map_id":"00790"},{"name":"tetrahydrofolate 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."}],"proteins":[{"created_at":"2011-05-29T04:30:10.000Z","updated_at":"2011-07-22T17:54:37.000Z","name":"Folic acid synthesis protein FOL1","uniprot_id":"P53848","uniprot_name":"FOL1_YEAST","enzyme":true,"transporter":false,"gene_name":"FOL1","num_residues":824,"molecular_weight":"93119.10156","theoretical_pi":"6.4","general_function":"Involved in dihydropteroate synthase activity","specific_function":"Catalyzes three sequential steps of tetrahydrofolate biosynthesis","reactions":[{"id":1140,"direction":"\u003e","locations":"mitochondrion","altext":null,"export":true,"pw_reaction_id":null,"source":null},{"id":1457,"direction":"\u003e","locations":"mitochondrion","altext":null,"export":true,"pw_reaction_id":null,"source":null},{"id":1461,"direction":"\u003e","locations":"mitochondrion","altext":null,"export":true,"pw_reaction_id":null,"source":null},{"id":1462,"direction":"\u003e","locations":"mitochondrion","altext":null,"export":true,"pw_reaction_id":null,"source":null},{"id":2843,"direction":"\u003e","locations":"Mitochondrion membrane","altext":"2-amino-4-hydroxy-6-(D-erythro-1,2,3-trihydroxypropyl)-7,8-dihydropteridine = 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine + glycolaldehyde.","export":false,"pw_reaction_id":null,"source":null},{"id":2844,"direction":"\u003e","locations":"Mitochondrion membrane","altext":"ATP + 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine = AMP + (2-amino-4-hydroxy-7,8-dihydropteridin-6-yl)methyl diphosphate.","export":false,"pw_reaction_id":null,"source":null},{"id":2845,"direction":"\u003e","locations":"Mitochondrion membrane","altext":"(2-amino-4-hydroxy-7,8-dihydropteridin-6-yl)methyl diphosphate + 4-aminobenzoate = diphosphate + dihydropteroate.","export":false,"pw_reaction_id":null,"source":null},{"id":4141,"direction":"\u003e","locations":null,"altext":null,"export":true,"pw_reaction_id":"PW_R006442","source":"Smpdb"},{"id":4142,"direction":"\u003e","locations":null,"altext":null,"export":true,"pw_reaction_id":"PW_R006443","source":"Smpdb"},{"id":4143,"direction":"\u003e","locations":null,"altext":null,"export":true,"pw_reaction_id":"PW_R006444","source":"Smpdb"}],"signal_regions":"None","transmembrane_regions":"None","pdb_id":null,"cellular_location":"Mitochondrion membrane","genbank_gene_id":null,"genbank_protein_id":null,"gene_card_id":"FOL1","chromosome_location":"chromosome 14","locus":"YNL256W","synonyms":["Dihydroneopterin aldolase","DHNA","FASA","FASB","2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase","6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase","PPPK","7,8-dihydro-6-hydroxymethylpterin-pyrophosphokinase","HPPK","FASC","Dihydropteroate synthase","DHPS","Dihydropteroate pyrophosphorylase","FASD"],"enzyme_classes":["4.1.2.25","2.7.6.3","2.5.1.15"],"go_classes":[{"category":"Component","description":" Not Available"},{"category":"Function","description":" transferase activity, transferring phosphorus-containing groups"},{"category":"Function","description":" lyase activity"},{"category":"Function","description":" carbon-carbon lyase activity"},{"category":"Function","description":" transferase activity, transferring alkyl or aryl (other than methyl) groups"},{"category":"Function","description":" diphosphotransferase activity"},{"category":"Function","description":" 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase activity"},{"category":"Function","description":" aldehyde-lyase activity"},{"category":"Function","description":" dihydroneopterin aldolase activity"},{"category":"Function","description":" catalytic activity"},{"category":"Function","description":" dihydropteroate synthase activity"},{"category":"Function","description":" transferase 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":" pteridine and derivative metabolic process"},{"category":"Process","description":" metabolic process"},{"category":"Process","description":" tetrahydrofolate biosynthetic process"}],"pfams":[{"name":"FolB","identifier":"PF02152"},{"name":"HPPK","identifier":"PF01288"},{"name":"Pterin_bind","identifier":"PF00809"}],"pathways":[{"name":"Folate biosynthesis","kegg_map_id":"00790"},{"name":"tetrahydrofolate biosynthesis","kegg_map_id":null}],"gene_sequence":"ATGTCAAAGCTATTTTCTACTGTCAATTCTGCAAGACATAGTGTACCACTAGGCGGCATGAGAGATTATGTGCACATTAAGAAACTAGAGATGAATACAGTTCTTGGGCCTGATTCCTGGAATCAATTAATGCCTCAGAAATGTCTACTAAGCTTAGATATGGGTACAGATTTTAGTAAATCTGCGGCTACGGATGATTTGAAATATTCTCTAAATTATGCAGTTATTTCTCGTGATTTGACGAATTTCGTCAGCAAAAAAAAGAATTGGGGTTCTGTTTCTAATTTGGCTAAATCTGTGTCTCAATTTGTTATGGACAAATATTCTGGTGTCGAGTGTCTGAATTTAGAAGTGCAGGCGGATACAACGCATATTAGAAGTGACCACATATCTTGTATTATTCAACAAGAAAGAGGGAATCCAGAATCACAGGAATTTGACGTTGTTAGGATATCTGAGTTAAAAATGTTGACTTTGATTGGTGTTTTCACCTTTGAGAGACTTAAGAAACAGTATGTAACTTTGGATATAAAGTTGCCTTGGCCAAAGAAAGCCGAATTGCCACCGCCAGTGCAAAGCATAATTGATAACGTTGTCAAGTTTGTGGAGGAATCAAATTTCAAGACTGTGGAAGCTCTTGTAGAATCTGTGTCAGCTGTTATTGCCCATAACGAGTATTTTCAAAAGTTTCCAGATTCGCCTTTGGTGGTGAAGGTTTTGAAATTAAACGCAATCACAGCCACAGAAGGTGTTGGTGTAAGCTGTATTAGAGAGCCCAGGGAGATTGCGATGGTAAATATTCCATATCTTTCCTCCATACATGAATCGTCTGATATTAAGTTCCAATTGTCTTCATCACAAAACACTCCTATTGAGGGTAAAAATACATGGAAAAGAGCGTTTTTAGCGTTTGGTTCAAACATTGGGGACCGTTTCAAACACATTCAAATGGCGTTGCAATTATTATCAAGGGAAAAAACGGTTAAATTACGGAATATTTCGTCTATTTTTGAAAGTGAACCAATGTATTTCAAAGATCAAACCCCTTTCATGAATGGGTGTGTTGAGGTGGAGACATTACTGACCCCAAGCGAATTATTAAAATTGTGTAAAAAAATTGAATATGAAGAGTTGCAAAGAGTCAAGCATTTTGATAATGGTCCGAGAACAATAGATCTGGATATTGTTATGTTTTTGAATAGCGCCGGAGAAGATATTATAGTAAATGAACCGGATTTGAATATACCGCATCCTAGAATGCTGGAGAGGACTTTCGTTCTTGAGCCGTTATGTGAATTAATATCCCCCGTTCACCTTCATCCTGTGACAGCGGAACCCATTGTAGACCATTTAAAACAGTTATACGACAAACAGCATGATGAAGATACCTTATGGAAATTAGTTCCATTGCCTTATCGTAGTGGTGTGGAGCCTAGATTTTTGAAATTCAAGACCGCTACAAAACTTGACGAATTTACTGGAGAAACAAACAGAATTACTGTTTCACCTACATATATCATGGCTATCTTCAACGCTACACCAGATTCATTTTCCGATGGAGGTGAGCATTTTGCGGACATTGAAAGTCAATTGAATGATATCATTAAATTGTGTAAAGACGCATTATATTTGCATGAGAGCGTCATCATCGACGTTGGAGGGTGTTCTACCAGGCCTAACTCTATTCAGGCGTCTGAGGAAGAAGAAATACGCAGGTCTATCCCATTAATTAAGGCCATTAGAGAAAGCACTGAGTTACCGCAAGATAAAGTCATACTATCCATTGATACTTATCGTTCCAATGTCGCTAAAGAAGCGATTAAAGTTGGAGTGGATATTATTAATGATATTTCGGGAGGTTTATTTGACAGCAACATGTTTGCCGTAATTGCAGAGAACCCAGAAATTTGTTATATTTTATCACACACACGTGGTGATATTTCAACGATGAATAGGCTGGCGCATTACGAAAATTTTGCATTGGGTGATTCTATTCAGCAAGAATTTGTTCATAATACCGACATTCAGCAGCTAGACGACTTGAAAGACAAAACAGTGTTAATCAGGAATGTTGGTCAAGAAATTGGCGAAAGGTATATCAAAGCGATTGATAATGGAGTAAAGCGCTGGCAAATTCTAATCGACCCTGGACTTGGTTTTGCTAAGACCTGGAAGCAAAACTTACAAATTATTAGACATATCCCCATTTTAAAGAACTACTCATTCACCATGAACTCAAACAATTCGCAAGTGTATGTTAACCTCAGAAATATGCCCGTTTTATTGGGTCCATCGCGCAAAAAATTCATTGGACATATCACAAAAGATGTGGATGCGAAGCAAAGAGACTTTGCTACTGGAGCGGTGGTAGCGTCGTGTATTGGTTTCGGCAGCGACATGGTTAGGGTCCATGACGTTAAAAATTGTTCGAAGAGCATTAAATTAGCAGATGCTATTTATAAAGGTTTGGAATAA","protein_sequence":"MSKLFSTVNSARHSVPLGGMRDYVHIKKLEMNTVLGPDSWNQLMPQKCLLSLDMGTDFSKSAATDDLKYSLNYAVISRDLTNFVSKKKNWGSVSNLAKSVSQFVMDKYSGVECLNLEVQADTTHIRSDHISCIIQQERGNPESQEFDVVRISELKMLTLIGVFTFERLKKQYVTLDIKLPWPKKAELPPPVQSIIDNVVKFVEESNFKTVEALVESVSAVIAHNEYFQKFPDSPLVVKVLKLNAITATEGVGVSCIREPREIAMVNIPYLSSIHESSDIKFQLSSSQNTPIEGKNTWKRAFLAFGSNIGDRFKHIQMALQLLSREKTVKLRNISSIFESEPMYFKDQTPFMNGCVEVETLLTPSELLKLCKKIEYEELQRVKHFDNGPRTIDLDIVMFLNSAGEDIIVNEPDLNIPHPRMLERTFVLEPLCELISPVHLHPVTAEPIVDHLKQLYDKQHDEDTLWKLVPLPYRSGVEPRFLKFKTATKLDEFTGETNRITVSPTYIMAIFNATPDSFSDGGEHFADIESQLNDIIKLCKDALYLHESVIIDVGGCSTRPNSIQASEEEEIRRSIPLIKAIRESTELPQDKVILSIDTYRSNVAKEAIKVGVDIINDISGGLFDSNMFAVIAENPEICYILSHTRGDISTMNRLAHYENFALGDSIQQEFVHNTDIQQLDDLKDKTVLIRNVGQEIGERYIKAIDNGVKRWQILIDPGLGFAKTWKQNLQIIRHIPILKNYSFTMNSNNSQVYVNLRNMPVLLGPSRKKFIGHITKDVDAKQRDFATGAVVASCIGFGSDMVRVHDVKNCSKSIKLADAIYKGLE"},{"created_at":"2011-05-29T04:45:54.000Z","updated_at":"2011-07-22T17:53:48.000Z","name":"Aminodeoxychorismate lyase","uniprot_id":"Q03266","uniprot_name":"PABC_YEAST","enzyme":true,"transporter":false,"gene_name":"ABZ2","num_residues":374,"molecular_weight":"42639.39844","theoretical_pi":"5.53","general_function":"Involved in catalytic activity","specific_function":"Converts 4-amino-4-deoxychorismate into 4-aminobenzoate (PABA) and pyruvate","reactions":[{"id":1191,"direction":"\u003e","locations":"cytoplasm","altext":null,"export":true,"pw_reaction_id":null,"source":null},{"id":2848,"direction":"\u003e","locations":"Cytoplasm","altext":"4-amino-4-deoxychorismate = 4-aminobenzoate + pyruvate.","export":false,"pw_reaction_id":null,"source":null},{"id":4144,"direction":"\u003e","locations":null,"altext":null,"export":true,"pw_reaction_id":"PW_R006445","source":"Smpdb"}],"signal_regions":"None","transmembrane_regions":"None","pdb_id":null,"cellular_location":"Cytoplasm","genbank_gene_id":null,"genbank_protein_id":null,"gene_card_id":"ABZ2","chromosome_location":"chromosome 13","locus":"YMR289W","synonyms":["4-amino-4-deoxychorismate lyase","ADC lyase","ADCL"],"enzyme_classes":["4.1.3.38"],"go_classes":[{"category":"Component","description":" Not Available"},{"category":"Function","description":" catalytic activity"},{"category":"Process","description":" metabolic process"}],"pfams":[{"name":"Aminotran_4","identifier":"PF01063"}],"pathways":[{"name":"Folate biosynthesis","kegg_map_id":"00790"},{"name":"tetrahydrofolate biosynthesis","kegg_map_id":null}],"gene_sequence":"ATGTCACTAATGGACAATTGGAAGACTGATATGGAAAGTTACGATGAAGGAGGCCTAGTTGCTAATCCGAACTTCGAGGTTCTGGCCACTTTCAGGTACGACCCTGGTTTTGCACGCCAGTCAGCGTCAAAGAAAGAGATCTTTGAAACTCCAGACCCTCGATTAGGTTTGAGAGACGAAGATATTAGGCAGCAGATAATTAATGAGGATTACTCAAGTTATTTACGAGTAAGGGAGGTTAATTCCGGCGGTGACCTTCTCGAAAATATTCAGCATCCTGATGCTTGGAAGCATGATTGCAAGACCATTGTGTGCCAGCGTGTAGAAGATATGCTACAAGTCATTTATGAACGATTTTTTTTATTAGATGAACAATACCAAAGAATAAGAATAGCATTATCATACTTTAAAATTGACTTCAGCACGTCTCTGAATGATTTATTGAAGTTATTGGTTGAAAACTTGATTAATTGTAAAGAAGGAAATTCAGAGTATCACGAAAAAATTCAAAAAATGATCAACGAAAGGCAATGCTATAAAATGCGGGTACTTGTCTCTAAGACAGGAGATATACGAATTGAGGCAATTCCAATGCCTATGGAGCCTATCCTAAAATTAACAACCGATTATGACAGTGTTTCCACATACTTCATCAAAACGATGCTCAATGGATTTTTAATTGATAGCACAATAAATTGGGATGTTGTTGTTTCATCTGAACCATTGAACGCATCAGCTTTCACCAGTTTTAAAACCACTTCAAGAGATCATTACGCTAGGGCGAGAGTTCGCATGCAAACTGCTATAAATAACTTAAGAGGTTCAGAACCTACTTCTTCTGTCTCGCAATGCGAAATTTTATTTTCCAACAAATCTGGCCTGCTGATGGAAGGTTCAATAACAAACGTGGCTGTAATTCAAAAAGATCCTAACGGTTCTAAAAAGTATGTGACACCAAGATTAGCAACTGGATGTTTGTGCGGAACAATGCGTCATTATTTATTGCGGCTCGGCCTTATTGAAGAGGGAGATATAGATATAGGAAGCCTTACCGTTGGCAACGAAGTTTTGCTTTTCAATGGCGTCATGGGATGCATAAAGGGAACAGTGAAGACAAAATATTGA","protein_sequence":"MSLMDNWKTDMESYDEGGLVANPNFEVLATFRYDPGFARQSASKKEIFETPDPRLGLRDEDIRQQIINEDYSSYLRVREVNSGGDLLENIQHPDAWKHDCKTIVCQRVEDMLQVIYERFFLLDEQYQRIRIALSYFKIDFSTSLNDLLKLLVENLINCKEGNSEYHEKIQKMINERQCYKMRVLVSKTGDIRIEAIPMPMEPILKLTTDYDSVSTYFIKTMLNGFLIDSTINWDVVVSSEPLNASAFTSFKTTSRDHYARARVRMQTAINNLRGSEPTSSVSQCEILFSNKSGLLMEGSITNVAVIQKDPNGSKKYVTPRLATGCLCGTMRHYLLRLGLIEEGDIDIGSLTVGNEVLLFNGVMGCIKGTVKTKY"}]}