{"ymdb_id":"YMDB00120","created_at":"2011-05-29T15:58:54.000Z","updated_at":"2016-09-08T18:35:03.000Z","name":"Phosphoadenosine phosphosulfate","cas":"485-84-7","state":"Solid","melting_point":"","description":"Phosphoadenosine phosphosulfate is a key intermediate in the formation of sulfate esters of phenols, alcohols, steroids, sulfated polysaccharides, and simple esters, such as choline sulfate. It is an important step in the process of sulfur fixation in plants and microorganisms.","experimental_water_solubility":"","experimental_logp_hydrophobicity":"","location":"cytoplasm","synthesis_reference":"Lin, Chun-Hung; Shen, Gwo-Jenn; Garcia-Junceda, Eduardo; Wong, Chi-Huey. Enzymic Synthesis and Regeneration of 3'-Phosphoadenosine 5'-Phosphosulfate (PAPS) for Regioselective Sulfation of Oligosaccharides. Journal of the American Chemical Society (1995), ","chebi_id":"17709","hmdb_id":"HMDB01003","kegg_id":"C00053","pubchem_id":"990","cs_id":"9799","foodb_id":null,"wikipedia_link":"amps","biocyc_id":"APS","iupac":"[({[(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-4-hydroxy-3-(phosphonooxy)oxolan-2-yl]methoxy}(hydroxy)phosphoryl)oxy]sulfonic acid","traditional_iupac":"3'-phosphoadenylyl sulfate","logp":"-5.7470361976147775","pka":"0.8553623074051853","alogps_solubility":"5.05e+00 g/l","alogps_logp":"-0.65","alogps_logs":"-2.00","acceptor_count":"14","donor_count":"6","rotatable_bond_count":"8","polar_surface_area":"275.96999999999997","refractivity":"94.93319999999999","polarizability":"39.26356277423854","formal_charge":"0","physiological_charge":"-4","pka_strongest_basic":"3.938960906987655","pka_strongest_acidic":"-2.358629323070134","bioavailability":"0","number_of_rings":"3","rule_of_five":"0","ghose_filter":"0","veber_rule":"0","mddr_like_rule":"1","synonyms":["3'-Phospho-5'-adenylyl sulfate","3'-Phosphoadenosine 5'-phosphosulfate","3'-phosphoadenosine-5'-phosphosulfate","3'-Phosphoadenylyl sulfate","3'-phosphoadenylyl-sulfate","5-phosphoadenosine 3-phosphosulfate","PAPS","Phosphoadenosine Phosphosulfate","Phosphoadenosine phosphosulfic acid"],"pathways":[{"name":"Purine metabolism","kegg_map_id":"00230"},{"name":"Sulfur metabolism","kegg_map_id":"00920"}],"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":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":3060034,"citation":"Schwenn, J. D., Krone, F. A., Husmann, K. (1988). \"Yeast PAPS reductase: properties and requirements of the purified enzyme.\" Arch Microbiol 150:313-319."},{"pubmed_id":2203779,"citation":"Thomas, D., Barbey, R., Surdin-Kerjan, Y. (1990). \"Gene-enzyme relationship in the sulfate assimilation pathway of Saccharomyces cerevisiae. Study of the 3'-phosphoadenylylsulfate reductase structural gene.\" J Biol Chem 265:15518-15524."},{"pubmed_id":1654509,"citation":"Korch, C., Mountain, H. A., Bystrom, A. S. (1991). \"Cloning, nucleotide sequence, and regulation of MET14, the gene encoding the APS kinase of Saccharomyces cerevisiae.\" Mol Gen Genet 229:96-108."},{"pubmed_id":19889834,"citation":"Boer, V. M., Crutchfield, C. A., Bradley, P. H., Botstein, D., Rabinowitz, J. D. (2010). \"Growth-limiting intracellular metabolites in yeast growing under diverse nutrient limitations.\" Mol Biol Cell 21:198-211."}],"proteins":[{"created_at":"2011-05-26T20:15:50.000Z","updated_at":"2011-07-22T17:54:01.000Z","name":"Adenylyl-sulfate kinase","uniprot_id":"Q02196","uniprot_name":"KAPS_YEAST","enzyme":true,"transporter":false,"gene_name":"MET14","num_residues":202,"molecular_weight":"23060.09961","theoretical_pi":"8.31","general_function":"Involved in ATP binding","specific_function":"Catalyzes the synthesis of activated sulfate","reactions":[{"id":1282,"direction":"\u003e","locations":"cytoplasm","altext":null,"export":true,"pw_reaction_id":null,"source":null},{"id":2591,"direction":"\u003e","locations":null,"altext":"ATP + adenylyl sulfate = ADP + 3'-phosphoadenylyl sulfate.","export":false,"pw_reaction_id":null,"source":null},{"id":14417,"direction":"\u003e","locations":null,"altext":null,"export":true,"pw_reaction_id":"PW_R006930","source":"Smpdb"}],"signal_regions":"None","transmembrane_regions":"None","pdb_id":null,"cellular_location":null,"genbank_gene_id":"AY558261","genbank_protein_id":"45270412","gene_card_id":"MET14","chromosome_location":"chromosome 11","locus":"YKL001C","synonyms":["ATP adenosine-5'-phosphosulfate 3'-phosphotransferase","Adenosine-5'-phosphosulfate kinase","APS kinase"],"enzyme_classes":["2.7.1.25"],"go_classes":[{"category":"Component","description":" Not Available"},{"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":" kinase activity"},{"category":"Function","description":" catalytic activity"},{"category":"Function","description":" transferase activity"},{"category":"Function","description":" transferase activity, transferring phosphorus-containing groups"},{"category":"Function","description":" binding"},{"category":"Process","description":" sulfur metabolic process"},{"category":"Process","description":" sulfate assimilation"},{"category":"Process","description":" metabolic process"},{"category":"Process","description":" cellular metabolic process"}],"pfams":[{"name":"APS_kinase","identifier":"PF01583"}],"pathways":[{"name":"Purine metabolism","kegg_map_id":"00230"},{"name":"Selenocompound metabolism","kegg_map_id":"00450"},{"name":"Sulfur metabolism","kegg_map_id":"00920"}],"gene_sequence":"ATGGCTACTAATATTACTTGGCATCCAAATCTTACTTACGACGAACGCAAGGCATTGAGAAAACAGGACGGTTGTACTATTTGGTTAACAGGTCTAAGTGCGTCAGGTAAAAGTACAATCGCCTGTGCGCTAGAACAGTTACTGCTCCAAAAAAACTTGTCTGCATATAGATTGGATGGTGACAACATTCGTTTTGGATTGAACAAGGATTTGGGTTTCTCAGAAAAGGACAGAAATGAAAACATTCGTAGAATTAGCGAAGTTTCTAAGCTATTTGCTGATTCATGTGCTATTTCAATCACCTCATTTATCTCTCCATACAGAGTTGACAGAGATAGAGCTCGTGAACTACATAAGGAGGCTGGTTTGAAGTTCATTGAAATATTTGTTGATGTTCCATTAGAAGTCGCTGAGCAAAGGGACCCTAAGGGTTTATACAAGAAAGCTAGGGAGGGTGTAATCAAGGAGTTTACAGGTATTTCTGCCCCATATGAAGCGCCAAAAGCTCCAGAGCTACATTTGAGAACCGACCAGAAGACGGTTGAAGAATGTGCTACCATTATTTATGAGTACTTAATCAGTGAAAAAATCATCCGTAAGCATTTGTAA","protein_sequence":"MATNITWHPNLTYDERKALRKQDGCTIWLTGLSASGKSTIACALEQLLLQKNLSAYRLDGDNIRFGLNKDLGFSEKDRNENIRRISEVSKLFADSCAISITSFISPYRVDRDRARELHKEAGLKFIEIFVDVPLEVAEQRDPKGLYKKAREGVIKEFTGISAPYEAPKAPELHLRTDQKTVEECATIIYEYLISEKIIRKHL"},{"created_at":"2011-05-27T02:04:30.000Z","updated_at":"2011-05-27T15:01:16.000Z","name":"Phosphoadenosine phosphosulfate reductase","uniprot_id":"P18408","uniprot_name":"MET16_YEAST","enzyme":true,"transporter":false,"gene_name":"MET16","num_residues":261,"molecular_weight":"30380.09961","theoretical_pi":"5.8","general_function":"Involved in phosphoadenylyl-sulfate reductase (thioredoxin) activity","specific_function":"The NADP dependent reduction of PAPS into sulfite involves thioredoxin which probably plays the role of a thiol carrier","reactions":[{"id":2658,"direction":"\u003e","locations":null,"altext":"Adenosine 3',5'-bisphosphate + sulfite + thioredoxin disulfide = 3'-phosphoadenylyl sulfate + thioredoxin.","export":false,"pw_reaction_id":null,"source":null},{"id":14419,"direction":"\u003e","locations":null,"altext":null,"export":true,"pw_reaction_id":"PW_R006932","source":"Smpdb"}],"signal_regions":"None","transmembrane_regions":"None","pdb_id":null,"cellular_location":null,"genbank_gene_id":"AY693236","genbank_protein_id":"51013923","gene_card_id":"MET16","chromosome_location":"chromosome 16","locus":"YPR167C","synonyms":["3'-phosphoadenylylsulfate reductase","PAPS reductase, thioredoxin dependent","PAdoPS reductase"],"enzyme_classes":["1.8.4.8"],"go_classes":[{"category":"Component","description":" Not Available"},{"category":"Function","description":" oxidoreductase activity, acting on a sulfur group of donors"},{"category":"Function","description":" phosphoadenylyl-sulfate reductase (thioredoxin) activity"},{"category":"Function","description":" oxidoreductase activity, acting on a sulfur group of donors, disulfide as acceptor"},{"category":"Function","description":" catalytic activity"},{"category":"Function","description":" oxidoreductase activity"},{"category":"Process","description":" oxidation reduction"},{"category":"Process","description":" sulfur metabolic process"},{"category":"Process","description":" sulfate assimilation"},{"category":"Process","description":" sulfur amino acid metabolic process"},{"category":"Process","description":" sulfur amino acid biosynthetic process"},{"category":"Process","description":" cysteine biosynthetic process"},{"category":"Process","description":" sulfate assimilation, phosphoadenylyl sulfate reduction by phosphoadenylyl-sulfate reductase (thioredoxin)"},{"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"}],"pfams":[{"name":"PAPS_reduct","identifier":"PF01507"}],"pathways":[{"name":"Sulfur metabolism","kegg_map_id":"00920"}],"gene_sequence":"ATGAAGACCTATCATTTGAATAATGATATAATTGTCACACAAGAACAGTTGGATCATTGGAATGAACAACTAATCAAGCTGGAAACGCCACAGGAGATTATTGCATGGTCTATCGTAACGTTTCCTCACCTTTTCCAAACCACTGCATTTGGTTTGACTGGCTTGGTTACTATCGATATGTTGTCAAAGCTATCTGAAAAATACTACATGCCAGAACTATTATTTATAGACACTTTGCACCATTTCCCACAAACTTTAACACTAAAAAACGAGATTGAGAAAAAATACTACCAGCCTAAAAATCAAACCATTCACGTATATAAGCCGGATGGATGTGAATCGGAGGCAGATTTTGCCTCGAAATACGGGGATTTCTTATGGGAGAAAGATGATGACAAGTACGATTATCTGGCCAAAGTGGAACCTGCACATCGTGCCTACAAAGAGCTACATATAAGTGCTGTGTTTACTGGTAGAAGAAAATCACAAGGTTCTGCCCGCTCCCAACTGTCGATTATTGAAATAGACGAACTTAATGGAATCTTAAAAATAAATCCATTGATCAATTGGACGTTCGAGCAGGTTAAACAGTATATAGATGCAAACAATGTACCATACAACGAACTTTTGGACCTTGGATATAGATCCATTGGTGATTACCATTCCACACAACCCGTCAAGGAAGGTGAAGATGAGAGAGCAGGAAGATGGAAGGGCAAGGCCAAGACCGAGTGTGGAATTCATGAAGCCAGCCGATTCGCGCAATTTTTAAAGCAAGATGCCTAG","protein_sequence":"MKTYHLNNDIIVTQEQLDHWNEQLIKLETPQEIIAWSIVTFPHLFQTTAFGLTGLVTIDMLSKLSEKYYMPELLFIDTLHHFPQTLTLKNEIEKKYYQPKNQTIHVYKPDGCESEADFASKYGDFLWEKDDDKYDYLAKVEPAHRAYKELHISAVFTGRRKSQGSARSQLSIIEIDELNGILKINPLINWTFEQVKQYIDANNVPYNELLDLGYRSIGDYHSTQPVKEGEDERAGRWKGKAKTECGIHEASRFAQFLKQDA"}]}