{"ymdb_id":"YMDB00731","created_at":"2011-05-29T18:47:29.000Z","updated_at":"2016-09-08T18:35:50.000Z","name":"3-hydroxyicosanoyl-CoA","cas":null,"state":null,"melting_point":null,"description":"3-Hydroxyicosanoyl-CoA is a coenzyme A derivative of hydroxyicosanoate. Fatty acids must be activated with CoA before any chemical modification can be applied. Also fatty acid metabolic intermediates will also exists as CoA derivatives until the CoA is enzymatically cleaved. The fatty acid group is linked to the terminal thoil moiety of CoA.","experimental_water_solubility":null,"experimental_logp_hydrophobicity":null,"location":"endoplasmic reticulum","synthesis_reference":null,"chebi_id":"52324","hmdb_id":null,"kegg_id":null,"pubchem_id":null,"cs_id":"23106991","foodb_id":null,"wikipedia_link":null,"biocyc_id":null,"iupac":"{[(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-4-hydroxy-2-({[hydroxy({hydroxy[(3R)-3-hydroxy-3-{[2-({2-[(3-hydroxyicosanoyl)sulfanyl]ethyl}carbamoyl)ethyl]carbamoyl}-2,2-dimethylpropoxy]phosphoryl}oxy)phosphoryl]oxy}methyl)oxolan-3-yl]oxy}phosphonic acid","traditional_iupac":"3-hydroxyeicosanoyl-coa","logp":"0.05218121503364798","pka":"1.8334045176178444","alogps_solubility":"9.89e-01 g/l","alogps_logp":"2.72","alogps_logs":"-3.04","acceptor_count":"18","donor_count":"10","rotatable_bond_count":"38","polar_surface_area":"383.8599999999999","refractivity":"256.5674","polarizability":"110.84033828528482","formal_charge":"0","physiological_charge":"-4","pka_strongest_basic":"4.946047024039826","pka_strongest_acidic":"0.8252479627216065","bioavailability":"0","number_of_rings":"3","rule_of_five":"0","ghose_filter":"0","veber_rule":"0","mddr_like_rule":"1","synonyms":["3-hydroxy-C20-CoA","3-hydroxyeicosanoyl-CoA","3-hydroxyeicosanoyl-coenzyme A","3-hydroxyicosanoyl-coenzyme A"],"pathways":[],"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":12087109,"citation":"Han, G., Gable, K., Kohlwein, S. D., Beaudoin, F., Napier, J. A., Dunn, T. M. (2002). \"The Saccharomyces cerevisiae YBR159w gene encodes the 3-ketoreductase of the microsomal fatty acid elongase.\" J Biol Chem 277:35440-35449."}],"proteins":[{"created_at":"2011-05-27T07:21:07.000Z","updated_at":"2011-05-27T15:01:27.000Z","name":"3-ketoacyl-CoA reductase","uniprot_id":"P38286","uniprot_name":"MKAR_YEAST","enzyme":true,"transporter":false,"gene_name":"IFA38","num_residues":347,"molecular_weight":"38707.80078","theoretical_pi":"10.01","general_function":"Involved in oxidoreductase activity","specific_function":"Component of the microsomal membrane bound fatty acid elongation system, which produces the 26-carbon very long-chain fatty acids (VLCFA) from palmitate. Catalyzes the reduction of the 3-ketoacyl-CoA intermediate that is formed in each cycle of fatty acid elongation. VLCFAs serve as precursors for ceramide and sphingolipids","reactions":[{"id":1741,"direction":"\u003c\u003e","locations":"endoplasmic reticulum","altext":null,"export":true,"pw_reaction_id":null,"source":null},{"id":1742,"direction":"\u003c\u003e","locations":"endoplasmic reticulum","altext":null,"export":true,"pw_reaction_id":null,"source":null},{"id":1743,"direction":"\u003c\u003e","locations":"endoplasmic reticulum","altext":null,"export":true,"pw_reaction_id":null,"source":null},{"id":1744,"direction":"\u003c\u003e","locations":"endoplasmic reticulum","altext":null,"export":true,"pw_reaction_id":null,"source":null},{"id":1745,"direction":"\u003c\u003e","locations":"endoplasmic reticulum","altext":null,"export":true,"pw_reaction_id":null,"source":null},{"id":1746,"direction":"\u003c\u003e","locations":"endoplasmic reticulum","altext":null,"export":true,"pw_reaction_id":null,"source":null},{"id":1747,"direction":"\u003c\u003e","locations":"endoplasmic reticulum","altext":null,"export":true,"pw_reaction_id":null,"source":null},{"id":2810,"direction":"\u003e","locations":"Endoplasmic reticulum membrane; Single-pass membrane protein (Potential)","altext":"3-hydroxyacyl-CoA + NADP(+) = 3-oxoacyl-CoA + NADPH.","export":false,"pw_reaction_id":null,"source":null}],"signal_regions":"None","transmembrane_regions":"20-40","pdb_id":null,"cellular_location":"Endoplasmic reticulum membrane; Single-pass membrane protein (Potential)","genbank_gene_id":"AY557868","genbank_protein_id":"45269627","gene_card_id":"IFA38","chromosome_location":"chromosome 2","locus":"YBR159W","synonyms":["3-ketoreductase","KAR","Microsomal beta-keto-reductase"],"enzyme_classes":["1.1.1.-"],"go_classes":[{"category":"Component","description":" Not Available"},{"category":"Function","description":" catalytic activity"},{"category":"Function","description":" binding"},{"category":"Function","description":" oxidoreductase activity"},{"category":"Process","description":" metabolic process"},{"category":"Process","description":" oxidation reduction"}],"pfams":[{"name":"adh_short","identifier":"PF00106"}],"pathways":[],"gene_sequence":"ATGACTTTTATGCAACAGCTTCAAGAGGCTGGGGAAAGATTTAGGTGTATCAATGGTCTTTTATGGGTTGTTTTTGGGCTTGGTGTCTTAAAATGTACAACGTTATCACTTAGATTTTTAGCTCTTATTTTTGATCTTTTTTTACTACCAGCAGTCAATTTCGACAAGTATGGTGCTAAAACTGGTAAATACTGTGCTATCACTGGTGCAAGTGACGGTATTGGTAAAGAATTTGCTAGACAAATGGCGAAACGTGGCTTCAACTTGGTATTGATCTCGAGAACGCAATCTAAATTGGAGGCTTTACAAAAAGAACTAGAAGATCAACATCATGTCGTTGTAAAGATTCTAGCCATTGACATTGCGGAGGATAAAGAATCCAACTATGAATCCATTAAGGAATTGTGTGCGCAGTTACCAATCACCGTTTTGGTCAATAATGTTGGTCAATCACACTCCATTCCTGTTCCATTTTTGGAAACAGAAGAGAAGGAGCTTAGAAATATTATCACTATCAATAACACTGCTACATTATTAATTACACAAATCATTGCACCAAAGATTGTGGAAACTGTGAAAGCTGAAAACAAGAAGTCGGGTACTCGTGGTTTGATCTTAACCATGGGCTCATTTGGTGGTCTGATTCCCACCCCACTTTTGGCTACATACAGTGGTTCGAAATCATTCTTACAAGGTTGGTCTAACTCTTTGGCTGGGGAATTATCTAAAGATGCTATCGATGTTGAATTAATCATTTCATATTTGGTCACTAGCTCGATGTCTAAAATCAGAAGATCATCTTTAATGATCCCAAATCCACAACAGTTTGTAAAATCCACTTTAAGAAGCGTTGGCAGACGCTGCGGCTCTCAAGAAAGATACGCTACTATGACCCCTTACTGGGCGCACGCAGTGTATCAATTTGTAATTACAGAGACCTTTGGCGTTTACTCTAAGATTGTTAACTCCATTAATTATTCCTTCCATAAATCTATCAGAATTAGAGCCTTAAAAAAAGCCGCAAGACAGGTTAAAAAGGAATAG","protein_sequence":"MTFMQQLQEAGERFRCINGLLWVVFGLGVLKCTTLSLRFLALIFDLFLLPAVNFDKYGAKTGKYCAITGASDGIGKEFARQMAKRGFNLVLISRTQSKLEALQKELEDQHHVVVKILAIDIAEDKESNYESIKELCAQLPITVLVNNVGQSHSIPVPFLETEEKELRNIITINNTATLLITQIIAPKIVETVKAENKKSGTRGLILTMGSFGGLIPTPLLATYSGSKSFLQGWSNSLAGELSKDAIDVELIISYLVTSSMSKIRRSSLMIPNPQQFVKSTLRSVGRRCGSQERYATMTPYWAHAVYQFVITETFGVYSKIVNSINYSFHKSIRIRALKKAARQVKKE"}]}