{"ymdb_id":"YMDB00882","created_at":"2011-05-29T19:01:04.000Z","updated_at":"2016-09-08T18:36:01.000Z","name":"Heme A","cas":"57560-10-8","state":"Solid","melting_point":"","description":"Heme a is a derivative of protoheme IX (heme b or heme). Heme a differs from heme b in that a methyl side chain at ring position 8 is oxidized into a formyl group, and one of the vinyl side chains, at ring position 2, has been replaced by an isoprenoid chain. In the heme biosynthesis from uroporphyrinogen-III pathway, different derivatives of protoheme can actually be formed that differ in modifications to the porphyrin ring, including how it is bound to the protein (e.g. heme o, heme a, heme c, and heme d). [Biocyc PWY-5189]","experimental_water_solubility":"","experimental_logp_hydrophobicity":"","location":"mitochondrion","synthesis_reference":null,"chebi_id":"24479","hmdb_id":"HMDB06901","kegg_id":"C15670","pubchem_id":"23724533","cs_id":null,"foodb_id":null,"wikipedia_link":"Heme_A","biocyc_id":"HEME_A","iupac":"4,20-bis(2-carboxyethyl)-15-ethenyl-5-formyl-10-[(4E,8E)-1-hydroxy-5,9,13-trimethyltetradeca-4,8,12-trien-1-yl]-9,14,19-trimethyl-2lambda5,22,23lambda5,25-tetraaza-1-ferraoctacyclo[11.9.1.1^{1,8}.1^{3,21}.0^{2,6}.0^{16,23}.0^{18,22}.0^{11,25}]pentacosa-2,4,6,8,10,12,14,16(23),17,19,21(24)-undecaene-2,23-bis(ylium)","traditional_iupac":"4,20-bis(2-carboxyethyl)-15-ethenyl-5-formyl-10-[(4E,8E)-1-hydroxy-5,9,13-trimethyltetradeca-4,8,12-trien-1-yl]-9,14,19-trimethyl-2lambda5,22,23lambda5,25-tetraaza-1-ferraoctacyclo[11.9.1.1^{1,8}.1^{3,21}.0^{2,6}.0^{16,23}.0^{18,22}.0^{11,25}]pentacosa-2,4,6,8,10,12,14,16(23),17,19,21(24)-undecaene-2,23-bis(ylium)","logp":"4.584151617056509","pka":"3.8155641716420643","alogps_solubility":"2.06e-04 g/l","alogps_logp":"2.16","alogps_logs":"-6.65","acceptor_count":"6","donor_count":"3","rotatable_bond_count":"18","polar_surface_area":"129.52","refractivity":"244.19140000000013","polarizability":"100.19878062592451","formal_charge":"2","physiological_charge":"0","pka_strongest_basic":"-3.051362726899786","pka_strongest_acidic":"3.2038280657546654","bioavailability":"0","number_of_rings":"8","rule_of_five":"0","ghose_filter":"0","veber_rule":"0","mddr_like_rule":"1","synonyms":["(SP-4-2)[7-ethenyl-17-formyl-12-[(4E,8E)-1-hydroxy-5,9,13-trimethyl-4,8,12-tetradecatrienyl]-3,8,13-trimethyl-21H,23H-porphine-2,18-dipropanoato(4-)-kappaN21,kappaN22,kappaN23,kappaN24]-Ferrate(2-)","[SP-4-2-(E,E)]-[7-ethenyl-17-formyl-12-(1-hydroxy-5,9,13-trimethyl-4,8,12-tetradecatrienyl)-3,8,13-trimethyl-21H,23H-porphine-2,18-dipropanoato(4-)-N21,N22,N23,N24]-Ferrate(2-)","Heme a"],"pathways":[{"name":"Porphyrin and chlorophyll metabolism","kegg_map_id":"00860"},{"name":"Porphyrin Metabolism","kegg_map_id":null}],"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":20979346,"citation":"Buchensky, C., Almiron, P., Mantilla, B. S., Silber, A. M., Cricco, J. A. (2010). \"The Trypanosoma cruzi proteins TcCox10 and TcCox15 catalyze the formation of heme A in the yeast Saccharomyces cerevisiae.\" FEMS Microbiol Lett 312:133-141."}],"proteins":[{"created_at":"2011-05-27T02:28:40.000Z","updated_at":"2011-05-29T05:06:36.000Z","name":"Cytochrome c oxidase assembly protein COX15","uniprot_id":"P40086","uniprot_name":"COX15_YEAST","enzyme":true,"transporter":false,"gene_name":"COX15","num_residues":486,"molecular_weight":"54657.89844","theoretical_pi":"10.83","general_function":"Involved in protein complex assembly","specific_function":"Required for the assembly of yeast cytochrome oxidase. Involved in the biosynthesis of heme A and the initial step in this pathway, the hydroxylation of heme O, is thought to be catalyzed by a three-component mono-oxygenase consisting of COX15, ferredoxin and ferredoxin reductase","reactions":[],"signal_regions":"None","transmembrane_regions":"86-106;171-191;201-221;244-264;294-314;403-423;425-445","pdb_id":null,"cellular_location":"Mitochondrion inner membrane; Multi-pass membrane protein","genbank_gene_id":"L38643","genbank_protein_id":"603947","gene_card_id":"COX15","chromosome_location":"chromosome 5","locus":"YER141W","synonyms":[],"enzyme_classes":[],"go_classes":[{"category":"Component","description":" cell part"},{"category":"Component","description":" membrane"},{"category":"Function","description":" Not Available"},{"category":"Process","description":" cellular component organization or biogenesis"},{"category":"Process","description":" cellular component organization"},{"category":"Process","description":" cellular component assembly"},{"category":"Process","description":" macromolecular complex assembly"},{"category":"Process","description":" protein complex assembly"}],"pfams":[{"name":"COX15-CtaA","identifier":"PF02628"}],"pathways":[],"gene_sequence":"ATGCTTTTCAGAAACATAGAAGTGGGCAGGCAGGCAGCTAAGCTATTAACGAGAACCTCGAGTCGTTTGGCCTGGCAAAGTATTGGGGCCTCAAGGAATATTTCTACCATCAGACAACAAATCAGAAAGACTCAACTATATAATTTTAAGAAAACTGTGAGCATCCGTCCATTTTCTCTCTCCTCCCCTGTTTTTAAACCACATGTTGCTTCAGAATCAAACCCTATAGAATCACGTTTGAAGACCTCGAAGAATGTTGCTTACTGGTTAATAGGTACATCCGGTTTGGTATTTGGTATTGTTGTTCTTGGTGGGTTGACTAGACTAACAGAATCGGGGCTGAGTATTACCGAATGGAAACCTGTCACAGGTACTTTGCCCCCTATGAACCAGAAGGAATGGGAAGAAGAATTTATCAAGTATAAGGAATCACCAGAATTTAAATTGTTGAATTCTCACATTGATTTAGACGAGTTCAAGTTTATATTTTTTATGGAGTGGATTCATAGATTGTGGGGTCGTGCTATCGGCGCTGTTTTTATATTACCTGCAGTTTATTTCGCTGTATCTAAAAAAACTTCAGGCCATGTCAATAAGAGGTTGTTTGGTCTCGCAGGTTTATTAGGATTACAAGGATTTGTTGGTTGGTGGATGGTGAAGTCTGGTCTTGATCAAGAGCAACTAGACGCAAGAAAATCAAAGCCTACCGTTTCTCAATATAGACTTACTACGCATTTGGGTACCGCCTTCTTTTTATACATGGGTATGCTCTGGACTGGTTTGGAAATATTGAGAGAATGTAAATGGATTAAGAACCCTGTTCAAGCCATTAGTCTCTTCAAAAAATTAGATAATCCCGCAATTGGCCCAATGAGAAAGATTTCTTTAGCTTTGTTAGCGGTGTCTTTCCTTACCGCTATGAGTGGCGGTATGGTTGCCGGTTTGGATGCTGGTTGGGTCTATAACACCTGGCCAAAAATGGGTGAACGATGGTTCCCTAGTTCTCGTGAATTAATGGACGAAAACTTCTGTAGAAGAGAGGACAAGAAAGATCTGTGGTGGAGGAATTTGCTAGAAAACCCGGTTACAGTTCAGTTGGTCCATAGGACATGTGCGTACGTTGCGTTTACATCAGTACTAGCTGCTCATATGTACGCTATCAAAAAGAAGGCCGTAATTCCAAGGAACGCGATGACCTCTTTGCATGTTATGATGGGCGTCGTTACTTTACAAGCAACACTTGGTATTTTAACTATATTGTACCTAGTCCCAATATCGTTAGCTTCTATCCATCAAGCTGGTGCTTTGGCGTTGCTAACAAGTTCTTTGGTGTTTGCCTCTCAATTAAGGAAGCCAAGAGCTCCGATGAGAAACGTAATCATTACCTTGCCACATTCAAGCAAAGTAACTAGCGGTAAAATTTTAAGTGAAGCGTCGAAGTTAGCCTCGAAACCATTATAA","protein_sequence":"MLFRNIEVGRQAAKLLTRTSSRLAWQSIGASRNISTIRQQIRKTQLYNFKKTVSIRPFSLSSPVFKPHVASESNPIESRLKTSKNVAYWLIGTSGLVFGIVVLGGLTRLTESGLSITEWKPVTGTLPPMNQKEWEEEFIKYKESPEFKLLNSHIDLDEFKFIFFMEWIHRLWGRAIGAVFILPAVYFAVSKKTSGHVNKRLFGLAGLLGLQGFVGWWMVKSGLDQEQLDARKSKPTVSQYRLTTHLGTAFFLYMGMLWTGLEILRECKWIKNPVQAISLFKKLDNPAIGPMRKISLALLAVSFLTAMSGGMVAGLDAGWVYNTWPKMGERWFPSSRELMDENFCRREDKKDLWWRNLLENPVTVQLVHRTCAYVAFTSVLAAHMYAIKKKAVIPRNAMTSLHVMMGVVTLQATLGILTILYLVPISLASIHQAGALALLTSSLVFASQLRKPRAPMRNVIITLPHSSKVTSGKILSEASKLASKPL"}]}