{"ymdb_id":"YMDB00041","created_at":"2011-05-29T15:50:56.000Z","updated_at":"2016-09-08T18:34:56.000Z","name":"Heme","cas":"14875-96-8","state":"Solid","melting_point":null,"description":"Protoheme IX (heme b or heme) is the final product in the heme biosynthesis from uroporphyrinogen-III pathway. It is an iron-containing prosthetic group found in many essential proteins including cytochromes and heme-containing globins. In addition to its role in oxidative metabolism, heme also functions as a regulatory molecule in transcription, translation, protein targeting, protein stability, and cellular differentiation. 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":null,"experimental_logp_hydrophobicity":"","location":"mitochondrion","synthesis_reference":null,"chebi_id":"17627","hmdb_id":"HMDB03178","kegg_id":"C00032","pubchem_id":"26945","cs_id":"7289","foodb_id":null,"wikipedia_link":"Heme_b","biocyc_id":"PROTOHEME","iupac":null,"traditional_iupac":null,"logp":null,"pka":null,"alogps_solubility":"1.24e-03 g/l","alogps_logp":"2.00","alogps_logs":"-5.75","acceptor_count":"0","donor_count":"0","rotatable_bond_count":"8","polar_surface_area":"121.19","refractivity":"176.18550000000002","polarizability":"69.91870062807914","formal_charge":"2","physiological_charge":"2","pka_strongest_basic":null,"pka_strongest_acidic":null,"bioavailability":"0","number_of_rings":"8","rule_of_five":"0","ghose_filter":"0","veber_rule":"0","mddr_like_rule":"1","synonyms":["(protoporphyrinato)iron","Ferroheme","Ferroheme b","Ferroprotoheme","Ferroprotoporphyrin","Ferroprotoporphyrin IX","Ferrous protoheme","Ferrous protoheme IX","Haem","Hem","Heme","Iron protoporphyrin","Iron protoporphyrin IX","Iron(II) protoporphyrin IX","Protoferroheme","Protohaem","Protoheme","Protoheme IX","Reduced hematin"],"pathways":[{"name":"Porphyrin and chlorophyll metabolism","kegg_map_id":"00860"},{"name":"Porphyrin Metabolism","kegg_map_id":null},{"name":"Steroid biosynthesis","kegg_map_id":"00100"},{"name":"Oxidative phosphorylation","kegg_map_id":"00190"}],"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":3028387,"citation":"Enosawa, S., Ohashi, A. (1986). \"Localization of enzyme for heme attachment to apocytochrome c in yeast mitochondria.\" Biochem Biophys Res Commun 141:1145-1150."},{"pubmed_id":8234090,"citation":"Chelstowska, A., Rytka, J. (1993). \"[Biosynthesis of heme in yeast Saccharomyces cerevisiae].\" Postepy Biochem 39:173-185."},{"pubmed_id":14559249,"citation":"Hoffman, M., Gora, M., Rytka, J. (2003). \"Identification of rate-limiting steps in yeast heme biosynthesis.\" Biochem Biophys Res Commun 310:1247-1253."}],"proteins":[{"created_at":"2011-05-24T21:10:55.000Z","updated_at":"2011-05-27T15:00:57.000Z","name":"Cytochrome c heme lyase","uniprot_id":"P06182","uniprot_name":"CCHL_YEAST","enzyme":true,"transporter":false,"gene_name":"CYC3","num_residues":269,"molecular_weight":"30080.69922","theoretical_pi":"5.18","general_function":"Involved in holocytochrome-c synthase activity","specific_function":"Links covalently the heme group to the apoprotein of cytochrome c","reactions":[{"id":2365,"direction":"\u003e","locations":"Mitochondrion inner membrane","altext":"Holocytochrome c = apocytochrome c + heme.","export":false,"pw_reaction_id":null,"source":null}],"signal_regions":"None","transmembrane_regions":"None","pdb_id":null,"cellular_location":"Mitochondrion inner membrane","genbank_gene_id":"U12980","genbank_protein_id":"595545","gene_card_id":"CYC3","chromosome_location":"chromosome 1","locus":"YAL039C","synonyms":["CCHL","Holocytochrome-c synthase"],"enzyme_classes":["4.4.1.17"],"go_classes":[{"category":"Component","description":" organelle"},{"category":"Component","description":" membrane-bounded organelle"},{"category":"Component","description":" intracellular membrane-bounded organelle"},{"category":"Component","description":" mitochondrion"},{"category":"Function","description":" holocytochrome-c synthase activity"},{"category":"Function","description":" catalytic activity"},{"category":"Function","description":" lyase activity"},{"category":"Function","description":" carbon-sulfur lyase activity"},{"category":"Process","description":" Not Available"}],"pfams":[{"name":"Cyto_heme_lyase","identifier":"PF01265"}],"pathways":[{"name":"Porphyrin and chlorophyll metabolism","kegg_map_id":"00860"}],"gene_sequence":"ATGGGTTGGTTTTGGGCAGATCAAAAAACTACGGGCAAAGATATTGGTGGGGCAGCAGTATCATCCATGTCAGGGTGCCCAGTCATGCACGAGTCGTCGTCGTCGTCGCCACCATCCTCTGAGTGCCCCGTTATGCAGGGAGATAACGATAGAATAAACCCGCTGAACAATATGCCGGAGTTGGCAGCATCCAAACAGCCTGGCCAAAAGATGGACTTGCCCGTTGATCGGACCATCTCCAGCATCCCCAAGAGTCCAGACAGTAACGAGTTCTGGGAGTATCCTTCTCCACAACAGATGTACAATGCTATGGTTAGAAAGGGCAAGATTGGCGGTAGCGGCGAAGTCGCCGAAGATGCAGTGGAGTCCATGGTGCAGGTCCACAACTTTCTAAATGAAGGGTGCTGGCAGGAAGTGCTCGAATGGGAAAAACCGCACACAGATGAAAGCCACGTGCAGCCTAAGTTGCTGAAATTCATGGGGAAACCGGGCGTATTGAGCCCTCGTGCTCGCTGGATGCACCTGTGCGGCCTACTGTTTCCGTCCCATTTTAGCCAAGAACTACCATTCGACAGGCACGACTGGATTGTACTCCGAGGCGAGCGCAAAGCGGAACAACAACCTCCAACCTTCAAGGAAGTTAGATACGTCTTGGATTTCTACGGAGGGCCCGACGACGAAAACGGAATGCCTACTTTCCACGTGGATGTCCGTCCTGCCCTAGATAGTCTAGACAATGCTAAGGACCGGATGACCCGTTTCTTGGACCGGATGATCTCGGGTCCGTCCTCTTCGTCCTCCGCCCCTTAA","protein_sequence":"MGWFWADQKTTGKDIGGAAVSSMSGCPVMHESSSSSPPSSECPVMQGDNDRINPLNNMPELAASKQPGQKMDLPVDRTISSIPKSPDSNEFWEYPSPQQMYNAMVRKGKIGGSGEVAEDAVESMVQVHNFLNEGCWQEVLEWEKPHTDESHVQPKLLKFMGKPGVLSPRARWMHLCGLLFPSHFSQELPFDRHDWIVLRGERKAEQQPPTFKEVRYVLDFYGGPDDENGMPTFHVDVRPALDSLDNAKDRMTRFLDRMISGPSSSSSAP"},{"created_at":"2011-05-24T21:11:28.000Z","updated_at":"2011-07-22T17:55:05.000Z","name":"Ferrochelatase, mitochondrial","uniprot_id":"P16622","uniprot_name":"HEMH_YEAST","enzyme":true,"transporter":false,"gene_name":"HEM15","num_residues":393,"molecular_weight":"44595.80078","theoretical_pi":"9.46","general_function":"Involved in ferrochelatase activity","specific_function":"Catalyzes the ferrous insertion into protoporphyrin IX","reactions":[{"id":1538,"direction":"\u003e","locations":"mitochondrion","altext":null,"export":true,"pw_reaction_id":null,"source":null},{"id":2366,"direction":"\u003e","locations":"Mitochondrion inner membrane; Peripheral membrane protein; Matrix side.","altext":"Protoheme + 2 H(+) = protoporphyrin + Fe(2+).","export":false,"pw_reaction_id":null,"source":null}],"signal_regions":"None","transmembrane_regions":"None","pdb_id":"1LBQ","cellular_location":"Mitochondrion inner membrane; Peripheral membrane protein; Matrix side.","genbank_gene_id":"J05395","genbank_protein_id":"171660","gene_card_id":"HEM15","chromosome_location":"chromosome 15","locus":"YOR176W","synonyms":["Heme synthase","Protoheme ferro-lyase"],"enzyme_classes":["4.99.1.1"],"go_classes":[{"category":"Component","description":" Not Available"},{"category":"Function","description":" ferrochelatase activity"},{"category":"Function","description":" catalytic activity"},{"category":"Function","description":" lyase activity"},{"category":"Process","description":" porphyrin biosynthetic process"},{"category":"Process","description":" metabolic process"},{"category":"Process","description":" nitrogen compound metabolic process"},{"category":"Process","description":" heme biosynthetic process"},{"category":"Process","description":" tetrapyrrole metabolic process"},{"category":"Process","description":" porphyrin metabolic process"}],"pfams":[{"name":"Ferrochelatase","identifier":"PF00762"}],"pathways":[{"name":"Porphyrin and chlorophyll metabolism","kegg_map_id":"00860"}],"gene_sequence":"ATGCTTTCCAGAACAATCCGTACACAAGGTTCCTTCCTAAGAAGATCACAACTGACCATTACAAGATCATTTTCGGTTACATTCAACATGCAGAATGCACAAAAGAGATCACCCACAGGAATTGTTTTGATGAACATGGGTGGCCCCTCTAAAGTTGAGGAAACATATGATTTTTTGTATCAATTATTTGCCGATAATGACCTAATTCCCATTAGTGCTAAGTATCAGAAGACAATTGCTAAATATATTGCTAAGTTTCGTACCCCCAAGATAGAGAAGCAATATAGGGAAATTGGTGGGGGCTCCCCAATCCGGAAATGGTCTGAGTATCAAGCCACTGAGGTCTGTAAAATCTTAGATAAAACCTGTCCAGAAACGGCGCCTCATAAGCCTTACGTGGCGTTTCGTTACGCAAAGCCGCTAACCGCAGAAACTTATAAACAAATGCTAAAAGATGGCGTGAAGAAGGCAGTGGCCTTTTCTCAATATCCTCATTTCTCTTATTCCACTACCGGGTCATCCATCAACGAATTGTGGAGACAGATTAAGGCATTGGACTCCGAGAGATCTATATCTTGGTCGGTTATTGATCGTTGGCCTACAAATGAAGGTCTAATCAAGGCCTTCTCCGAAAATATCACCAAAAAACTACAAGAGTTTCCGCAACCTGTCAGAGACAAGGTTGTTTTATTGTTTTCCGCACATTCTCTACCCATGGATGTTGTTAACACCGGTGATGCCTACCCAGCTGAGGTAGCTGCGACGGTTTACAACATCATGCAAAAATTAAAGTTTAAAAACCCTTATAGGTTGGTTTGGCAATCCCAAGTTGGACCAAAACCATGGTTGGGAGCGCAGACAGCTGAAATTGCGGAATTTTTAGGCCCCAAAGTTGATGGCCTAATGTTTATTCCTATCGCCTTTACCTCTGATCATATTGAAACATTGCATGAAATTGACTTAGGCGTCATTGGGGAATCGGAATATAAGGATAAATTTAAGAGATGCGAATCTTTAAATGGCAACCAGACCTTTATTGAAGGCATGGCAGATCTCGTCAAAAGCCACTTACAGAGTAACCAACTCTATTCTAATCAACTACCTCTTGATTTTGCACTTGGCAAGTCCAATGATCCTGTAAAGGACCTTTCATTGGTATTTGGCAATCACGAATCTACTTGA","protein_sequence":"MLSRTIRTQGSFLRRSQLTITRSFSVTFNMQNAQKRSPTGIVLMNMGGPSKVEETYDFLYQLFADNDLIPISAKYQKTIAKYIAKFRTPKIEKQYREIGGGSPIRKWSEYQATEVCKILDKTCPETAPHKPYVAFRYAKPLTAETYKQMLKDGVKKAVAFSQYPHFSYSTTGSSINELWRQIKALDSERSISWSVIDRWPTNEGLIKAFSENITKKLQEFPQPVRDKVVLLFSAHSLPMDVVNTGDAYPAEVAATVYNIMQKLKFKNPYRLVWQSQVGPKPWLGAQTAEIAEFLGPKVDGLMFIPIAFTSDHIETLHEIDLGVIGESEYKDKFKRCESLNGNQTFIEGMADLVKSHLQSNQLYSNQLPLDFALGKSNDPVKDLSLVFGNHEST"}]}