ID A0A1D8GYF6_9SACH Unreviewed; 534 AA. AC A0A1D8GYF6; DT 18-JAN-2017, integrated into UniProtKB/TrEMBL. DT 18-JAN-2017, sequence version 1. DT 16-JAN-2019, entry version 11. DE RecName: Full=Cytochrome c oxidase subunit 1 {ECO:0000256|RuleBase:RU000369}; DE EC=1.9.3.1 {ECO:0000256|RuleBase:RU000369}; GN Name=cox1 {ECO:0000313|EMBL:AOT85112.1}; OS Saccharomyces arboricola. OG Mitochondrion {ECO:0000313|EMBL:AOT85112.1}. OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; OC Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=706196 {ECO:0000313|EMBL:AOT85112.1}; RN [1] {ECO:0000313|EMBL:AOT85112.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=CBS 10644 {ECO:0000313|EMBL:AOT85112.1}, and NRRL Y-63701 RC {ECO:0000313|EMBL:AOT85126.1}; RX PubMed=28992063; DOI=.1093/dnares/dsx026; RA Sulo P., Szaboova D., Bielik P., Polakova S., Soltys K., Jatzova K., RA Szemes T.; RT "The evolutionary history of Saccharomyces species inferred from RT completed mitochondrial genomes and revision in the 'yeast RT mitochondrial genetic code'."; RL DNA Res. 24:571-583(2017). CC -!- FUNCTION: Cytochrome c oxidase is the component of the respiratory CC chain that catalyzes the reduction of oxygen to water. Subunits 1- CC 3 form the functional core of the enzyme complex. CO I is the CC catalytic subunit of the enzyme. Electrons originating in CC cytochrome c are transferred via the copper A center of subunit 2 CC and heme A of subunit 1 to the bimetallic center formed by heme A3 CC and copper B. {ECO:0000256|RuleBase:RU000369}. CC -!- CATALYTIC ACTIVITY: CC Reaction=4 [Fe(II)cytochrome c] + 4 H(+) + O2 = 4 CC [Fe(III)cytochrome c] + 2 H2O; Xref=Rhea:RHEA:11436, Rhea:RHEA- CC COMP:10350, Rhea:RHEA-COMP:14399, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:29033, CC ChEBI:CHEBI:29034; EC=1.9.3.1; CC Evidence={ECO:0000256|RuleBase:RU000369, CC ECO:0000256|SAAS:SAAS01116619}; CC -!- PATHWAY: Energy metabolism; oxidative phosphorylation. CC {ECO:0000256|RuleBase:RU000369, ECO:0000256|SAAS:SAAS00887552}. CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane CC {ECO:0000256|RuleBase:RU000369}; Multi-pass membrane protein CC {ECO:0000256|RuleBase:RU000369}. CC -!- SIMILARITY: Belongs to the heme-copper respiratory oxidase family. CC {ECO:0000256|RuleBase:RU000369}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; KX657740; AOT85112.1; -; Genomic_DNA. DR EMBL; KX657741; AOT85126.1; -; Genomic_DNA. DR RefSeq; YP_009310804.1; NC_031511.1. DR GeneID; 29991780; -. DR UniPathway; UPA00705; -. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell. DR GO; GO:0045277; C:respiratory chain complex IV; IEA:InterPro. DR GO; GO:0004129; F:cytochrome-c oxidase activity; IEA:UniProtKB-EC. DR GO; GO:0020037; F:heme binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0009060; P:aerobic respiration; IEA:InterPro. DR GO; GO:0006119; P:oxidative phosphorylation; IEA:UniProtKB-UniPathway. DR CDD; cd01663; Cyt_c_Oxidase_I; 1. DR Gene3D; 1.20.210.10; -; 1. DR InterPro; IPR023616; Cyt_c_oxase-like_su1_dom. DR InterPro; IPR036927; Cyt_c_oxase-like_su1_sf. DR InterPro; IPR000883; Cyt_C_Oxase_1. DR InterPro; IPR023615; Cyt_c_Oxase_su1_BS. DR InterPro; IPR033944; Cyt_c_oxase_su1_dom. DR PANTHER; PTHR10422; PTHR10422; 1. DR Pfam; PF00115; COX1; 1. DR PRINTS; PR01165; CYCOXIDASEI. DR SUPFAM; SSF81442; SSF81442; 1. DR PROSITE; PS50855; COX1; 1. DR PROSITE; PS00077; COX1_CUB; 1. PE 3: Inferred from homology; KW Copper {ECO:0000256|RuleBase:RU000369, ECO:0000256|SAAS:SAAS00887236}; KW Electron transport {ECO:0000256|RuleBase:RU000369, KW ECO:0000256|SAAS:SAAS00711094}; KW Heme {ECO:0000256|RuleBase:RU000369, ECO:0000256|SAAS:SAAS00711161}; KW Iron {ECO:0000256|RuleBase:RU000369, ECO:0000256|SAAS:SAAS00711183}; KW Membrane {ECO:0000256|RuleBase:RU000369, KW ECO:0000256|SAAS:SAAS00711163, ECO:0000256|SAM:Phobius}; KW Metal-binding {ECO:0000256|RuleBase:RU000369, KW ECO:0000256|SAAS:SAAS00711155}; KW Mitochondrion {ECO:0000256|RuleBase:RU000369, KW ECO:0000256|SAAS:SAAS00711157, ECO:0000313|EMBL:AOT85112.1}; KW Mitochondrion inner membrane {ECO:0000256|RuleBase:RU000369}; KW Oxidoreductase {ECO:0000256|RuleBase:RU000369, KW ECO:0000256|SAAS:SAAS00711097}; KW Respiratory chain {ECO:0000256|RuleBase:RU000369, KW ECO:0000256|SAAS:SAAS00711106}; KW Transmembrane {ECO:0000256|RuleBase:RU000369, KW ECO:0000256|SAAS:SAAS00711093, ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00711122, KW ECO:0000256|SAM:Phobius}; KW Transport {ECO:0000256|RuleBase:RU000369, KW ECO:0000256|SAAS:SAAS00711099}. FT TRANSMEM 14 36 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 56 80 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 101 127 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 147 172 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 184 212 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 244 262 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 274 291 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 303 326 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 338 359 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 379 397 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 409 430 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 450 473 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 1 534 COX1. {ECO:0000259|PROSITE:PS50855}. SQ SEQUENCE 534 AA; 58819 MW; 20F84927232E6DC6 CRC64; MVQRWLYSTN AKDIAVLYFM LAIFSGMAGT AMSLIIRLEL AAPGSQYLQG NSQLFNVLVV GHAVLMIFFL VMPALIGGFG NYLLPLMIGA TDTAFPRINN IAFWVLPMGL VCLVTSTLVE SGAGTGWTVY PPLSSIQAHS GPSVDLAIFA LHLTSISSLL GAINFIVTTL NMRTNGMTMH KLPLFVWSIF ITAFLLLLSL PVLSAGITML LLDRNFNTSF FEVAGGGDPI LYEHLFWFFG HPEVYILIIP GFGIISHVVS TYSKKPVFGE ISMVYAMASI GLLGFLVWSH HMYIVGLDAD TRAYFTSATM IIAIPTGIKI FSWLATVYGG SIRLATPMLY AIAFLFLFTM GGLTGVALAN ASLDVAFHDT YYVVGHFHYV LSMGAIFSLF AGYYYWSPQI LGLNYNEKLA QIQFWLIFIG ANVIFFPMHF LGINGMPRRI PDYPDAFAGW NYVASIGSFI ATLSLFLFIY ILYDQLVNGL NNKVTNKSVI YSKTPDFIES NMIFNLNTVK SSSIEFLLTS PPAVHSFNTP AVQS //