ID R9Z4S4_9CNID Unreviewed; 265 AA. AC R9Z4S4; DT 18-SEP-2013, integrated into UniProtKB/TrEMBL. DT 18-SEP-2013, sequence version 1. DT 06-JUL-2016, entry version 16. DE RecName: Full=Cytochrome c oxidase subunit 1 {ECO:0000256|RuleBase:RU000369}; DE EC=1.9.3.1 {ECO:0000256|RuleBase:RU000369}; DE Flags: Fragment; GN Name=cox1 {ECO:0000313|EMBL:AGO35974.1}; OS Callogorgia gilberti. OG Mitochondrion {ECO:0000313|EMBL:AGO35974.1}. OC Eukaryota; Metazoa; Cnidaria; Anthozoa; Octocorallia; Alcyonacea; OC Calcaxonia; Primnoidae; Callogorgia. OX NCBI_TaxID=1239271 {ECO:0000313|EMBL:AGO35974.1}; RN [1] {ECO:0000313|EMBL:AGO35974.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=MOL-502-1 {ECO:0000313|EMBL:AGO35974.1}; RX PubMed=23786376; DOI=10.1111/mec.12370; RA Quattrini A.M., Georgian S.E., Byrnes L., Stevens A., Falco R., RA Cordes E.E.; RT "Niche divergence by deep-sea octocorals in the genus Callogorgia RT across the continental slope of the Gulf of Mexico."; RL Mol. Ecol. 22:4123-4140(2013). 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: 4 ferrocytochrome c + O(2) + 4 H(+) = 4 CC ferricytochrome c + 2 H(2)O. {ECO:0000256|RuleBase:RU000369}. CC -!- PATHWAY: Energy metabolism; oxidative phosphorylation. CC {ECO:0000256|RuleBase:RU000369}. 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; KC771680; AGO35974.1; -; Genomic_DNA. 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:0070469; C:respiratory chain; IEA:UniProtKB-KW. DR GO; GO:0004129; F:cytochrome-c oxidase activity; IEA:UniProtKB-EC. DR GO; GO:0020037; F:heme binding; IEA:InterPro. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR GO; GO:0009060; P:aerobic respiration; IEA:InterPro. DR GO; GO:0006119; P:oxidative phosphorylation; IEA:UniProtKB-UniPathway. DR Gene3D; 1.20.210.10; -; 1. DR InterPro; IPR000883; COX1. DR InterPro; IPR023616; 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. PE 3: Inferred from homology; KW Copper {ECO:0000256|RuleBase:RU000369}; KW Electron transport {ECO:0000256|RuleBase:RU000369}; KW Heme {ECO:0000256|RuleBase:RU000369}; KW Iron {ECO:0000256|RuleBase:RU000369}; KW Membrane {ECO:0000256|RuleBase:RU000369, ECO:0000256|SAM:Phobius}; KW Metal-binding {ECO:0000256|RuleBase:RU000369}; KW Mitochondrion {ECO:0000256|RuleBase:RU000369, KW ECO:0000313|EMBL:AGO35974.1}; KW Mitochondrion inner membrane {ECO:0000256|RuleBase:RU000369}; KW Oxidoreductase {ECO:0000256|RuleBase:RU000369}; KW Respiratory chain {ECO:0000256|RuleBase:RU000369}; KW Transmembrane {ECO:0000256|RuleBase:RU000369, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}; KW Transport {ECO:0000256|RuleBase:RU000369}. FT TRANSMEM 20 39 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 59 85 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 106 130 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 150 173 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 185 212 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 245 263 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 2 265 COX1. {ECO:0000259|PROSITE:PS50855}. FT NON_TER 265 265 {ECO:0000313|EMBL:AGO35974.1}. SQ SEQUENCE 265 AA; 28929 MW; 191C00008DD74435 CRC64; MNKYLTRWLF STNHKDIGTL YLLFGAFSGM AGTASSMLIR LELSAPGSML GDDHLYNVVV TSHALLMIFF LVMPVMIGGF GNWFVPIMIG APDMAFPRLN NISFWLLPPS LILLVGSMFV EQGAGTGWTI YPPLASVQAH SGGAVDMAIF SLHLAGVSSI LSSINFITTI INMRVPGMTM HRLPLFVWSV LVTTILLLLS LPVLAGAITM LLTDRNFNTT FFDPAGGGDP ILFQHLFWFF GHPEVYILIL PGFGIVSQII PTFSA //