ID R9Z4S4_9CNID Unreviewed; 265 AA. AC R9Z4S4; DT 18-SEP-2013, integrated into UniProtKB/TrEMBL. DT 18-SEP-2013, sequence version 1. DT 27-MAR-2024, entry version 37. DE RecName: Full=Cytochrome c oxidase subunit 1 {ECO:0000256|ARBA:ARBA00015947, ECO:0000256|RuleBase:RU000369}; DE EC=7.1.1.9 {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; Scleralcyonacea; OC 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 across RT the continental slope of the Gulf of Mexico."; RL Mol. Ecol. 22:4123-4140(2013). CC -!- FUNCTION: Component of the cytochrome c oxidase, the last enzyme in the CC mitochondrial electron transport chain which drives oxidative CC phosphorylation. The respiratory chain contains 3 multisubunit CC complexes succinate dehydrogenase (complex II, CII), ubiquinol- CC cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CC CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to CC transfer electrons derived from NADH and succinate to molecular oxygen, CC creating an electrochemical gradient over the inner membrane that CC drives transmembrane transport and the ATP synthase. Cytochrome c CC oxidase is the component of the respiratory chain that catalyzes the CC reduction of oxygen to water. Electrons originating from reduced CC cytochrome c in the intermembrane space (IMS) are transferred via the CC dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 CC to the active site in subunit 1, a binuclear center (BNC) formed by CC heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 CC water molecules using 4 electrons from cytochrome c in the IMS and 4 CC protons from the mitochondrial matrix. {ECO:0000256|RuleBase:RU000369}. CC -!- CATALYTIC ACTIVITY: CC Reaction=4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(III)- CC [cytochrome c] + 4 H(+)(out) + 2 H2O; Xref=Rhea:RHEA:11436, CC Rhea:RHEA-COMP:10350, Rhea:RHEA-COMP:14399, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:29033, CC ChEBI:CHEBI:29034; EC=7.1.1.9; CC Evidence={ECO:0000256|RuleBase:RU000369}; CC -!- COFACTOR: CC Name=heme; Xref=ChEBI:CHEBI:30413; CC Evidence={ECO:0000256|ARBA:ARBA00001971}; CC -!- PATHWAY: Energy metabolism; oxidative phosphorylation. CC {ECO:0000256|ARBA:ARBA00004673, 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|ARBA:ARBA00009578, 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 AlphaFoldDB; R9Z4S4; -. DR UniPathway; UPA00705; -. DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell. DR GO; GO:0070469; C:respirasome; 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:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0006119; P:oxidative phosphorylation; IEA:UniProtKB-UniPathway. DR Gene3D; 1.20.210.10; Cytochrome c oxidase-like, subunit I domain; 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 PANTHER; PTHR10422; CYTOCHROME C OXIDASE SUBUNIT 1; 1. DR PANTHER; PTHR10422:SF18; CYTOCHROME C OXIDASE SUBUNIT 1; 1. DR Pfam; PF00115; COX1; 1. DR PRINTS; PR01165; CYCOXIDASEI. DR SUPFAM; SSF81442; Cytochrome c oxidase subunit I-like; 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}; 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, ECO:0000313|EMBL:AGO35974.1}; KW Mitochondrion inner membrane {ECO:0000256|RuleBase:RU000369}; KW Respiratory chain {ECO:0000256|RuleBase:RU000369}; KW Transmembrane {ECO:0000256|RuleBase:RU000369, ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}; KW Transport {ECO:0000256|RuleBase:RU000369}. FT TRANSMEM 20..39 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 59..85 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 106..130 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 150..173 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 185..212 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 245..263 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 2..265 FT /note="Cytochrome oxidase subunit I profile" FT /evidence="ECO:0000259|PROSITE:PS50855" FT NON_TER 265 FT /evidence="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 //