ID C7DR73_9ARAC Unreviewed; 319 AA. AC C7DR73; DT 22-SEP-2009, integrated into UniProtKB/TrEMBL. DT 22-SEP-2009, sequence version 1. DT 29-SEP-2021, entry version 48. DE RecName: Full=Cytochrome c oxidase subunit 1 {ECO:0000256|RuleBase:RU000369}; DE EC=7.1.1.9 {ECO:0000256|RuleBase:RU000369}; DE Flags: Fragment; GN Name=COI {ECO:0000313|EMBL:ACT98040.1}; OS Sitalcina californica. OG Mitochondrion {ECO:0000313|EMBL:ACT98040.1}. OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; OC Opiliones; Laniatores; Gonyleptoidea; Phalangodidae; Sitalcina. OX NCBI_TaxID=656469 {ECO:0000313|EMBL:ACT98040.1}; RN [1] {ECO:0000313|EMBL:ACT98040.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=19699807; DOI=10.1016/j.ympev.2009.08.020; RA Hedin M., Thomas S.M.; RT "Molecular systematics of eastern North American Phalangodidae (Arachnida: RT Opiliones: Laniatores), demonstrating convergent morphological evolution in RT caves."; RL Mol. Phylogenet. Evol. 54:107-121(2010). 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 CC [Fe(III)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 -!- PATHWAY: Energy metabolism; oxidative phosphorylation. CC {ECO:0000256|ARBA:ARBA00004673, ECO:0000256|RuleBase:RU000369}. CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi- CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}. Mitochondrion CC inner membrane {ECO:0000256|ARBA:ARBA00004448, CC ECO:0000256|RuleBase:RU000369}; Multi-pass membrane protein CC {ECO:0000256|ARBA:ARBA00004448, 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; GQ200406; ACT98040.1; -; 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: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; -; 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 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}; KW Electron transport {ECO:0000256|RuleBase:RU000369}; KW Heme {ECO:0000256|RuleBase:RU000369}; Iron {ECO:0000256|RuleBase:RU000369}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU000369}; KW Metal-binding {ECO:0000256|RuleBase:RU000369}; KW Mitochondrion {ECO:0000256|RuleBase:RU000369, ECO:0000313|EMBL:ACT98040.1}; KW Mitochondrion inner membrane {ECO:0000256|RuleBase:RU000369}; KW Respiratory chain {ECO:0000256|RuleBase:RU000369}; KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, KW ECO:0000256|RuleBase:RU000369}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|RuleBase:RU000369}. FT TRANSMEM 7..28 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 48..70 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 82..109 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 142..161 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 173..190 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 202..224 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 236..258 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 278..300 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 1..319 FT /note="COX1" FT /evidence="ECO:0000259|PROSITE:PS50855" FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:ACT98040.1" FT NON_TER 319 FT /evidence="ECO:0000313|EMBL:ACT98040.1" SQ SEQUENCE 319 AA; 35440 MW; BDE853E42C342F5F CRC64; FWLLPPSLMF LMSASLINQG VGTGWTIYPP LVLYITYPDM SVDMVIFSLH LAGVSSILGA INFISTILNM QQKMMSMEQM PLFPWSILIT AILLLLSLPV LAGAITMLLT DRNFNTSFFD PAGGGDPILF QHLFWFFGHP EVYILILPGF GMISHIISFY ANKKTPFGTL GMIYAMSTIG ILGFVVWAHH SFTIGMDVDT RAYFTSATMI IAVPTGIKIF SWIATLYGSK LTNSPALWWA MGFVFLFTIG GITGVILANS SLDIILHDTY YVVAHFHYVL SMGAVFAIMG GFIHWSPLFI GVEMNKTMLN IQFMIMFIG //