ID B7UEA1_HYRCU Unreviewed; 511 AA. AC B7UEA1; DT 10-FEB-2009, integrated into UniProtKB/TrEMBL. DT 10-FEB-2009, sequence version 1. DT 07-APR-2021, entry version 55. DE RecName: Full=Cytochrome c oxidase subunit 1 {ECO:0000256|RuleBase:RU000369}; DE EC=7.1.1.9 {ECO:0000256|RuleBase:RU000369}; GN Name=COX1 {ECO:0000313|EMBL:ACK57380.1}; OS Hyriopsis cumingii (Triangle sail mussel) (Unio cumingii). OG Mitochondrion {ECO:0000313|EMBL:ACK57380.1}. OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Bivalvia; OC Autobranchia; Heteroconchia; Palaeoheterodonta; Unionida; Unionoidea; OC Unionidae; Gonideinae; Hyriopsis. OX NCBI_TaxID=165450 {ECO:0000313|EMBL:ACK57380.1}; RN [1] {ECO:0000313|EMBL:ACK57380.1} RP NUCLEOTIDE SEQUENCE. RA Zheng R.L., Li J.L.; RL Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases. 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] + 4 H(+) + O2 = 4 [Fe(III)cytochrome c] CC + 2 H2O; Xref=Rhea:RHEA:11436, Rhea:RHEA-COMP:10350, Rhea:RHEA- CC COMP:14399, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, CC ChEBI:CHEBI:29033, 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|RuleBase:RU000369}; Multi-pass membrane CC protein {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; FJ529186; ACK57380.1; -; Genomic_DNA. DR RefSeq; YP_002427675.1; NC_011763.1. DR GeneID; 7138842; -. DR CTD; 4512; -. 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 Calcium {ECO:0000256|ARBA:ARBA00022837}; KW Copper {ECO:0000256|ARBA:ARBA00023008, 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 ECO:0000256|SAM:Phobius}; Metal-binding {ECO:0000256|RuleBase:RU000369}; KW Mitochondrion {ECO:0000256|RuleBase:RU000369, ECO:0000313|EMBL:ACK57380.1}; 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, ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|RuleBase:RU000369}. FT TRANSMEM 12..34 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 54..79 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 99..123 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 143..168 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 180..207 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 227..252 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 264..288 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 300..323 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 335..356 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 376..397 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 409..430 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 450..470 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 1..510 FT /note="COX1" FT /evidence="ECO:0000259|PROSITE:PS50855" SQ SEQUENCE 511 AA; 56146 MW; 1432D926B65320A8 CRC64; MRWLCSTNHK DIGTLYLLLA LWSGLIGLAL SLLIRAELGQ PGSLLGDDQL YNVIVTAHAF MMIFFLVMPM MIGGFGNWLI PLMIGAPDMA FPRLNNLSFW LLVPALFLLL SSSLVESGVG TGWTVYPPLS GNVAHSGASV DLAIFSLHLA GASSILGAIN FISTVGNMRS PGLVAERIPL FVWAVTVTAI LLVAALPVLA GAITMLLTDR NLNTSFFDPT GGGDPILYMH LFWFFGHPEV YILILPGFGM ISHIVMHYAG KKQVFGYLGM VYAIVSIGVL GFIVWAHHMF TVGMDVDTRA YFTAATMIIA VPTGIKVFSW LATIHGFVNK TEPPILWALG FIFLFTVGGL TGIVLSNSSL DIVLHDTYYV VAHFHYVLSM GAVFALFSAF SYWYPLISGV TFHAVWSKVH FVLMFVGVNL TFFPQHFLGL AGMPRRYSDY PDSFAKWNVV SSWGSLISFV SVLLFMFMLL ESFVSQRSVV WGSALSSSFE WQDANFPASF HSNSQMAKVF V //