ID B7UEA1_HYRCU Unreviewed; 511 AA. AC B7UEA1; DT 10-FEB-2009, integrated into UniProtKB/TrEMBL. DT 10-FEB-2009, sequence version 1. DT 15-FEB-2017, entry version 38. 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:ACK57380.1}; OS Hyriopsis cumingii (Triangle sail mussel) (Unio cumingii). OG Mitochondrion {ECO:0000313|EMBL:ACK57380.1}. OC Eukaryota; Metazoa; Lophotrochozoa; Mollusca; Bivalvia; OC Palaeoheterodonta; Unionoida; Unionoidea; Unionidae; Gonideinae; OC 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: 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 ECO:0000256|SAAS:SAAS00672464}. CC -!- PATHWAY: Energy metabolism; oxidative phosphorylation. CC {ECO:0000256|RuleBase:RU000369, ECO:0000256|SAAS:SAAS00672508}. 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; 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: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 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; 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:SAAS00675112}; 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:0000256|SAAS:SAAS00672487, ECO:0000313|EMBL:ACK57380.1}; 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 12 34 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 54 79 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 99 123 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 143 168 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 180 207 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 227 252 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 264 288 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 300 323 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 335 356 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 376 397 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 409 430 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 450 470 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 1 510 COX1. {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 //