ID H6U2B4_9DINO Unreviewed; 351 AA. AC H6U2B4; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 14-OCT-2015, entry version 19. 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=COI {ECO:0000313|EMBL:AEM91567.1}; OS Symbiodinium sp. F5.1. OG Mitochondrion {ECO:0000313|EMBL:AEM91567.1}. OC Eukaryota; Alveolata; Dinophyceae; Suessiales; Symbiodiniaceae; OC Symbiodinium. OX NCBI_TaxID=452047 {ECO:0000313|EMBL:AEM91567.1}; RN [1] {ECO:0000313|EMBL:AEM91567.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=22238660; DOI=10.1371/journal.pone.0029816; RA Pochon X., Putnam H.M., Burki F., Gates R.D.; RT "Identifying and characterizing alternative molecular markers for the RT symbiotic and free-living dinoflagellate genus Symbiodinium."; RL PLoS ONE 7:E29816-E29816(2012). 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; JN557898; AEM91567.1; -; 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; IPR023615; Cyt_c_Oxase_su1_BS. 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. 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}; 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:AEM91567.1}; 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 33 58 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 78 102 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 122 147 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 159 186 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 219 242 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 249 266 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 278 300 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 321 341 Helical. {ECO:0000256|SAM:Phobius}. FT NON_TER 1 1 {ECO:0000313|EMBL:AEM91567.1}. FT NON_TER 351 351 {ECO:0000313|EMBL:AEM91567.1}. SQ SEQUENCE 351 AA; 38997 MW; A3D854B436736F6F CRC64; SGTLISVLIR IELYSSGNRI ISPENQNFYN ISITLHGFLM IFFLVMPGLF GGFGNYFLPI FQGSPEVVYP RVNNFSILIL LLSYLFLILS LISEFGGGTG WTVYPPLSTS FMTLSPSSIG NLIFGLIISG ISSCLTSLNF WTTIHFLRSY YLILSSIPLF PWAFLITAFM LLLTLPILSG TLLLILGDLH SNTLFFDPIF GGDPIFYQHL FWFFGHPEVY ILIIPAFGII SIIISGILQL IIFANQSMIF AMSSISLLGG LVWGHHMYTV GLESDTRAYF TGVTILISLP TGTKIFNWLF TYLSNPPLLH LRITSVFLSH LFLLMFTIGG STGIILGNGA VDLGLHDTYY V //