ID H6U2A7_9DINO Unreviewed; 352 AA. AC H6U2A7; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 11-DEC-2019, entry version 30. 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:AEM91560.1}; OS Cladocopium sp. C1. OG Mitochondrion {ECO:0000313|EMBL:AEM91560.1}. OC Eukaryota; Alveolata; Dinophyceae; Suessiales; Symbiodiniaceae; OC Cladocopium; unclassified Cladocopium; Cladocopium sp. clade C. OX NCBI_TaxID=2558453 {ECO:0000313|EMBL:AEM91560.1}; RN [1] {ECO:0000313|EMBL:AEM91560.1} 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 1-3 CC form the functional core of the enzyme complex. CO I is the catalytic CC subunit of the enzyme. Electrons originating in cytochrome c are CC transferred via the copper A center of subunit 2 and heme A of subunit CC 1 to the bimetallic center formed by heme A3 and copper B. CC {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=1.9.3.1; CC Evidence={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; JN557891; AEM91560.1; -; 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: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; 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|RuleBase:RU000369, ECO:0000256|SAM:Phobius}; KW Metal-binding {ECO:0000256|RuleBase:RU000369}; KW Mitochondrion {ECO:0000256|RuleBase:RU000369, ECO:0000313|EMBL:AEM91560.1}; 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, ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}; KW Transport {ECO:0000256|RuleBase:RU000369}. FT TRANSMEM 33..58 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 78..103 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 123..147 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 159..186 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 219..242 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 249..266 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 278..300 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 321..341 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 1..352 FT /note="COX1" FT /evidence="ECO:0000259|PROSITE:PS50855" FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:AEM91560.1" FT NON_TER 352 FT /evidence="ECO:0000313|EMBL:AEM91560.1" SQ SEQUENCE 352 AA; 39084 MW; 5480C0B15C64FA36 CRC64; SGTLISVLIR IELYSSGNRI ISPENQNFYN ISITLHGFLM IFFLVMPGLF GGFGNYFVPI FQGSPEVVYP RVNNFSILIL LLSYLFLILS LISEFGGGTG WTLYPPLSTS FMTLSPSSTG NLIFGLIISG ISSCLTSLNF WTTIHFLRSY YLILSSIPLF PWAFLITAFM LLLTLPILSG TLLLILGDLH SNTLFFDPIF GGDPIFYQHL FWFFGHPEVY ILIIPAFGII SIIISGILQL IIFANQSMIF AMSSISLLGG LVWGHHMYTV GLESDTRAYF TGVTILISLP TGTKIFNWLF TYLSNPPLLH LRITSVFLSH LFLLMFTIGG STGIILGNGA VDLGLHDTYY VV //