ID B3XYB8_9APIC Unreviewed; 477 AA. AC B3XYB8; DT 23-SEP-2008, integrated into UniProtKB/TrEMBL. DT 23-SEP-2008, sequence version 1. DT 11-DEC-2019, entry version 44. 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=cox1 {ECO:0000313|EMBL:BAG68543.1}; OS Plasmodium fieldi. OG Mitochondrion {ECO:0000313|EMBL:BAG68543.1}. OC Eukaryota; Alveolata; Apicomplexa; Aconoidasida; Haemosporida; OC Plasmodiidae; Plasmodium; Plasmodium (Plasmodium). OX NCBI_TaxID=77518 {ECO:0000313|EMBL:BAG68543.1}; RN [1] {ECO:0000313|EMBL:BAG68543.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=18687771; DOI=10.1093/molbev/msn171; RA Hayakawa T., Culleton R., Otani H., Horii T., Tanabe K.; RT "Big bang in the evolution of extant malaria parasites."; RL Mol. Biol. Evol. 25:2233-2239(2008). 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; AB354574; BAG68543.1; -; 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:BAG68543.1}; 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 20..39 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 59..78 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 108..128 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 148..172 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 193..217 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 250..267 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 279..297 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 309..334 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 346..370 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 382..403 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 415..438 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 458..476 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 3..477 FT /note="COX1" FT /evidence="ECO:0000259|PROSITE:PS50855" FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:BAG68543.1" SQ SEQUENCE 477 AA; 52967 MW; ADB1A1806F6C0BA8 CRC64; FFVLNRYTLI TNCNHKTLGL YYLWFSFLFG SYGFLLSVIL RTELYSSSLR IIAQENVNLY NMIFTLHGII MIFFNIMPGL FGGFGNYFLP ILCGSPELAY PRINSISLLL QPIAFILVIL STAAEFGGGT GWTLYPPLST SLMSLSPVAV DVIIVGLLVS GIASIMSSLN FITTVMHLRS KGLTLGILSV STWSLIITSV MLLLTLPVLT GGVLMLLSDL HFNTLFFDPT FAGDPILYQH LFWFFGHPEV YILILPAFGV ISHVISTNYC RSLFGNQSMI LAMSCIAILG SVVWAHHMYT TGLEVDTRAF FTSTTILISI PTGTKIFNWI CTYMGSNFGI THSSSLLSLL FICTFTFGGT TGVILGNAAI DIALHDTYYV IAHFHFVLSI GAIIGLFTLV SSFQENFFGK HLRENSIIIL WSILFFIGVV LTFLPMHFLG FNVMPRRIPD YPDALNGWNM ICSIGSTMTL FGLFIFK //