ID B3XYB8_9APIC Unreviewed; 477 AA. AC B3XYB8; DT 23-SEP-2008, integrated into UniProtKB/TrEMBL. DT 23-SEP-2008, sequence version 1. DT 22-FEB-2023, entry version 52. DE RecName: Full=Cytochrome c oxidase subunit 1 {ECO:0000256|RuleBase:RU000369}; DE EC=7.1.1.9 {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; Sar; 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: 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] + 8 H(+)(in) + O2 = 4 Fe(III)- CC [cytochrome c] + 4 H(+)(out) + 2 H2O; Xref=Rhea:RHEA:11436, CC Rhea:RHEA-COMP:10350, Rhea:RHEA-COMP:14399, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:29033, CC ChEBI:CHEBI:29034; EC=7.1.1.9; CC Evidence={ECO:0000256|RuleBase:RU000369}; CC -!- PATHWAY: Energy metabolism; oxidative phosphorylation. CC {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|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 AlphaFoldDB; B3XYB8; -. DR UniPathway; UPA00705; -. 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:0006119; P:oxidative phosphorylation; IEA:UniProtKB-UniPathway. DR Gene3D; 1.20.210.10; Cytochrome c oxidase-like, subunit I domain; 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; CYTOCHROME C OXIDASE SUBUNIT 1; 1. DR PANTHER; PTHR10422:SF18; CYTOCHROME C OXIDASE SUBUNIT 1; 1. DR Pfam; PF00115; COX1; 1. DR PRINTS; PR01165; CYCOXIDASEI. DR SUPFAM; SSF81442; Cytochrome c oxidase subunit I-like; 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|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU000369}; 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 Respiratory chain {ECO:0000256|RuleBase:RU000369}; KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, KW ECO:0000256|RuleBase:RU000369}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, KW ECO:0000256|SAM:Phobius}; 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="Cytochrome oxidase subunit I profile" 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 //