ID A0A7G9UKS7_9APIC Unreviewed; 477 AA. AC A0A7G9UKS7; DT 10-FEB-2021, integrated into UniProtKB/TrEMBL. DT 10-FEB-2021, sequence version 1. DT 07-APR-2021, entry version 2. DE RecName: Full=Cytochrome c oxidase subunit 1 {ECO:0000256|RuleBase:RU000369}; DE EC=7.1.1.9 {ECO:0000256|RuleBase:RU000369}; GN Name=cox1 {ECO:0000313|EMBL:QNN94628.1}; OS Haemoproteus sp. OG Mitochondrion {ECO:0000313|EMBL:QNN94628.1}. OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida; OC Haemoproteidae; Haemoproteus; unclassified Haemoproteus. OX NCBI_TaxID=191679 {ECO:0000313|EMBL:QNN94628.1}; RN [1] {ECO:0000313|EMBL:QNN94628.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Kaz18 {ECO:0000313|EMBL:QNN94628.1}; RX PubMed=32866615; RA Ciloglu A., Ellis V.A., Duc M., Downing P.A., Inci A., Bensch S.; RT "Evolution of vector transmitted parasites by host switching revealed RT through sequencing of Haemoproteus parasite mitochondrial genomes."; RL Mol. Phylogenet. Evol. 106947:0-0(2020). 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] + 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=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; MT513726; QNN94628.1; -; Genomic_DNA. DR UniPathway; UPA00705; -. DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-KW. 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|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU000369}; KW Metal-binding {ECO:0000256|RuleBase:RU000369}; KW Mitochondrion {ECO:0000256|RuleBase:RU000369, ECO:0000313|EMBL:QNN94628.1}; 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 113..132 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 152..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 237..261 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 273..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:QNN94628.1" SQ SEQUENCE 477 AA; 52844 MW; 2FBF83CF95AE3568 CRC64; FIVLQRYTLI TNCNHKTLGL YYLWFSFLFG SYGFLLSVII RTELYSSSLR IIAQENVNFY NMIFTIHGII MIFFNIMPGL FGGFGNYFLP ILCGSSELAY PRINSISLLL QPIAFGLVIL STTAEFGGGT GWTLYPPLST SLMSLSPVAV DVIVIGLLVS GVASIMSSLN FLTTVVHLRA KGLTLGILSV STWSIVITSV MLLLTLPVLT GGVLMLLSDL HFNTLFYDPT FSGDPVLYQH LFWFFGHPEV YILILPAFGI ISHVISTNYC RSLFGNQSMI LAMACIAVLG SIVWAHHMYT TGLEVDTRAY FTSTTILISI PTGTKVFNWL CTYMSSNFGI THNSSLLALL FICTFTFGGT TGVILGNAAI DIALHDTYYV IAHFHFVLSI GAIIGVFTAV SAFQENYFGK NLRDNTIIIL WIMLFFVGVV LTFLPMHFLG FNVMPRRIPD YPDALNGWNM ICSIGSTMTL FGLLIFK //