ID A0A7D2N5E5_9APIC Unreviewed; 381 AA. AC A0A7D2N5E5; DT 02-DEC-2020, integrated into UniProtKB/TrEMBL. DT 02-DEC-2020, sequence version 1. DT 10-FEB-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}; DE Flags: Fragment; GN Name=cox1 {ECO:0000313|EMBL:QIR82920.1}; OS Plasmodium cynomolgi. OG Mitochondrion {ECO:0000313|EMBL:QIR82920.1}. OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida; OC Plasmodiidae; Plasmodium; Plasmodium (Plasmodium). OX NCBI_TaxID=5827 {ECO:0000313|EMBL:QIR82920.1}; RN [1] {ECO:0000313|EMBL:QIR82920.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=K222 {ECO:0000313|EMBL:QIR82920.1}; RA Nada Raja T., Kadir K.A., Hu T.H., Awang Mohamad D.S., Rosli N., Wong L.L., RA Hii K.C., Divis P.C.S., Singh B.; RL Submitted (AUG-2019) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:QIR82920.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=K222 {ECO:0000313|EMBL:QIR82920.1}; RX PubMed=32687020; RA Raja T.N., Hu T.H., Kadir K.A., Mohamad D.S.A., Rosli N., Wong L.L., RA Hii K.C., Simon Divis P.C., Singh B.; RT "Naturally Acquired Human Plasmodium cynomolgi and P. knowlesi Infections, RT Malaysian Borneo."; RL Emerg. Infect. Dis. 26:1801-1809(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; MN372335; QIR82920.1; -; 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 ECO:0000256|SAM:Phobius}; Metal-binding {ECO:0000256|RuleBase:RU000369}; KW Mitochondrion {ECO:0000256|RuleBase:RU000369, ECO:0000313|EMBL:QIR82920.1}; 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, ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|RuleBase:RU000369}. FT TRANSMEM 16..36 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 56..84 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 104..124 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 144..168 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 189..213 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 246..263 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 275..293 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 305..330 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 342..366 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 1..381 FT /note="COX1" FT /evidence="ECO:0000259|PROSITE:PS50855" FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:QIR82920.1" FT NON_TER 381 FT /evidence="ECO:0000313|EMBL:QIR82920.1" SQ SEQUENCE 381 AA; 42019 MW; 9EA7EFEFF1D9422D CRC64; NRYTLITNCN HKTLGLYYLW FSFLFGSYGF LLSVILRTEL YSSSLRIIAQ ENVNLYNMIF TLHGIIMIFF NIMPGLFGGF GNYFLPILCG SPELAYPRIN SISLLFQPIA FILVILSTAA EFGGGTGWTL YPPLSTSLMS LSPVAVDVII VGLLVSGIAS IMSSLNFITT VMHLRSKGLT LGILSVSTWS LIITSVMLLL TLPVLTGGVL MLLSDLHFNT LFFDPTFAGD PILYQHLFWF FGHPEVYILI LPAFGVISHV ISTNYCRSLF GNQSMILAMS CIAILGSVVW AHHMYTTGLE VDTRAFFTST TILISIPTGT KIFNWICTYM GSNFGITHSS SLLSLLFICT FTFGGTTGVI LGNAAIDIAL HDTYYVIAHF H //