ID B2C412_9APIC Unreviewed; 319 AA. AC B2C412; DT 20-MAY-2008, integrated into UniProtKB/TrEMBL. DT 20-MAY-2008, sequence version 1. DT 14-DEC-2022, 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=coI {ECO:0000313|EMBL:ABY87003.1}; OS Haemoproteus sp. 2223. OG Mitochondrion {ECO:0000313|EMBL:ABY87003.1}. OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida; OC Haemoproteidae; Haemoproteus. OX NCBI_TaxID=498819 {ECO:0000313|EMBL:ABY87003.1}; RN [1] {ECO:0000313|EMBL:ABY87003.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=18248741; DOI=10.1016/j.ympev.2007.11.012; RA Martinsen E.S., Perkins S.L., Schall J.J.; RT "A three-genome phylogeny of malaria parasites (Plasmodium and closely RT related genera): evolution of life-history traits and host switches."; RL Mol. Phylogenet. Evol. 47:261-273(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; EU254600; ABY87003.1; -; Genomic_DNA. DR AlphaFoldDB; B2C412; -. 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; -; 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 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:ABY87003.1}; 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 6..27 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 39..59 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 79..99 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 120..144 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 164..188 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 200..224 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 236..260 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 272..297 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 1..319 FT /note="COX1" FT /evidence="ECO:0000259|PROSITE:PS50855" FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:ABY87003.1" FT NON_TER 319 FT /evidence="ECO:0000313|EMBL:ABY87003.1" SQ SEQUENCE 319 AA; 34382 MW; F589026D5239EDCC CRC64; FNIMPGLFGG FGNYFLPILC GSSELAYPRL NSISLLLQPV AFGLVILSTA AEFGGGTGWT LYPPLSTSLM SLSPVAVDVI VIGLLVSGIA SIMSSLNFLT TVIHLRAKGL TLGILSVSTW SIVLTAVMLL FTLPVLTGGV LMLLSDLHFN TLFYDPTFSG DPVLYQHLFW FFGHPEVYIL ILPAFGVISH VISTNYCRSL FGNQSMILAM ACIAVLGSIV WAHHMYTTGL EVDTRAYFTS TTILISIPTG TKVLTGLCTY MSSNFGITHN SCLLALLFKC TFTFGGTTGV ILGNAAIDIA LHDTYYVIAH FHFVYTIGA //