ID B2C412_9APIC Unreviewed; 319 AA. AC B2C412; DT 20-MAY-2008, integrated into UniProtKB/TrEMBL. DT 20-MAY-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=coI {ECO:0000313|EMBL:ABY87003.1}; OS Haemoproteus sp. 2223. OG Mitochondrion {ECO:0000313|EMBL:ABY87003.1}. OC Eukaryota; Alveolata; Apicomplexa; Aconoidasida; Haemosporida; OC Haemoproteidae; Haemoproteus; unclassified 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: 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; EU254600; ABY87003.1; -; 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:ABY87003.1}; 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 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 //