ID A0A146J9L1_9INSE Unreviewed; 153 AA. AC A0A146J9L1; DT 08-JUN-2016, integrated into UniProtKB/TrEMBL. DT 08-JUN-2016, sequence version 1. DT 24-JAN-2024, entry version 28. DE RecName: Full=Cytochrome c oxidase subunit 1 {ECO:0000256|ARBA:ARBA00015947, ECO:0000256|RuleBase:RU000369}; DE EC=7.1.1.9 {ECO:0000256|ARBA:ARBA00012949, ECO:0000256|RuleBase:RU000369}; DE Flags: Fragment; GN Name=COI {ECO:0000313|EMBL:BAU79679.1}; OS Isonychia ignota. OG Mitochondrion {ECO:0000313|EMBL:BAU79679.1}. OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Palaeoptera; Ephemeroptera; Setisura; Isonychiidae; Isonychia. OX NCBI_TaxID=764591 {ECO:0000313|EMBL:BAU79679.1}; RN [1] {ECO:0000313|EMBL:BAU79679.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=12431 {ECO:0000313|EMBL:BAU79675.1}, 12432 RC {ECO:0000313|EMBL:BAU79676.1}, 12433 {ECO:0000313|EMBL:BAU79677.1}, RC 12934 {ECO:0000313|EMBL:BAU79678.1}, and 12935 RC {ECO:0000313|EMBL:BAU79679.1}; RA Saito R., Jo J., Sekine K., Bae Y.J., Tojo K.; RT "Phylogenetic analyses of the isonychiid mayflies (Ephemeroptera: RT Isonychiidae) in the northeast palearctic region."; RL Entomol. Res. 0:0-0(2016). 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|ARBA:ARBA00029331}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11437; CC Evidence={ECO:0000256|ARBA:ARBA00029331}; CC -!- COFACTOR: CC Name=heme; Xref=ChEBI:CHEBI:30413; CC Evidence={ECO:0000256|ARBA:ARBA00001971}; CC -!- PATHWAY: Energy metabolism; oxidative phosphorylation. CC {ECO:0000256|ARBA:ARBA00004673, ECO:0000256|RuleBase:RU000369}. CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane CC {ECO:0000256|ARBA:ARBA00004448, ECO:0000256|RuleBase:RU000369}; Multi- CC pass membrane protein {ECO:0000256|ARBA:ARBA00004448, CC ECO:0000256|RuleBase:RU000369}. CC -!- SIMILARITY: Belongs to the heme-copper respiratory oxidase family. CC {ECO:0000256|ARBA:ARBA00009578, 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; LC114396; BAU79675.1; -; Genomic_DNA. DR EMBL; LC114397; BAU79676.1; -; Genomic_DNA. DR EMBL; LC114398; BAU79677.1; -; Genomic_DNA. DR EMBL; LC114399; BAU79678.1; -; Genomic_DNA. DR EMBL; LC114400; BAU79679.1; -; Genomic_DNA. DR AlphaFoldDB; A0A146J9L1; -. 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 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. 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:BAU79679.1}; KW Mitochondrion inner membrane {ECO:0000256|RuleBase:RU000369}; KW Respiratory chain {ECO:0000256|RuleBase:RU000369}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|RuleBase:RU000369, ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}; KW Transport {ECO:0000256|RuleBase:RU000369}. FT SIGNAL 1..36 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 37..153 FT /note="Cytochrome c oxidase subunit 1" FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5007995785" FT TRANSMEM 58..84 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 96..123 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 1..153 FT /note="Cytochrome oxidase subunit I profile" FT /evidence="ECO:0000259|PROSITE:PS50855" FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:BAU79679.1" FT NON_TER 153 FT /evidence="ECO:0000313|EMBL:BAU79679.1" SQ SEQUENCE 153 AA; 16281 MW; 2EF77BAC71820029 CRC64; GAPDMAFPRM NNMSFWLLPP ALTLLLASSM VESGAGTGWT VYPPLSAGIA HAGASVDLAI FSLHLAGVSS ILGAVNFITT TINMRSSGMT MDRVPLFVWS VIITAILLLL SLPVLAGAIT MLLTDRNLNT SFFDPAGGGD PILYQHLFWF FGH //