ID E9L181_9HEMI Unreviewed; 216 AA. AC E9L181; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 27-NOV-2024, entry version 52. DE RecName: Full=Cytochrome c oxidase subunit 1 {ECO:0000256|ARBA:ARBA00015947, ECO:0000256|RuleBase:RU000369}; DE EC=7.1.1.9 {ECO:0000256|RuleBase:RU000369}; DE Flags: Fragment; GN Name=COI {ECO:0000313|EMBL:ADK08814.1}; OS Pseudococcus comstocki. OG Mitochondrion {ECO:0000313|EMBL:ADK08814.1}. OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Paraneoptera; Hemiptera; Sternorrhyncha; Coccoidea; OC Pseudococcidae; Pseudococcus. OX NCBI_TaxID=494596 {ECO:0000313|EMBL:ADK08814.1}; RN [1] {ECO:0000313|EMBL:ADK08814.1} RP NUCLEOTIDE SEQUENCE. RA Park D.-S., Oh H.-W., Suh S.-J.; RL Submitted (JUN-2010) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:ADK08814.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=21272395; DOI=10.1017/S0007485310000714; RA Park D.S., Suh S.J., Hebert P.D., Oh H.W., Hong K.J.; RT "DNA barcodes for two scale insect families, mealybugs (Hemiptera: RT Pseudococcidae) and armored scales (Hemiptera: Diaspididae)."; RL Bull. Entomol. Res. 0:0-0(2011). RN [3] {ECO:0000313|EMBL:AST10292.1} RP NUCLEOTIDE SEQUENCE. RA Ren J.-M., Ashfaq M., Hu X.-N., Ma J., Hebert P.D.N.; RT "Barcode Index Numbers Expedite Quarantine Inspections and Aid the RT Interception of Nonindigenous Mealybugs (Pseudococcidae)."; RL Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases. 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] + O2 + 8 H(+)(in) = 4 Fe(III)- CC [cytochrome c] + 2 H2O + 4 H(+)(out); 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 -!- SUBUNIT: Component of the cytochrome c oxidase (complex IV, CIV), a CC multisubunit enzyme composed of a catalytic core of 3 subunits and CC several supernumerary subunits. The complex exists as a monomer or a CC dimer and forms supercomplexes (SCs) in the inner mitochondrial CC membrane with ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 CC complex, complex III, CIII). {ECO:0000256|ARBA:ARBA00011164}. 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; HM474352; ADK08814.1; -; Genomic_DNA. DR EMBL; HM474353; ADK08815.1; -; Genomic_DNA. DR EMBL; HM474354; ADK08816.1; -; Genomic_DNA. DR EMBL; HM474355; ADK08817.1; -; Genomic_DNA. DR EMBL; HM474356; ADK08818.1; -; Genomic_DNA. DR EMBL; HM474357; ADK08819.1; -; Genomic_DNA. DR EMBL; HM474360; ADK08822.1; -; Genomic_DNA. DR EMBL; HM474361; ADK08823.1; -; Genomic_DNA. DR EMBL; HM474364; ADK08826.1; -; Genomic_DNA. DR EMBL; HM474366; ADK08828.1; -; Genomic_DNA. DR EMBL; HM474367; ADK08829.1; -; Genomic_DNA. DR EMBL; KY372433; AST10292.1; -; Genomic_DNA. DR EMBL; KY372445; AST10302.1; -; Genomic_DNA. DR EMBL; KY372548; AST10403.1; -; Genomic_DNA. DR EMBL; KY372630; AST10484.1; -; Genomic_DNA. DR EMBL; KY372673; AST10527.1; -; Genomic_DNA. DR EMBL; KY372745; AST10598.1; -; Genomic_DNA. DR EMBL; KY372824; AST10675.1; -; Genomic_DNA. DR EMBL; KY372830; AST10681.1; -; Genomic_DNA. DR EMBL; KY372859; AST10710.1; -; Genomic_DNA. DR EMBL; KY372915; AST10766.1; -; Genomic_DNA. DR EMBL; KY373034; AST10880.1; -; Genomic_DNA. DR AlphaFoldDB; E9L181; -. DR UniPathway; UPA00705; -. DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell. 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:0015990; P:electron transport coupled proton transport; IEA:TreeGrafter. DR GO; GO:0006123; P:mitochondrial electron transport, cytochrome c to oxygen; IEA:TreeGrafter. 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|ARBA:ARBA00022982, KW ECO:0000256|RuleBase:RU000369}; Heme {ECO:0000256|RuleBase:RU000369}; KW 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|ARBA:ARBA00023128, KW ECO:0000256|RuleBase:RU000369}; KW Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00022792, KW ECO:0000256|RuleBase:RU000369}; KW Respiratory chain {ECO:0000256|ARBA:ARBA00022660, KW ECO:0000256|RuleBase:RU000369}; KW Translocase {ECO:0000256|ARBA:ARBA00022967}; KW Transmembrane {ECO:0000256|RuleBase:RU000369, ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}; KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU000369}. FT TRANSMEM 6..25 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 37..64 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 84..102 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 123..152 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 164..192 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 1..216 FT /note="Cytochrome oxidase subunit I profile" FT /evidence="ECO:0000259|PROSITE:PS50855" FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:ADK08814.1" FT NON_TER 216 FT /evidence="ECO:0000313|EMBL:ADK08814.1" SQ SEQUENCE 216 AA; 25076 MW; 942BEA517B2C45C7 CRC64; LMYLLFGFWS GLMGLSMSFI IRIELMNLNN NFNNNMIYYM MITIHAFMMI FFMTMPIIIG SLSNWLLPLM LMSSDLIFPR LNNFSFWLLI PSLILMMLNM FLNNNINTGW TLYPPLINQN YISLNFIIFS LHLNGISSIF SSINFISSIF IINNNNFLLN NSSLYIWSII ITTILLIISI PILSSAITMI ILDNNLNMNF FNPMGNGNPI LYQHLF //