ID E9L181_9HEMI Unreviewed; 216 AA. AC E9L181; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 22-APR-2020, entry version 35. 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: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] + 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; 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; 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 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 PANTHER; PTHR10422; PTHR10422; 1. DR Pfam; PF00115; COX1; 1. DR PRINTS; PR01165; CYCOXIDASEI. DR SUPFAM; SSF81442; SSF81442; 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:ADK08814.1}; 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..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="COX1" 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 //