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Q9B229

- COX1_CHRKN

UniProt

Q9B229 - COX1_CHRKN

Protein

Cytochrome c oxidase subunit 1

Gene

COI

Organism
Chrysomela knabi (Leaf beetle)
Status
Reviewed - Annotation score: 4 out of 5- Protein inferred from homologyi
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    • History
      Entry version 62 (01 Oct 2014)
      Sequence version 2 (16 Aug 2004)
      Previous versions | rss
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    Functioni

    Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits 1-3 form the functional core of the enzyme complex. CO I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c are transferred via the copper A center of subunit 2 and heme A of subunit 1 to the bimetallic center formed by heme A3 and copper B.

    Catalytic activityi

    4 ferrocytochrome c + O2 + 4 H+ = 4 ferricytochrome c + 2 H2O.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi147 – 1471Copper BBy similarityCurated
    Metal bindingi151 – 1511Copper BBy similarityCurated
    Metal bindingi197 – 1971Copper BBy similarityCurated
    Metal bindingi198 – 1981Copper BBy similarityCurated

    GO - Molecular functioni

    1. cytochrome-c oxidase activity Source: UniProtKB-EC
    2. heme binding Source: InterPro
    3. iron ion binding Source: InterPro

    GO - Biological processi

    1. aerobic respiration Source: InterPro
    2. oxidative phosphorylation Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Electron transport, Respiratory chain, Transport

    Keywords - Ligandi

    Copper, Heme, Iron, Metal-binding

    Enzyme and pathway databases

    UniPathwayiUPA00705.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Cytochrome c oxidase subunit 1 (EC:1.9.3.1)
    Alternative name(s):
    Cytochrome c oxidase polypeptide I
    Gene namesi
    Name:COIImported
    Encoded oniMitochondrionImported
    OrganismiChrysomela knabi (Leaf beetle)
    Taxonomic identifieri153783 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaColeopteraPolyphagaCucujiformiaChrysomeloideaChrysomelidaeChrysomelinaeChrysomeliniChrysomela

    Subcellular locationi

    GO - Cellular componenti

    1. integral component of membrane Source: UniProtKB-KW
    2. mitochondrial inner membrane Source: UniProtKB-SubCell
    3. respiratory chain Source: UniProtKB-KW

    Keywords - Cellular componenti

    Membrane, Mitochondrion, Mitochondrion inner membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini‹1 – ›219›219Cytochrome c oxidase subunit 1PRO_0000183314Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Cross-linki147 ↔ 1511'-histidyl-3'-tyrosine (His-Tyr)By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliQ9B229.
    SMRiQ9B229. Positions 1-219.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini‹1 – 1›1Mitochondrial matrixBy similarity
    Topological domaini25 – 4723Mitochondrial intermembraneBy similarityAdd
    BLAST
    Topological domaini78 – 8912Mitochondrial matrixBy similarityAdd
    BLAST
    Topological domaini120 – 13415Mitochondrial intermembraneBy similarityAdd
    BLAST
    Topological domaini169 – 1768Mitochondrial matrixBy similarity
    Topological domaini194 – 20512Mitochondrial intermembraneBy similarityAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei2 – 2423Helical; Name=IIIBy similarityAdd
    BLAST
    Transmembranei48 – 7730Helical; Name=IVBy similarityAdd
    BLAST
    Transmembranei90 – 11930Helical; Name=VBy similarityAdd
    BLAST
    Transmembranei135 – 16834Helical; Name=VIBy similarityAdd
    BLAST
    Transmembranei177 – 19317Helical; Name=VIIBy similarityAdd
    BLAST
    Transmembranei206 – ›219›14Helical; Name=VIIIBy similarityAdd
    BLAST

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the heme-copper respiratory oxidase family.UniRule annotation

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Family and domain databases

    Gene3Di1.20.210.10. 1 hit.
    InterProiIPR000883. COX1.
    IPR023615. Cyt_c_Oxase_su1_BS.
    IPR023616. Cyt_c_Oxase_su1_dom.
    [Graphical view]
    PANTHERiPTHR10422. PTHR10422. 1 hit.
    PfamiPF00115. COX1. 1 hit.
    [Graphical view]
    PRINTSiPR01165. CYCOXIDASEI.
    SUPFAMiSSF81442. SSF81442. 1 hit.
    PROSITEiPS50855. COX1. 1 hit.
    PS00077. COX1_CUB. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Fragment.

    Q9B229-1 [UniParc]FASTAAdd to Basket

    « Hide

    FPRMNNMSFW LLPPSLFLLI MSSIVENGAG TGWTVYPPLS SNIAHGGSSV    50
    DLAIFSLHLA GISSILGAIN FITTVINMRP MGMKLDRMPL FVWAVVITAI 100
    LLLLSLPVLA GAITMLLTDR NLNTSFFDPA GGGDPILYQH LFWFFGHPEV 150
    YILILPGFGM ISHIISQESS KKEVFGTLGM IYAMMAIGLL GFIVWAHHMF 200
    TVGMDVDTQT YFTSATMII 219
    Length:219
    Mass (Da):24,021
    Last modified:August 16, 2004 - v2
    Checksum:i93BD81BF4358C92D
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Non-terminal residuei1 – 11Imported
    Sequence conflicti20 – 201I → L in AAK16643. (PubMed:11259651)Curated
    Sequence conflicti41 – 466SNIAHG → ANTAHS in AAK16643. (PubMed:11259651)Curated
    Sequence conflicti81 – 888MGMKLDRM → EGMNFEQT in AAK16643. (PubMed:11259651)Curated
    Sequence conflicti96 – 961V → L in AAK16643. (PubMed:11259651)Curated
    Non-terminal residuei219 – 2191Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY242402 Genomic DNA. Translation: AAP13120.1.
    AY027627 Genomic DNA. Translation: AAK16643.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY242402 Genomic DNA. Translation: AAP13120.1 .
    AY027627 Genomic DNA. Translation: AAK16643.1 .

    3D structure databases

    ProteinModelPortali Q9B229.
    SMRi Q9B229. Positions 1-219.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    UniPathwayi UPA00705 .

    Family and domain databases

    Gene3Di 1.20.210.10. 1 hit.
    InterProi IPR000883. COX1.
    IPR023615. Cyt_c_Oxase_su1_BS.
    IPR023616. Cyt_c_Oxase_su1_dom.
    [Graphical view ]
    PANTHERi PTHR10422. PTHR10422. 1 hit.
    Pfami PF00115. COX1. 1 hit.
    [Graphical view ]
    PRINTSi PR01165. CYCOXIDASEI.
    SUPFAMi SSF81442. SSF81442. 1 hit.
    PROSITEi PS50855. COX1. 1 hit.
    PS00077. COX1_CUB. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Convergent evolution of cucurbitacin feeding in spatially isolated rootworm taxa (Coleoptera: Chrysomelidae; Galerucinae, Luperini)."
      Gillespie J.J., Kjer K.M., Duckett C.N., Tallamy D.W.
      Mol. Phylogenet. Evol. 29:161-175(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-154.
      Strain: Isolate JJG2371 Publication.
    2. "Feeding specialization and host-derived chemical defense in Chrysomeline leaf beetles did not lead to an evolutionary dead end."
      Termonia A., Hsiao T.H., Pasteels J.M., Milinkovitch M.C.
      Proc. Natl. Acad. Sci. U.S.A. 98:3909-3914(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 10-219.

    Entry informationi

    Entry nameiCOX1_CHRKN
    AccessioniPrimary (citable) accession number: Q9B229
    Secondary accession number(s): Q85KD6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 16, 2004
    Last sequence update: August 16, 2004
    Last modified: October 1, 2014
    This is version 62 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)

    Miscellaneousi

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3