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P24010

- COX1_BACSU

UniProt

P24010 - COX1_BACSU

Protein

Cytochrome c oxidase subunit 1

Gene

ctaD

Organism
Bacillus subtilis (strain 168)
Status
Reviewed - Annotation score: 5 out of 5- Protein inferred from homologyi
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    • History
      Entry version 127 (01 Oct 2014)
      Sequence version 3 (16 Jun 2009)
      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. This cytochrome c oxidase shows proton pump activity across the membrane in addition to the electron transfer.

    Catalytic activityi

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

    Cofactori

    Binds 1 copper B ion per subunit.
    Binds 2 heme groups per subunit.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi73 – 731Iron (heme A axial ligand)Curated
    Metal bindingi249 – 2491Copper BCurated
    Metal bindingi253 – 2531Copper BCurated
    Metal bindingi298 – 2981Copper BCurated
    Metal bindingi299 – 2991Copper BCurated
    Metal bindingi384 – 3841Iron (heme A3 axial ligand)Curated
    Metal bindingi386 – 3861Iron (heme A axial ligand)Curated

    GO - Molecular functioni

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

    GO - Biological processi

    1. aerobic respiration Source: InterPro
    2. electron transport chain Source: InterPro
    3. oxidative phosphorylation Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Electron transport, Hydrogen ion transport, Ion transport, Respiratory chain, Transport

    Keywords - Ligandi

    Copper, Heme, Iron, Metal-binding

    Enzyme and pathway databases

    BioCyciBSUB:BSU14900-MONOMER.
    RETL1328306-WGS:GSTH-6904-MONOMER.
    UniPathwayiUPA00705.

    Protein family/group databases

    TCDBi3.D.4.4.1. the proton-translocating cytochrome oxidase (cox) superfamily.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Cytochrome c oxidase subunit 1 (EC:1.9.3.1)
    Alternative name(s):
    Caa-3605 subunit 1
    Cytochrome aa3 subunit 1
    Cytochrome c oxidase polypeptide I
    Oxidase aa(3) subunit 1
    Gene namesi
    Name:ctaD
    Ordered Locus Names:BSU14900
    OrganismiBacillus subtilis (strain 168)
    Taxonomic identifieri224308 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
    ProteomesiUP000001570: Chromosome

    Organism-specific databases

    GenoListiBSU14900. [Micado]

    Subcellular locationi

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Cell membrane, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 622622Cytochrome c oxidase subunit 1PRO_0000183436Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Cross-linki249 ↔ 2531'-histidyl-3'-tyrosine (His-Tyr)By similarity

    Proteomic databases

    PaxDbiP24010.

    Interactioni

    Protein-protein interaction databases

    STRINGi224308.BSU14900.

    Structurei

    3D structure databases

    ProteinModelPortaliP24010.
    SMRiP24010. Positions 22-516.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 2727ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini47 – 6822CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini89 – 11022ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini129 – 15931CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini179 – 19618ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini216 – 24126CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini262 – 28423ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini305 – 3128CytoplasmicSequence Analysis
    Topological domaini332 – 34615ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini367 – 3748CytoplasmicSequence Analysis
    Topological domaini395 – 42127ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini442 – 45918CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini480 – 55273ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini573 – 5808CytoplasmicSequence Analysis
    Topological domaini605 – 62218CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei28 – 4619HelicalSequence AnalysisAdd
    BLAST
    Transmembranei69 – 8820HelicalSequence AnalysisAdd
    BLAST
    Transmembranei111 – 12818HelicalSequence AnalysisAdd
    BLAST
    Transmembranei160 – 17819HelicalSequence AnalysisAdd
    BLAST
    Transmembranei197 – 21519HelicalSequence AnalysisAdd
    BLAST
    Transmembranei242 – 26120HelicalSequence AnalysisAdd
    BLAST
    Transmembranei285 – 30420HelicalSequence AnalysisAdd
    BLAST
    Transmembranei313 – 33119HelicalSequence AnalysisAdd
    BLAST
    Transmembranei347 – 36620HelicalSequence AnalysisAdd
    BLAST
    Transmembranei375 – 39420HelicalSequence AnalysisAdd
    BLAST
    Transmembranei422 – 44120HelicalSequence AnalysisAdd
    BLAST
    Transmembranei460 – 47920HelicalSequence AnalysisAdd
    BLAST
    Transmembranei553 – 57220HelicalSequence AnalysisAdd
    BLAST
    Transmembranei581 – 60424HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG0843.
    HOGENOMiHOG000085275.
    KOiK02274.
    OrthoDBiEOG6B35XR.
    PhylomeDBiP24010.

    Family and domain databases

    Gene3Di1.20.210.10. 1 hit.
    InterProiIPR000883. COX1.
    IPR023615. Cyt_c_Oxase_su1_BS.
    IPR023616. Cyt_c_Oxase_su1_dom.
    IPR014241. Cyt_c_oxidase_su1_bac.
    [Graphical view]
    PANTHERiPTHR10422. PTHR10422. 1 hit.
    PfamiPF00115. COX1. 1 hit.
    [Graphical view]
    PRINTSiPR01165. CYCOXIDASEI.
    SUPFAMiSSF81442. SSF81442. 1 hit.
    TIGRFAMsiTIGR02891. CtaD_CoxA. 1 hit.
    PROSITEiPS50855. COX1. 1 hit.
    PS00077. COX1_CUB. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P24010-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLNALTEKRT RGSMLWDYLT TVDHKKIAIL YLVAGGFFFL VGGIEAMFIR    50
    IQLAKPENAF LSAQAYNEVM TMHGTTMIFL AAMPLLFALM NAVVPLQIGA 100
    RDVSFPFLNA LGFWLFFFGG IFLNLSWFLG GAPDAGWTSY ASLSLHSKGH 150
    GIDFFVLGLQ ISGLGTLIAG INFLATIINM RAPGMTYMRL PLFTWTTFVA 200
    SALILFAFPP LTVGLALMML DRLFGTNFFN PELGGNTVIW EHLFWIFGHP 250
    EVYILILPAF GIFSEVIPVF ARKRLFGYSS MVFAIVLIGF LGFMVWVHHM 300
    FTTGLGPIAN AIFAVATMAI AIPTGIKIFN WLLTIWGGNV KYTTAMLYAV 350
    SFIPSFVLGG VTGVMLAAAA ADYQFHDTYF VVAHFHYVII GGVVFGLLAG 400
    VHFWWPKMFG KILHETMGKI SFVLFFIGFH LTFFIQHFVG LMGMPRRVYT 450
    FLPGQGLETG NLISTIGAFF MAAAVILLLV NVIWTSVKGE YVGADPWHDG 500
    RTLEWTVSSP PPEYNFKQLP FVRGLDPLWI EKQAGHKSMT PAEPVDDIHM 550
    PNGSILPLII SFGLFVAAFG LLYRSDYAWG LPVIFIGLGI TFITMLLRSV 600
    IDDHGYHIHK EELPNDDKGV KA 622
    Length:622
    Mass (Da):69,028
    Last modified:June 16, 2009 - v3
    Checksum:iDF159F21D191332D
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti120 – 1201G → H in CAB11343. 1 PublicationCurated
    Sequence conflicti155 – 1562FV → SI in CAA38077. (PubMed:1847686)Curated
    Sequence conflicti288 – 2881Missing in CAA38077. (PubMed:1847686)Curated
    Sequence conflicti474 – 4741A → R in CAA38077. (PubMed:1847686)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X54140 Genomic DNA. Translation: CAA38077.1.
    Z98682 Genomic DNA. Translation: CAB11343.1.
    AL009126 Genomic DNA. Translation: CAB13363.2.
    PIRiE69609.
    RefSeqiNP_389373.2. NC_000964.3.

    Genome annotation databases

    EnsemblBacteriaiCAB13363; CAB13363; BSU14900.
    GeneIDi936898.
    KEGGibsu:BSU14900.
    PATRICi18974781. VBIBacSub10457_1582.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X54140 Genomic DNA. Translation: CAA38077.1 .
    Z98682 Genomic DNA. Translation: CAB11343.1 .
    AL009126 Genomic DNA. Translation: CAB13363.2 .
    PIRi E69609.
    RefSeqi NP_389373.2. NC_000964.3.

    3D structure databases

    ProteinModelPortali P24010.
    SMRi P24010. Positions 22-516.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 224308.BSU14900.

    Protein family/group databases

    TCDBi 3.D.4.4.1. the proton-translocating cytochrome oxidase (cox) superfamily.

    Proteomic databases

    PaxDbi P24010.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAB13363 ; CAB13363 ; BSU14900 .
    GeneIDi 936898.
    KEGGi bsu:BSU14900.
    PATRICi 18974781. VBIBacSub10457_1582.

    Organism-specific databases

    GenoListi BSU14900. [Micado ]

    Phylogenomic databases

    eggNOGi COG0843.
    HOGENOMi HOG000085275.
    KOi K02274.
    OrthoDBi EOG6B35XR.
    PhylomeDBi P24010.

    Enzyme and pathway databases

    UniPathwayi UPA00705 .
    BioCyci BSUB:BSU14900-MONOMER.
    RETL1328306-WGS:GSTH-6904-MONOMER.

    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.
    IPR014241. Cyt_c_oxidase_su1_bac.
    [Graphical view ]
    PANTHERi PTHR10422. PTHR10422. 1 hit.
    Pfami PF00115. COX1. 1 hit.
    [Graphical view ]
    PRINTSi PR01165. CYCOXIDASEI.
    SUPFAMi SSF81442. SSF81442. 1 hit.
    TIGRFAMsi TIGR02891. CtaD_CoxA. 1 hit.
    PROSITEi PS50855. COX1. 1 hit.
    PS00077. COX1_CUB. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The Bacillus subtilis cytochrome-c oxidase. Variations on a conserved protein theme."
      Saraste M., Metso T., Nakari T., Jalli T., Lauraeus M., van der Oost J.
      Eur. J. Biochem. 195:517-525(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: 168.
    2. "Bacillus subtilis chromosomal region downstream nprE."
      Bertero M., Presecan E., Glaser P., Richou A., Danchin A.
      Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: 168.
    3. "The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
      Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V.
      , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
      Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: 168.
    4. "From a consortium sequence to a unified sequence: the Bacillus subtilis 168 reference genome a decade later."
      Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A., Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.
      Microbiology 155:1758-1775(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: SEQUENCE REVISION TO 120.

    Entry informationi

    Entry nameiCOX1_BACSU
    AccessioniPrimary (citable) accession number: P24010
    Secondary accession number(s): O34467
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 1, 1992
    Last sequence update: June 16, 2009
    Last modified: October 1, 2014
    This is version 127 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Bacillus subtilis
      Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3