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Protein

Carbon monoxide dehydrogenase small chain

Gene

coxS

Organism
Oligotropha carboxidovorans (strain ATCC 49405 / DSM 1227 / OM5)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the oxidation of carbon monoxide to carbon dioxide.2 Publications

Catalytic activityi

CO + a quinone + H2O = CO2 + a quinol.2 Publications

Cofactori

[2Fe-2S] cluster2 PublicationsNote: Binds 2 [2Fe-2S] clusters.2 Publications

Kineticsi

  1. KM=16.4 µM for 1,4-benzoquinone1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi42 – 421Iron-sulfur 1 (2Fe-2S)2 Publications
    Metal bindingi47 – 471Iron-sulfur 1 (2Fe-2S)2 Publications
    Metal bindingi50 – 501Iron-sulfur 1 (2Fe-2S)2 Publications
    Metal bindingi62 – 621Iron-sulfur 1 (2Fe-2S)2 Publications
    Metal bindingi102 – 1021Iron-sulfur 2 (2Fe-2S)2 Publications
    Metal bindingi105 – 1051Iron-sulfur 2 (2Fe-2S)2 Publications
    Metal bindingi137 – 1371Iron-sulfur 2 (2Fe-2S)2 Publications
    Metal bindingi139 – 1391Iron-sulfur 2 (2Fe-2S)2 Publications

    GO - Molecular functioni

    Complete GO annotation...

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    2Fe-2S, Iron, Iron-sulfur, Metal-binding

    Enzyme and pathway databases

    BioCyciOCAR504832:GJPZ-3597-MONOMER.
    BRENDAi1.2.99.2. 4399.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Carbon monoxide dehydrogenase small chain (EC:1.2.5.32 Publications)
    Short name:
    CO dehydrogenase subunit S
    Short name:
    CO-DH S
    Gene namesi
    Name:coxS
    Ordered Locus Names:OCA5_pHCG300300
    Encoded oniPlasmid megaplasmid pHCG30 Publication
    OrganismiOligotropha carboxidovorans (strain ATCC 49405 / DSM 1227 / OM5)
    Taxonomic identifieri504832 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBradyrhizobiaceaeOligotropha
    Proteomesi
    • UP000007730 Componenti: Plasmid pHCG3

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 166166Carbon monoxide dehydrogenase small chainPRO_0000079817Add
    BLAST

    Interactioni

    Subunit structurei

    Dimer of heterotrimers. Each heterotrimer consists of a large, a medium and a small subunit.1 Publication

    Chemistry

    BindingDBiP19921.

    Structurei

    Secondary structure

    1
    166
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi4 – 107Combined sources
    Beta strandi13 – 197Combined sources
    Helixi25 – 317Combined sources
    Beta strandi43 – 453Combined sources
    Beta strandi51 – 544Combined sources
    Beta strandi57 – 604Combined sources
    Helixi61 – 633Combined sources
    Helixi66 – 694Combined sources
    Beta strandi73 – 753Combined sources
    Helixi77 – 793Combined sources
    Helixi89 – 968Combined sources
    Helixi106 – 11914Combined sources
    Helixi125 – 1317Combined sources
    Turni132 – 1343Combined sources
    Beta strandi138 – 1403Combined sources
    Helixi143 – 15715Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1N5WX-ray1.50A/D1-166[»]
    1N60X-ray1.19A/D1-166[»]
    1N61X-ray1.30A/D1-166[»]
    1N62X-ray1.09A/D1-166[»]
    1N63X-ray1.21A/D1-166[»]
    1ZXIX-ray1.70A/D1-166[»]
    ProteinModelPortaliP19921.
    SMRiP19921. Positions 3-163.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP19921.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini4 – 80772Fe-2S ferredoxin-typePROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 2Fe-2S ferredoxin-type domain.PROSITE-ProRule annotation

    Phylogenomic databases

    KOiK03518.
    OMAiCTPGMIT.

    Family and domain databases

    Gene3Di1.10.150.120. 1 hit.
    3.10.20.30. 1 hit.
    InterProiIPR002888. 2Fe-2S-bd.
    IPR001041. 2Fe-2S_ferredoxin-type.
    IPR012675. Beta-grasp_dom.
    [Graphical view]
    PfamiPF00111. Fer2. 1 hit.
    PF01799. Fer2_2. 1 hit.
    [Graphical view]
    SUPFAMiSSF47741. SSF47741. 1 hit.
    SSF54292. SSF54292. 1 hit.
    PROSITEiPS51085. 2FE2S_FER_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P19921-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MAKAHIELTI NGHPVEALVE PRTLLIHFIR EQQNLTGAHI GCDTSHCGAC
    60 70 80 90 100
    TVDLDGMSVK SCTMFAVQAN GASITTIEGM AAPDGTLSAL QEGFRMMHGL
    110 120 130 140 150
    QCGYCTPGMI MRSHRLLQEN PSPTEAEIRF GIGGNLCRCT GYQNIVKAIQ
    160
    YAAAKINGVP FEEAAE
    Length:166
    Mass (Da):17,792
    Last modified:July 26, 2002 - v2
    Checksum:iE63AD31D726D22C1
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    CP002827 Genomic DNA. Translation: AEI08105.1.
    PIRiB56279.
    RefSeqiWP_013913729.1. NC_015689.1.

    Genome annotation databases

    EnsemblBacteriaiAEI08105; AEI08105; OCA5_pHCG300300.
    KEGGiocg:OCA5_pHCG300300.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    CP002827 Genomic DNA. Translation: AEI08105.1.
    PIRiB56279.
    RefSeqiWP_013913729.1. NC_015689.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1N5WX-ray1.50A/D1-166[»]
    1N60X-ray1.19A/D1-166[»]
    1N61X-ray1.30A/D1-166[»]
    1N62X-ray1.09A/D1-166[»]
    1N63X-ray1.21A/D1-166[»]
    1ZXIX-ray1.70A/D1-166[»]
    ProteinModelPortaliP19921.
    SMRiP19921. Positions 3-163.
    ModBaseiSearch...
    MobiDBiSearch...

    Chemistry

    BindingDBiP19921.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAEI08105; AEI08105; OCA5_pHCG300300.
    KEGGiocg:OCA5_pHCG300300.

    Phylogenomic databases

    KOiK03518.
    OMAiCTPGMIT.

    Enzyme and pathway databases

    BioCyciOCAR504832:GJPZ-3597-MONOMER.
    BRENDAi1.2.99.2. 4399.

    Miscellaneous databases

    EvolutionaryTraceiP19921.

    Family and domain databases

    Gene3Di1.10.150.120. 1 hit.
    3.10.20.30. 1 hit.
    InterProiIPR002888. 2Fe-2S-bd.
    IPR001041. 2Fe-2S_ferredoxin-type.
    IPR012675. Beta-grasp_dom.
    [Graphical view]
    PfamiPF00111. Fer2. 1 hit.
    PF01799. Fer2_2. 1 hit.
    [Graphical view]
    SUPFAMiSSF47741. SSF47741. 1 hit.
    SSF54292. SSF54292. 1 hit.
    PROSITEiPS51085. 2FE2S_FER_2. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Molecular characterization of the gene cluster coxMSL encoding the molybdenum-containing carbon monoxide dehydrogenase of Oligotropha carboxidovorans."
      Schuebel U., Kraut M., Moersdorf G., Meyer O.
      J. Bacteriol. 177:2197-2203(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 49405 / DSM 1227 / OM5.
    2. "Complete nucleotide sequence of the circular megaplasmid pHCG3 of Oligotropha carboxidovorans: function in the chemolithoautotrophic utilization of CO, H(2) and CO(2)."
      Fuhrmann S., Ferner M., Jeffke T., Henne A., Gottschalk G., Meyer O.
      Gene 322:67-75(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 49405 / DSM 1227 / OM5.
    3. "Complete genome sequences of the chemolithoautotrophic Oligotropha carboxidovorans strains OM4 and OM5."
      Volland S., Rachinger M., Strittmatter A., Daniel R., Gottschalk G., Meyer O.
      J. Bacteriol. 193:5043-5043(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 49405 / DSM 1227 / OM5.
    4. "Homology and distribution of CO dehydrogenase structural genes in carboxydotrophic bacteria."
      Kraut M., Hugendieck I., Herwig S., Meyer O.
      Arch. Microbiol. 152:335-341(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 1-21.
    5. "Reaction of the molybdenum- and copper-containing carbon monoxide dehydrogenase from Oligotropha carboxydovorans with quinones."
      Wilcoxen J., Zhang B., Hille R.
      Biochemistry 50:1910-1916(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
    6. "Crystal structure and mechanism of CO dehydrogenase, a molybdo iron-sulfur flavoprotein containing S-selanylcysteine."
      Dobbek H., Gremer L., Meyer O., Huber R.
      Proc. Natl. Acad. Sci. U.S.A. 96:8884-8889(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH CODH LARGE AND MEDIUM SUBUNITS; IRON-SULFUR (2FE-2S), COFACTOR, SUBUNIT.
    7. "Catalysis at a dinuclear CuSMo(==O)OH cluster in a CO dehydrogenase resolved at 1.1-A resolution."
      Dobbek H., Gremer L., Kiefersauer R., Huber R., Meyer O.
      Proc. Natl. Acad. Sci. U.S.A. 99:15971-15976(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.09 ANGSTROMS) IN COMPLEX WITH CODH LARGE AND MEDIUM SUBUNITS; IRON-SULFUR (2FE-2S), FUNCTION, COFACTOR, CATALYTIC ACTIVITY, REACTION MECHANISM.

    Entry informationi

    Entry nameiDCMS_OLICO
    AccessioniPrimary (citable) accession number: P19921
    Secondary accession number(s): F8C0Z5, Q51324
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1991
    Last sequence update: July 26, 2002
    Last modified: July 6, 2016
    This is version 113 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Plasmid, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.