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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.

Catalytic activityi

CO + H2O + A = CO2 + AH2.

Cofactori

[2Fe-2S] clusterNote: Binds 2 [2Fe-2S] clusters.

Sites

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

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:1.2.99.2)
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.

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. "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).
  6. "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).

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: December 9, 2015
This is version 112 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.