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Protein

Carbon monoxide dehydrogenase small chain

Gene

cutS

Organism
Hydrogenophaga pseudoflava (Pseudomonas carboxydoflava)
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.By similarity

Catalytic activityi

CO + a quinone + H2O = CO2 + a quinol.By similarity

Cofactori

[2Fe-2S] cluster1 PublicationNote: Binds 2 [2Fe-2S] clusters.1 Publication

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 bindingi101 – 1011Iron-sulfur 2 (2Fe-2S)
Metal bindingi104 – 1041Iron-sulfur 2 (2Fe-2S)
Metal bindingi136 – 1361Iron-sulfur 2 (2Fe-2S)
Metal bindingi138 – 1381Iron-sulfur 2 (2Fe-2S)

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

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

Names & Taxonomyi

Protein namesi
Recommended name:
Carbon monoxide dehydrogenase small chain (EC:1.2.5.3By similarity)
Short name:
CO dehydrogenase subunit S
Short name:
CO-DH S
Gene namesi
Name:cutS
OrganismiHydrogenophaga pseudoflava (Pseudomonas carboxydoflava)
Taxonomic identifieri47421 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesComamonadaceaeHydrogenophaga

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 163163Carbon monoxide dehydrogenase small chainPRO_0000079816Add
BLAST

Interactioni

Subunit structurei

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

Structurei

Secondary structure

1
163
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
Beta strandi80 – 823Combined sources
Helixi88 – 958Combined sources
Helixi105 – 11814Combined sources
Helixi124 – 1307Combined sources
Turni131 – 1333Combined sources
Beta strandi137 – 1393Combined sources
Helixi142 – 15514Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FFUX-ray2.35A/D1-163[»]
1FFVX-ray2.25A/D1-163[»]
ProteinModelPortaliP19915.
SMRiP19915. Positions 2-157.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP19915.

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

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.

P19915-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAKKIITVNV NGKAQEKAVE PRTLLIHFLR EELNLTGAHI GCETSHCGAC
60 70 80 90 100
TVDIDGRSVK SCTHLAVQCD GSEVLTVEGL ANKGVLHAVR EGFYKEHGLQ
110 120 130 140 150
CGFCTPGMLM RAYRFLQENP NPTEAEIRMG MTGNLCRCTG YQNIVKAVQY
160
AARKLQEPST AAA
Length:163
Mass (Da):17,752
Last modified:July 11, 2002 - v2
Checksum:i9307050CC033410C
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti11 – 111Missing AA sequence (PubMed:2818128).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U80806 Genomic DNA. Translation: AAD00362.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U80806 Genomic DNA. Translation: AAD00362.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FFUX-ray2.35A/D1-163[»]
1FFVX-ray2.25A/D1-163[»]
ProteinModelPortaliP19915.
SMRiP19915. Positions 2-157.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP19915.

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

  1. "Cloning and molecular characterization of the genes for carbon monoxide dehydrogenase and localization of molybdopterin, flavin adenine dinucleotide, and iron-sulfur centers in the enzyme of Hydrogenophaga pseudoflava."
    Kang B.S., Kim Y.M.
    J. Bacteriol. 181:5581-5590(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], COFACTOR, SUBUNIT.
  2. "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.
  3. "The effect of intracellular molybdenum in Hydrogenophaga pseudoflava on the crystallographic structure of the seleno-molybdo-iron-sulfur flavoenzyme carbon monoxide dehydrogenase."
    Haenzelmann P., Dobbek H., Gremer L., Huber R., Meyer O.
    J. Mol. Biol. 301:1221-1235(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS).
  4. "The role of Se, Mo and Fe in the structure and function of carbon monoxide dehydrogenase."
    Meyer O., Gremer L., Ferner R., Ferner M., Dobbek H., Gnida M., Meyer-Klaucke W., Huber R.
    Biol. Chem. 381:865-876(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.

Entry informationi

Entry nameiDCMS_HYDPS
AccessioniPrimary (citable) accession number: P19915
Secondary accession number(s): Q9ZAR6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: July 11, 2002
Last modified: July 6, 2016
This is version 92 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, Direct protein sequencing

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.