Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
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)DescriptionActionsGraphical viewLength
Metal bindingi42Iron-sulfur 1 (2Fe-2S)1
Metal bindingi47Iron-sulfur 1 (2Fe-2S)1
Metal bindingi50Iron-sulfur 1 (2Fe-2S)1
Metal bindingi62Iron-sulfur 1 (2Fe-2S)1
Metal bindingi101Iron-sulfur 2 (2Fe-2S)1
Metal bindingi104Iron-sulfur 2 (2Fe-2S)1
Metal bindingi136Iron-sulfur 2 (2Fe-2S)1
Metal bindingi138Iron-sulfur 2 (2Fe-2S)1

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)DescriptionActionsGraphical viewLength
ChainiPRO_00000798161 – 163Carbon monoxide dehydrogenase small chainAdd BLAST163

Interactioni

Subunit structurei

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

Structurei

Secondary structure

1163
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi4 – 10Combined sources7
Beta strandi13 – 19Combined sources7
Helixi25 – 31Combined sources7
Beta strandi43 – 45Combined sources3
Beta strandi51 – 54Combined sources4
Beta strandi57 – 60Combined sources4
Helixi61 – 63Combined sources3
Helixi66 – 69Combined sources4
Beta strandi73 – 75Combined sources3
Helixi77 – 79Combined sources3
Beta strandi80 – 82Combined sources3
Helixi88 – 95Combined sources8
Helixi105 – 118Combined sources14
Helixi124 – 130Combined sources7
Turni131 – 133Combined sources3
Beta strandi137 – 139Combined sources3
Helixi142 – 155Combined sources14

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP19915.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini4 – 802Fe-2S ferredoxin-typePROSITE-ProRule annotationAdd BLAST77

Sequence similaritiesi

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

Family and domain databases

CDDicd00207. fer2. 1 hit.
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)DescriptionActionsGraphical viewLength
Sequence conflicti11Missing AA sequence (PubMed:2818128).Curated1

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1FFUX-ray2.35A/D1-163[»]
1FFVX-ray2.25A/D1-163[»]
ProteinModelPortaliP19915.
SMRiP19915.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP19915.

Family and domain databases

CDDicd00207. fer2. 1 hit.
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...

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: November 2, 2016
This is version 95 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.