Carbon monoxide dehydrogenase small chain - Oligotropha carboxidovorans (strain ATCC 49405 / DSM 1227 / OM5)

Contribute

Send feedback

Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot P19921 (DCMS_OLICO)

Last modified November 24, 2009. Version 77. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data |

Customize display

text xml rdf/xml gff fasta

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Hide | Top

Names and origin

Protein names

Recommended name:
    Carbon monoxide dehydrogenase small chain
      Short name=CO dehydrogenase subunit S
      Short name=CO-DH S
    EC=1.2.99.2

Gene names

Name:	coxS
Ordered Locus Names:	OCAR_p_08033

Encoded on

Plasmid megaplasmid pHCG3

Organism

Oligotropha carboxidovorans (strain ATCC 49405 / DSM 1227 / OM5) [Complete proteome] [HAMAP]

Taxonomic identifier

504832 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Bradyrhizobiaceae › Oligotropha

Hide | Top

Protein attributes

Sequence length	166 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

Hide | Top

General annotation (Comments)

Function	Catalyzes the oxidation of carbon monoxide to carbon dioxide.
Catalytic activity	CO + H₂O + A = CO₂ + AH₂.
Cofactor	Binds 2 2Fe-2S clusters.
Subunit structure	Dimer of heterotrimers. Each heterotrimer consists of a large, a medium and a small subunit.
Sequence similarities	Contains 1 2Fe-2S ferredoxin-type domain.

Hide | Top

Ontologies

Keywords
Ligand	2Fe-2S Iron Iron-sulfur Metal-binding
Molecular function	Oxidoreductase
Technical term	3D-structure Complete proteome Direct protein sequencing Plasmid
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	2 iron, 2 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW carbon-monoxide dehydrogenase (acceptor) activity Inferred from electronic annotation. Source: EC electron carrier activity Inferred from electronic annotation. Source: InterPro iron ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Hide | Top

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 166

166

Carbon monoxide dehydrogenase small chain

PRO_0000079817

Regions

Domain

4 – 80

2Fe-2S ferredoxin-type

Sites

Metal binding

Iron-sulfur 1 (2Fe-2S)

Metal binding

Iron-sulfur 1 (2Fe-2S)

Metal binding

Iron-sulfur 1 (2Fe-2S)

Metal binding

Iron-sulfur 1 (2Fe-2S)

Metal binding

102

Iron-sulfur 2 (2Fe-2S)

Metal binding

105

Iron-sulfur 2 (2Fe-2S)

Metal binding

137

Iron-sulfur 2 (2Fe-2S)

Metal binding

139

Iron-sulfur 2 (2Fe-2S)

Secondary structure

166

Helix Strand Turn

Details...

Hide | Top

Sequences

Sequence

Length

Mass (Da)

Tools

P19921-1 [UniParc].

Last modified July 26, 2002. Version 2.
Checksum: E63AD31D726D22C1
Show »

FASTA

166

17,792

        10         20         30         40         50         60 
MAKAHIELTI NGHPVEALVE PRTLLIHFIR EQQNLTGAHI GCDTSHCGAC TVDLDGMSVK 

        70         80         90        100        110        120 
SCTMFAVQAN GASITTIEGM AAPDGTLSAL QEGFRMMHGL QCGYCTPGMI MRSHRLLQEN 

       130        140        150        160 
PSPTEAEIRF GIGGNLCRCT GYQNIVKAIQ YAAAKINGVP FEEAAE

« Hide

Hide | Top

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 7721710] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[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: 14644498] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	"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: 2818128] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-21.
[4]	"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: 10430865] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
[5]	"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: 12475995] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.09 ANGSTROMS).
+	Additional computationally mapped references.

Hide | Top

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X82447 Genomic DNA. Translation: CAA57828.1.

PIR

B56279.

RefSeq

YP_015604.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1N5W	X-ray	1.50	A/D	1-166	[»]
1N60	X-ray	1.19	A/D	1-166	[»]
1N61	X-ray	1.30	A/D	1-166	[»]
1N62	X-ray	1.09	A/D	1-166	[»]
1N63	X-ray	1.21	A/D	1-166	[»]
1ZXI	X-ray	1.70	A/D	1-166	[»]

ModBase

Search...

Genome annotation databases

GeneID

2807117.

GenomeReviews

Gene locus OCAR_p_08033 in contig X82447_GR.

Organism-specific databases

CMR

Search...

Phylogenomic databases

OMA

YQNIVKS.

Enzyme and pathway databases

BRENDA

1.2.99.2. 255922.

Family and domain databases

InterPro

IPR002888. 2Fe-2S_bd.
IPR001041. Ferredoxin.
[Graphical view]

Pfam

PF00111. Fer2. 1 hit.
PF01799. Fer2_2. 1 hit.
[Graphical view]

PROSITE

PS00197. 2FE2S_FER_1. False negative.
PS51085. 2FE2S_FER_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Hide | Top

Entry information

Entry name

DCMS_OLICO

Accession

Primary (citable) accession number: P19921
Secondary accession number(s): Q51324

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1991
Last sequence update:	July 26, 2002
Last modified:	November 24, 2009
This is version 77 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Hide | Top

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families