[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=CH5 / OM5 / DSM 1227; PubMed=7721710 [NCBI, ExPASy, EBI, Israel, Japan] Schuebel U., Kraut M., Moersdorf G., Meyer O.; "Molecular characterization of the gene cluster coxMSL encoding the molybdenum-containing carbon monoxide dehydrogenase of Oligotropha carboxidovorans."; J. Bacteriol. 177:2197-2203(1995).
[2]	PROTEIN SEQUENCE OF 1-21. STRAIN=CH5 / OM5 / DSM 1227; DOI=10.1007/BF00425170; PubMed=2818128 [NCBI, ExPASy, EBI, Israel, Japan] Kraut M., Hugendieck I., Herwig S., Meyer O.; "Homology and distribution of CO dehydrogenase structural genes in carboxydotrophic bacteria."; Arch. Microbiol. 152:335-341(1989).
[3]	X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS). DOI=10.1073/pnas.96.16.8884; PubMed=10430865 [NCBI, ExPASy, EBI, Israel, Japan] Dobbek H., Gremer L., Meyer O., Huber R.; "Crystal structure and mechanism of CO dehydrogenase, a molybdo iron-sulfur flavoprotein containing S-selanylcysteine."; Proc. Natl. Acad. Sci. U.S.A. 96:8884-8889(1999).
[4]	X-RAY CRYSTALLOGRAPHY (1.09 ANGSTROMS). DOI=10.1073/pnas.212640899; PubMed=12475995 [NCBI, ExPASy, EBI, Israel, Japan] Dobbek H., Gremer L., Kiefersauer R., Huber R., Meyer O.; "Catalysis at a dinuclear CuSMo(==O)OH cluster in a CO dehydrogenase resolved at 1.1-A resolution."; Proc. Natl. Acad. Sci. U.S.A. 99:15971-15976(2002).

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: Dimer of heterotrimers. Each heterotrimer consists of a large, a medium and a small subunit.
SIMILARITY: Contains 1 2Fe-2S ferredoxin-type domain.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

X82447; CAA57828.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

B56279; B56279.

RefSeq

YP_015604.1; -.

3D structure databases

PDB

1N5W; X-ray; 1.50 A; A/D=1-166.	[ExPASy / RCSB / EBI]
1N60; X-ray; 1.19 A; A/D=1-166.	[ExPASy / RCSB / EBI]
1N61; X-ray; 1.30 A; A/D=1-166.	[ExPASy / RCSB / EBI]
1N62; X-ray; 1.09 A; A/D=1-166.	[ExPASy / RCSB / EBI]
1N63; X-ray; 1.21 A; A/D=1-166.	[ExPASy / RCSB / EBI]
1ZXI; X-ray; 1.70 A; A/D=1-166.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1N5W; -.
1N60; -.
1N61; -.
1N62; -.
1N63; -.
1ZXI; -.

ModBase

P19921.

Ontologies

GO:0051537;	Molecular function: 2 iron, 2 sulfur cluster binding (inferred from electronic annotation from UniProtKB-KW).
GO:0018492;	Molecular function: carbon-monoxide dehydrogenase (acceptor) activity (inferred from electronic annotation from EC).
GO:0009055;	Molecular function: electron carrier activity (inferred from electronic annotation from InterPro).
GO:0005506;	Molecular function: iron ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR002888; 2Fe-2S_bd.
IPR006058; 2Fe2S_fd_BS.
IPR001041; Ferredoxin.
Graphical view of domain structure.

Pfam

PF00111; Fer2; 1.
PF01799; Fer2_2; 1.
Pfam graphical view of domain structure.

ProDom

PD186071; 2Fe-2S_bind; 1.
[Domain structure / List of seq. sharing at least 1 domain]

PROSITE

PS00197; 2FE2S_FER_1; FALSE_NEG.
PS51085; 2FE2S_FER_2; 1.
PROSITE graphical view of domain structure (profiles).

ProtoNet

P19921.

Genome annotation databases

GeneID

2807117; -.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

2Fe-2S; 3D-structure; Direct protein sequencing; Iron; Iron-sulfur; Metal-binding; Oxidoreductase; Plasmid.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 166`	`166`	`Carbon monoxide dehydrogenase small chain.`	`PRO_0000079817`
`DOMAIN`	`4 80`	`77`	`2Fe-2S ferredoxin-type.`
`METAL`	`42 42`		`Iron-sulfur 1 (2Fe-2S).`
`METAL`	`47 47`		`Iron-sulfur 1 (2Fe-2S).`
`METAL`	`50 50`		`Iron-sulfur 1 (2Fe-2S).`
`METAL`	`62 62`		`Iron-sulfur 1 (2Fe-2S).`
`METAL`	`102 102`		`Iron-sulfur 2 (2Fe-2S).`
`METAL`	`105 105`		`Iron-sulfur 2 (2Fe-2S).`
`METAL`	`137 137`		`Iron-sulfur 2 (2Fe-2S).`
`METAL`	`139 139`		`Iron-sulfur 2 (2Fe-2S).`
`STRAND`	`4 10`	`7`
`STRAND`	`13 19`	`7`
`HELIX`	`25 31`	`7`
`STRAND`	`43 45`	`3`
`STRAND`	`51 54`	`4`
`STRAND`	`57 60`	`4`
`HELIX`	`61 63`	`3`
`HELIX`	`66 69`	`4`
`STRAND`	`73 75`	`3`
`HELIX`	`77 79`	`3`
`HELIX`	`89 96`	`8`
`HELIX`	`106 119`	`14`
`HELIX`	`125 131`	`7`
`TURN`	`132 134`	`3`
`STRAND`	`138 140`	`3`
`HELIX`	`143 157`	`15`

Sequence information

Length: 166 AA [This is the length of the unprocessed precursor]

Molecular weight: 17792 Da [This is the MW of the unprocessed precursor]

CRC64: E63AD31D726D22C1 [This is a checksum on the sequence]

        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

P19921 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools