[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. PubMed=10482497 [NCBI, ExPASy, EBI, Israel, Japan] Kang B.S., Kim Y.M.; "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."; J. Bacteriol. 181:5581-5590(1999).
[2]	PROTEIN SEQUENCE OF 1-21. 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 (2.25 ANGSTROMS). DOI=10.1006/jmbi.2000.4023; PubMed=10966817 [NCBI, ExPASy, EBI, Israel, Japan] Haenzelmann P., Dobbek H., Gremer L., Huber R., Meyer O.; "The effect of intracellular molybdenum in Hydrogenophaga pseudoflava on the crystallographic structure of the seleno-molybdo-iron-sulfur flavoenzyme carbon monoxide dehydrogenase."; J. Mol. Biol. 301:1221-1235(2000).
[4]	REVIEW. DOI=10.1515/BC.2000.108; PubMed=11076018 [NCBI, ExPASy, EBI, Israel, Japan] Meyer O., Gremer L., Ferner R., Ferner M., Dobbek H., Gnida M., Meyer-Klaucke W., Huber R.; "The role of Se, Mo and Fe in the structure and function of carbon monoxide dehydrogenase."; Biol. Chem. 381:865-876(2000).

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

U80806; AAD00362.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

PDB

1FFU; X-ray; 2.35 A; A/D=1-163.	[ExPASy / RCSB / EBI]
1FFV; X-ray; 2.25 A; A/D=1-163.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1FFU; -.
1FFV; -.

ModBase

P19915.

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).

Other

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.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 163`	`163`	`Carbon monoxide dehydrogenase small chain.`	`PRO_0000079816`
`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`	`101 101`		`Iron-sulfur 2 (2Fe-2S).`
`METAL`	`104 104`		`Iron-sulfur 2 (2Fe-2S).`
`METAL`	`136 136`		`Iron-sulfur 2 (2Fe-2S).`
`METAL`	`138 138`		`Iron-sulfur 2 (2Fe-2S).`
`CONFLICT`	`11 11`		`Missing (in Ref. 2; AA sequence).`
`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`	`88 95`	`8`
`HELIX`	`105 118`	`14`
`HELIX`	`124 130`	`7`
`TURN`	`131 133`	`3`
`STRAND`	`137 139`	`3`
`HELIX`	`142 155`	`14`

Sequence information

Length: 163 AA [This is the length of the unprocessed precursor]

Molecular weight: 17752 Da [This is the MW of the unprocessed precursor]

CRC64: 9307050CC033410C [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAKKIITVNV NGKAQEKAVE PRTLLIHFLR EELNLTGAHI GCETSHCGAC TVDIDGRSVK 

        70         80         90        100        110        120 
SCTHLAVQCD GSEVLTVEGL ANKGVLHAVR EGFYKEHGLQ CGFCTPGMLM RAYRFLQENP 

       130        140        150        160 
NPTEAEIRMG MTGNLCRCTG YQNIVKAVQY AARKLQEPST AAA

P19915 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