[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 1-14. 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 1 FAD per subunit.
SUBUNIT: Dimer of heterotrimers. Each heterotrimer consists of a large, a medium and a small subunit.
SIMILARITY: Contains 1 FAD-binding PCMH-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; AAD00361.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

PDB

1FFU; X-ray; 2.35 A; C/F=1-287.	[ExPASy / RCSB / EBI]
1FFV; X-ray; 2.25 A; C/F=1-287.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1FFU; -.
1FFV; -.

ModBase

P19914.

Family and domain databases

InterPro

IPR005107; CO_DHase_flav_C.
IPR016169; CO_DHase_flavot_FAD-bd_sub2.
IPR016167; FAD-bd_2_sub1.
IPR002346; Mopterin_DHase_FAD-bd.
Graphical view of domain structure.

Gene3D

G3DSA:3.30.390.50; CO_DH_flav_C; 1.
G3DSA:3.30.465.10; CO_DH_flavoprot_FAD-bd_sub2; 1.
G3DSA:3.30.43.10; FAD-binding_2_sub1; 1.

Pfam

PF03450; CO_deh_flav_C; 1.
PF00941; FAD_binding_5; 1.
Pfam graphical view of domain structure.

PROSITE

PS51387; FAD_PCMH; 1.
PROSITE graphical view of domain structure (profiles).

Other

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

Keywords

3D-structure; Direct protein sequencing; FAD; Flavoprotein; Oxidoreductase.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 287`	`287`	`Carbon monoxide dehydrogenase medium chain.`	`PRO_0000079812`
`DOMAIN`	`1 177`	`177`	`FAD-binding PCMH-type.`
`NP_BIND`	`32 36`	`5`	`FAD.`
`NP_BIND`	`111 115`	`5`	`FAD.`
`CONFLICT`	`2 3`		`IP -> MI (in Ref. 2; AA sequence).`
`CONFLICT`	`13 13`		`S -> H (in Ref. 2; AA sequence).`
`STRAND`	`7 9`	`3`
`HELIX`	`14 24`	`11`
`HELIX`	`25 27`	`3`
`STRAND`	`28 33`	`6`
`HELIX`	`37 42`	`6`
`STRAND`	`49 53`	`5`
`HELIX`	`58 60`	`3`
`STRAND`	`63 66`	`4`
`STRAND`	`69 73`	`5`
`HELIX`	`78 83`	`6`
`HELIX`	`85 90`	`6`
`HELIX`	`92 97`	`6`
`HELIX`	`98 100`	`3`
`HELIX`	`104 107`	`4`
`HELIX`	`112 118`	`7`
`HELIX`	`125 131`	`7`
`STRAND`	`135 139`	`5`
`STRAND`	`144 149`	`6`
`STRAND`	`153 155`	`3`
`STRAND`	`158 160`	`3`
`STRAND`	`166 173`	`8`
`STRAND`	`180 186`	`7`
`STRAND`	`195 205`	`11`
`STRAND`	`208 222`	`15`
`HELIX`	`227 231`	`5`
`HELIX`	`240 252`	`13`
`HELIX`	`264 285`	`22`

Sequence information

Length: 287 AA [This is the length of the unprocessed precursor]

Molecular weight: 30722 Da [This is the MW of the unprocessed precursor]

CRC64: F3E9848BDCF4138E [This is a checksum on the sequence]

        10         20         30         40         50         60 
MIPPRFEYHA PKSVGEAVAL LGQLGSDAKL LAGGHSLLPM MKLRFAQPEH LIDINRIPEL 

        70         80         90        100        110        120 
RGIREEGSTV VIGAMTVEND LISSPIVQAR LPLLAEAAKL IADPQVRNRG TIGGDIAHGH 

       130        140        150        160        170        180 
PGNDHPALSI AVEAHFVLEG PNGRRTVPAD GFFLGTYMTL LEENEVMVEI RVPAFAQGTG 

       190        200        210        220        230        240 
WAYEKLKRKT GDWATAGCAV VMRKSGNTVS HIRIALTNVA PTALRREGGR SRLLGKAFTK 

       250        260        270        280 
EAVQAAADAA IAICEPAEDL RGDADYKTAM AGQMVKRALN AAWARCA

P19914 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