[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 1-29. DOI=10.1007/BF00245166; PubMed=1510563 [NCBI, ExPASy, EBI, Israel, Japan] Hugendieck I., Meyer O.; "The structural genes encoding CO dehydrogenase subunits (cox L, M and S) in Pseudomonas carboxydovorans OM5 reside on plasmid pHCG3 and are, with the exception of Streptomyces thermoautotrophicus, conserved in carboxydotrophic bacteria."; Arch. Microbiol. 157:301-304(1992).
[3]	PROTEIN SEQUENCE OF 1-14. 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).
[4]	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).
[5]	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 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

X82447; CAA57827.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A56279; A56279.

RefSeq

YP_015603.1; -.

3D structure databases

PDB

1N5W; X-ray; 1.50 A; C/F=1-288.	[ExPASy / RCSB / EBI]
1N60; X-ray; 1.19 A; C/F=1-288.	[ExPASy / RCSB / EBI]
1N61; X-ray; 1.30 A; C/F=1-288.	[ExPASy / RCSB / EBI]
1N62; X-ray; 1.09 A; C/F=1-288.	[ExPASy / RCSB / EBI]
1N63; X-ray; 1.21 A; C/F=1-288.	[ExPASy / RCSB / EBI]
1ZXI; X-ray; 1.70 A; C/F=1-288.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

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

ModBase

P19920.

Ontologies

GO:0018492;	Molecular function: carbon-monoxide dehydrogenase (acceptor) activity (inferred from electronic annotation from EC).
QuickGo view.

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).

BLOCKS

P19920.

Genome annotation databases

GeneID

2807116; -.

Other

ProtoNet

P19920.

UniRef

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

Keywords

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

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 288`	`288`	`Carbon monoxide dehydrogenase medium chain.`	`PRO_0000079813`
`DOMAIN`	`1 177`	`177`	`FAD-binding PCMH-type.`
`NP_BIND`	`32 36`	`5`	`FAD.`
`NP_BIND`	`111 115`	`5`	`FAD.`
`CONFLICT`	`1 1`		`M -> MM (in Ref. 3; 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 98`	`7`
`HELIX`	`104 109`	`6`
`HELIX`	`112 117`	`6`
`HELIX`	`125 132`	`8`
`STRAND`	`135 140`	`6`
`STRAND`	`143 148`	`6`
`HELIX`	`149 152`	`4`
`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`	`227 233`	`7`
`HELIX`	`240 251`	`12`
`HELIX`	`264 285`	`22`

Sequence information

Length: 288 AA [This is the length of the unprocessed precursor]

Molecular weight: 30241 Da [This is the MW of the unprocessed precursor]

CRC64: E3EA980056731FC5 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MIPGSFDYHR PKSIADAVAL LTKLGEDARP LAGGHSLIPI MKTRLATPEH LVDLRDIGDL 

        70         80         90        100        110        120 
VGIREEGTDV VIGAMTTQHA LIGSDFLAAK LPIIRETSLL IADPQIRYMG TIGGNAANGD 

       130        140        150        160        170        180 
PGNDMPALMQ CLGAAYELTG PEGARIVAAR DYYQGAYFTA IEPGELLTAI RIPVPPTGHG 

       190        200        210        220        230        240 
YAYEKLKRKI GDYATAAAAV VLTMSGGKCV TASIGLTNVA NTPLWAEEAG KVLVGTALDK 

       250        260        270        280 
PALDKAVALA EAITAPASDG RGPAEYRTKM AGVMLRRAVE RAKARAKN

P19920 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