Reviewed, UniProtKB/Swiss-Prot P19920 (DCMM_OLICO)

Names and origin

Protein names

Recommended name:
    Carbon monoxide dehydrogenase medium chain
      Short name=CO dehydrogenase subunit M
      Short name=CO-DH M
    EC=1.2.99.2

Gene names

Name:	coxM
Ordered Locus Names:	OCAR_p_08032

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

Protein attributes

Sequence length	288 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (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 structure	Dimer of heterotrimers. Each heterotrimer consists of a large, a medium and a small subunit.
Sequence similarities	Contains 1 FAD-binding PCMH-type domain.

Ontologies

Keywords
Ligand	FAD Flavoprotein
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	FAD binding Inferred from electronic annotation. Source: InterPro carbon-monoxide dehydrogenase (acceptor) activity Inferred from electronic annotation. Source: EC electron carrier activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 288

288

Carbon monoxide dehydrogenase medium chain

PRO_0000079813

Regions

Domain

1 – 177

177

FAD-binding PCMH-type

Nucleotide binding

32 – 36

5

FAD

Nucleotide binding

111 – 115

5

FAD

Experimental info

Sequence conflict

1

1

M → MM AA sequence Ref.4

Secondary structure

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288

Helix Strand Turn

Details...

Beta strand

7 – 9

3

Helix

14 – 24

11

Helix

25 – 27

3

Beta strand

28 – 33

6

Helix

37 – 42

6

Beta strand

49 – 53

5

Helix

58 – 60

3

Beta strand

63 – 66

4

Beta 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

Beta strand

135 – 140

6

Beta strand

143 – 148

6

Helix

149 – 152

4

Beta strand

153 – 155

3

Beta strand

158 – 160

3

Beta strand

166 – 173

8

Beta strand

180 – 186

7

Beta strand

195 – 205

11

Beta strand

208 – 222

15

Helix

227 – 233

7

Helix

240 – 251

12

Helix

264 – 285

22

Sequences

	Sequence		Length	Mass (Da)
	P19920-1 [UniParc]. Last modified July 11, 2002. Version 2. Checksum: E3EA980056731FC5	FASTA	288	30,241
	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

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]	"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." Hugendieck I., Meyer O. Arch. Microbiol. 157:301-304(1992) [PubMed: 1510563] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-29.
[4]	"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 1-14.
[5]	"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).
[6]	"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.

Cross-references

Sequence databases

EMBLGenBankDDBJ

X82447 Genomic DNA. Translation: CAA57827.1.

PIR

A56279.

RefSeq

YP_015603.1.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1N5W	X-ray	1.50	C/F	1-288	[»]
1N60	X-ray	1.19	C/F	1-288	[»]
1N61	X-ray	1.30	C/F	1-288	[»]
1N62	X-ray	1.09	C/F	1-288	[»]
1N63	X-ray	1.21	C/F	1-288	[»]
1ZXI	X-ray	1.70	C/F	1-288	[»]

ModBase

Search...

Genome annotation databases

GeneID

2807116.

GenomeReviews

Gene locus OCAR_p_08032 in contig X82447_GR.

Organism-specific databases

CMR

Search...

Enzyme and pathway databases

BRENDA

1.2.99.2. 255922.

Family and domain databases

InterPro

IPR005107. CO_DH_flav_C.
IPR016169. CO_DH_flavot_FAD-bd_sub2.
IPR016166. FAD-bd_2.
IPR016167. FAD-bd_2_sub1.
IPR002346. Mopterin_DH_FAD-bd.
[Graphical view]

Gene3D

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

Pfam

PF03450. CO_deh_flav_C. 1 hit.
PF00941. FAD_binding_5. 1 hit.
[Graphical view]

PROSITE

PS51387. FAD_PCMH. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

DCMM_OLICO

Accession

Primary (citable) accession number: P19920
Secondary accession number(s): Q51323

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1991
Last sequence update:	July 11, 2002
Last modified:	June 16, 2009
This is version 76 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)