Reviewed, UniProtKB/Swiss-Prot P19914 (DCMM_HYDPS)

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:

cutM

Organism

Hydrogenophaga pseudoflava (Pseudomonas carboxydoflava)

Taxonomic identifier

47421 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Comamonadaceae › Hydrogenophaga

Protein attributes

Sequence length	287 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 Direct protein sequencing
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 – 287

287

Carbon monoxide dehydrogenase medium chain

PRO_0000079812

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

2 – 3

2

IP → MI AA sequence Ref.2

Sequence conflict

13

1

S → H AA sequence Ref.2

Secondary structure

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287

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 – 97

6

Helix

98 – 100

3

Helix

104 – 107

4

Helix

112 – 118

7

Helix

125 – 131

7

Beta strand

135 – 139

5

Beta strand

144 – 149

6

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 – 231

5

Helix

240 – 252

13

Helix

264 – 285

22

Sequences

	Sequence		Length	Mass (Da)
	P19914-1 [UniParc]. Last modified July 11, 2002. Version 2. Checksum: F3E9848BDCF4138E	FASTA	287	30,722
	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

References

[1]	"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." Kang B.S., Kim Y.M. J. Bacteriol. 181:5581-5590(1999) [PubMed: 10482497] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"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.
[3]	"The effect of intracellular molybdenum in Hydrogenophaga pseudoflava on the crystallographic structure of the seleno-molybdo-iron-sulfur flavoenzyme carbon monoxide dehydrogenase." Haenzelmann P., Dobbek H., Gremer L., Huber R., Meyer O. J. Mol. Biol. 301:1221-1235(2000) [PubMed: 10966817] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS).
[4]	"The role of Se, Mo and Fe in the structure and function of carbon monoxide dehydrogenase." Meyer O., Gremer L., Ferner R., Ferner M., Dobbek H., Gnida M., Meyer-Klaucke W., Huber R. Biol. Chem. 381:865-876(2000) [PubMed: 11076018] [Abstract] Cited for: REVIEW.

Cross-references

Sequence databases

EMBLGenBankDDBJ

U80806 Genomic DNA. Translation: AAD00361.1.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1FFU	X-ray	2.35	C/F	1-287	[»]
1FFV	X-ray	2.25	C/F	1-287	[»]

ModBase

Search...

Enzyme and pathway databases

BRENDA

1.2.99.2. 2857.

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_HYDPS

Accession

Primary (citable) accession number: P19914
Secondary accession number(s): Q9ZAR7

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1991
Last sequence update:	July 11, 2002
Last modified:	June 16, 2009
This is version 65 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)