Reviewed, UniProtKB/Swiss-Prot P19921 (DCMS_OLICA)

Names and origin

Protein names

Recommended name:
    Carbon monoxide dehydrogenase small chain
      Short name(s)=CO dehydrogenase subunit S, CO-DH S
    EC=1.2.99.2

Gene names

Name:

coxS

Encoded on

Plasmid megaplasmid pHCG3

Organism

Oligotropha carboxidovorans (Pseudomonas carboxydovorans)

Taxonomic identifier

40137 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Bradyrhizobiaceae › Oligotropha

Protein attributes

Sequence length	166 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 + H(2)O + A = CO(2) + AH(2).
Cofactor	Binds 2 2Fe-2S clusters.
Subunit structure	Dimer of heterotrimers. Each heterotrimer consists of a large, a medium and a small subunit.
Sequence similarities	Contains 1 2Fe-2S ferredoxin-type domain.

Ontologies

Keywords
Ligand	2Fe-2S Iron Iron-sulfur Metal-binding
Molecular function	Oxidoreductase
Technical term	3D-structure Direct protein sequencing Plasmid
Gene Ontology (GO)
Molecular function	carbon-monoxide dehydrogenase (acceptor) activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Molecule processing

Chain

1 – 166

166

Carbon monoxide dehydrogenase small chain

Regions

Domain

4 – 80

77

2Fe-2S ferredoxin-type

Sites

Metal binding

42

1

Iron-sulfur 1 (2Fe-2S)

Metal binding

47

1

Iron-sulfur 1 (2Fe-2S)

Metal binding

50

1

Iron-sulfur 1 (2Fe-2S)

Metal binding

62

1

Iron-sulfur 1 (2Fe-2S)

Metal binding

102

1

Iron-sulfur 2 (2Fe-2S)

Metal binding

105

1

Iron-sulfur 2 (2Fe-2S)

Metal binding

137

1

Iron-sulfur 2 (2Fe-2S)

Metal binding

139

1

Iron-sulfur 2 (2Fe-2S)

Secondary structure

1

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166

Helix Strand Turn

Details...

Beta strand

4 – 10

7

Beta strand

13 – 19

7

Helix

25 – 31

7

Beta strand

43 – 45

3

Beta strand

51 – 54

4

Beta strand

57 – 60

4

Helix

61 – 63

3

Helix

66 – 69

4

Beta strand

73 – 75

3

Helix

77 – 79

3

Helix

89 – 96

8

Helix

106 – 119

14

Helix

125 – 131

7

Turn

132 – 134

3

Beta strand

138 – 140

3

Helix

143 – 157

15

Sequences

	Sequence		Length	Mass (Da)
	P19921-1 [UniParc]. Last modified July 26, 2002. Version 2. Checksum: E63AD31D726D22C1	FASTA	166	17,792
	10 20 30 40 50 60 MAKAHIELTI NGHPVEALVE PRTLLIHFIR EQQNLTGAHI GCDTSHCGAC TVDLDGMSVK 70 80 90 100 110 120 SCTMFAVQAN GASITTIEGM AAPDGTLSAL QEGFRMMHGL QCGYCTPGMI MRSHRLLQEN 130 140 150 160 PSPTEAEIRF GIGGNLCRCT GYQNIVKAIQ YAAAKINGVP FEEAAE

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]. Strain: CH5 / OM5 / DSM 1227.
[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 1-21. Strain: CH5 / OM5 / DSM 1227.
[3]	"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).
[4]	"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).

Cross-references

Sequence databases

EMBLGenBankDDBJ

X82447 Genomic DNA. Translation: CAA57828.1.

PIR

B56279.

RefSeq

YP_015604.1.

3D structure databases

PDBMSD

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1N5W	X-ray	1.50	A/D	1-166	[»]
1N60	X-ray	1.19	A/D	1-166	[»]
1N61	X-ray	1.30	A/D	1-166	[»]
1N62	X-ray	1.09	A/D	1-166	[»]
1N63	X-ray	1.21	A/D	1-166	[»]
1ZXI	X-ray	1.70	A/D	1-166	[»]

ModBase

Search...

Genome annotation databases

GeneID

2807117.

Family and domain databases

InterPro

IPR002888. 2Fe-2S_bd.
IPR006058. 2Fe2S_fd_BS.
IPR001041. Ferredoxin.
[Graphical view]

Pfam

PF00111. Fer2. 1 hit.
PF01799. Fer2_2. 1 hit.
[Graphical view]

ProDom

PD186071. 2Fe-2S_bind. 1 hit.
[Graphical view] [Entries sharing at least one domain]

PROSITE

PS00197. 2FE2S_FER_1. False negative.
PS51085. 2FE2S_FER_2. 1 hit.
[Graphical view]

BLOCKS

Search...

Other Resources

ProtoNet

Search...

Entry information

Entry name

DCMS_OLICA

Accession

Primary (citable) accession number: P19921
Secondary accession number(s): Q51324

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1991
Last sequence update:	July 26, 2002
Last modified:	July 22, 2008
This is version 69 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)