Reviewed, UniProtKB/Swiss-Prot P19915 (DCMS_HYDPS)

Names and origin

Protein names

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

Gene names

Name:

cutS

Organism

Hydrogenophaga pseudoflava (Pseudomonas carboxydoflava)

Taxonomic identifier

47421 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Comamonadaceae › Hydrogenophaga

Protein attributes

Sequence length	163 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 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
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	2 iron, 2 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW carbon-monoxide dehydrogenase (acceptor) activity Inferred from electronic annotation. Source: EC electron carrier activity Inferred from electronic annotation. Source: InterPro iron ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 163

163

Carbon monoxide dehydrogenase small chain

PRO_0000079816

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

101

1

Iron-sulfur 2 (2Fe-2S)

Metal binding

104

1

Iron-sulfur 2 (2Fe-2S)

Metal binding

136

1

Iron-sulfur 2 (2Fe-2S)

Metal binding

138

1

Iron-sulfur 2 (2Fe-2S)

Experimental info

Sequence conflict

11

1

Missing AA sequence Ref.2

Secondary structure

1

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163

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

88 – 95

8

Helix

105 – 118

14

Helix

124 – 130

7

Turn

131 – 133

3

Beta strand

137 – 139

3

Helix

142 – 155

14

Sequences

	Sequence		Length	Mass (Da)
	P19915-1 [UniParc]. Last modified July 11, 2002. Version 2. Checksum: 9307050CC033410C	FASTA	163	17,752
	10 20 30 40 50 60 MAKKIITVNV NGKAQEKAVE PRTLLIHFLR EELNLTGAHI GCETSHCGAC TVDIDGRSVK 70 80 90 100 110 120 SCTHLAVQCD GSEVLTVEGL ANKGVLHAVR EGFYKEHGLQ CGFCTPGMLM RAYRFLQENP 130 140 150 160 NPTEAEIRMG MTGNLCRCTG YQNIVKAVQY AARKLQEPST AAA

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 1-21.
[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: AAD00362.1.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1FFU	X-ray	2.35	A/D	1-163	[»]
1FFV	X-ray	2.25	A/D	1-163	[»]

ModBase

Search...

Enzyme and pathway databases

BRENDA

1.2.99.2. 2857.

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]

ProtoNet

Search...

Entry information

Entry name

DCMS_HYDPS

Accession

Primary (citable) accession number: P19915
Secondary accession number(s): Q9ZAR6

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1991
Last sequence update:	July 11, 2002
Last modified:	January 20, 2009
This is version 68 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)