Carbon monoxide dehydrogenase small chain - Oligotropha carboxidovorans (strain ATCC 49405 / DSM 1227 / OM5)

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P19921 (DCMS_OLICO) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 89. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

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:	coxS
Ordered Locus Names:	OCA5_pHCG300300

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	166 AA.
Sequence status	Complete.
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 Complete proteome Direct protein sequencing Plasmid
Gene Ontology (GO)
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 metal 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 – 166

166

Carbon monoxide dehydrogenase small chain

PRO_0000079817

Regions

Domain

4 – 80

2Fe-2S ferredoxin-type

Sites

Metal binding

Iron-sulfur 1 (2Fe-2S)

Metal binding

Iron-sulfur 1 (2Fe-2S)

Metal binding

Iron-sulfur 1 (2Fe-2S)

Metal binding

Iron-sulfur 1 (2Fe-2S)

Metal binding

102

Iron-sulfur 2 (2Fe-2S)

Metal binding

105

Iron-sulfur 2 (2Fe-2S)

Metal binding

137

Iron-sulfur 2 (2Fe-2S)

Metal binding

139

Iron-sulfur 2 (2Fe-2S)

Secondary structure

166

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P19921 [UniParc].

Last modified July 26, 2002. Version 2.
Checksum: E63AD31D726D22C1
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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

« Hide

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]. Strain: ATCC 49405 / DSM 1227 / OM5.
[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]. Strain: ATCC 49405 / DSM 1227 / OM5.
[3]	"Complete genome sequences of the chemolithoautotrophic Oligotropha carboxidovorans strains OM4 and OM5." Volland S., Rachinger M., Strittmatter A., Daniel R., Gottschalk G., Meyer O. J. Bacteriol. 193:5043-5043(2011) [PubMed: 21742883] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 49405 / DSM 1227 / OM5.
[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 1-21.
[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

EMBL
GenBank
DDBJ

CP002827 Genomic DNA. Translation: AEI08105.1.

PIR

B56279.

RefSeq

YP_004638432.1. NC_015689.1.
YP_015604.1. NC_005873.1.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

P19921.

SMR

P19921. Positions 3-163.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

10852781.
2807117.

GenomeReviews

Gene locus OCAR_p_08033 in contig X82447_GR.

Organism-specific databases

CMR

Search...

Phylogenomic databases

ProtClustDB

CLSK830307.

Family and domain databases

InterPro

IPR002888. 2Fe-2S-bd.
IPR012675. Beta-grasp_ferredoxin-type.
IPR001041. Ferredoxin.
[Graphical view]

Gene3D

G3DSA:1.10.150.120. 2Fe-2S-bd. 1 hit.
G3DSA:3.10.20.30. Ferredoxin_fold. 1 hit.

Pfam

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

SUPFAM

SSF47741. 2Fe-2S_bind. 1 hit.
SSF54292. Ferredoxin. 1 hit.

PROSITE

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

ProtoNet

Search...

Entry information

Entry name

DCMS_OLICO

Accession

Primary (citable) accession number: P19921
Secondary accession number(s): F8C0Z5, Q51324

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1991
Last sequence update:	July 26, 2002
Last modified:	January 25, 2012
This is version 89 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Family and domain databases

Entry information

Relevant documents