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Q9F8A8 (COOS2_CARHZ) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 79. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Carbon monoxide dehydrogenase 2
Short name=CODH 2
EC=1.2.99.2
Gene names
Name:cooS2
Synonyms:cooSII
Ordered Locus Names:CHY_0085
OrganismCarboxydothermus hydrogenoformans (strain Z-2901 / DSM 6008) [Complete proteome] [HAMAP]
Taxonomic identifier246194 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Clostridia › Thermoanaerobacterales › Thermoanaerobacteriaceae › Carboxydothermus

Protein attributes

Sequence length636 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

CODH oxidizes carbon monoxide coupled, via CooF, to the reduction of a hydrogen cation by a hydrogenase (possibly CooH) By similarity.

Catalytic activity

CO + H2O + A = CO2 + AH2.

Cofactor

Binds 3 4Fe-4S clusters per homodimer.

Binds 2 nickel-iron-sulfur clusters per homodimer.

Enzyme regulation

Inactivated by O2.

Subunit structure

Homodimer.

Subcellular location

Cytoplasm. Cell inner membrane; Peripheral membrane protein; Cytoplasmic side. Note: Loosely attached to the inner membrane, probably via CooF. Ref.3

Domain

Cluster B is an all-cysteinyl-liganded 4Fe4S cluster; cluster C is a mixed Ni-Fe-S cluster which appears to be the active site of CO oxidation. Cluster D is also an all-cysteinyl-liganded 4Fe4S cluster that bridges the two subunits of the CODH dimer.

Sequence similarities

Belongs to the Ni-containing carbon monoxide dehydrogenase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.3
Chain2 – 636635Carbon monoxide dehydrogenase 2
PRO_0000157138

Sites

Metal binding391Iron-sulfur 1 (4Fe-4S); shared with dimeric partner
Metal binding471Iron-sulfur 1 (4Fe-4S); shared with dimeric partner
Metal binding481Iron-sulfur 2 (4Fe-4S)
Metal binding511Iron-sulfur 2 (4Fe-4S)
Metal binding561Iron-sulfur 2 (4Fe-4S)
Metal binding701Iron-sulfur 2 (4Fe-4S)
Metal binding2611Nickel-iron-sulfur (Ni-4Fe-5S); via tele nitrogen
Metal binding2951Nickel-iron-sulfur (Ni-4Fe-5S)
Metal binding3331Nickel-iron-sulfur (Ni-4Fe-5S)
Metal binding4461Nickel-iron-sulfur (Ni-4Fe-5S)
Metal binding4761Nickel-iron-sulfur (Ni-4Fe-5S)
Metal binding5261Nickel-iron-sulfur (Ni-4Fe-5S)

Experimental info

Sequence conflict5281D → H in AAG29809. Ref.1
Sequence conflict5321A → S in AAG29809. Ref.1
Sequence conflict5441G → W in AAG29809. Ref.1
Sequence conflict5471L → M in AAG29809. Ref.1
Sequence conflict5581E → Q in AAG29809. Ref.1
Sequence conflict5831L → F in AAG29809. Ref.1
Sequence conflict615 – 6173ETA → VQQR in AAG29809. Ref.1
Sequence conflict6361W → R in AAG29809. Ref.1

Secondary structure

1 ................................................................................................. 636
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9F8A8 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: 61C1011E86022A63

FASTA63666,914
        10         20         30         40         50         60 
MAKQNLKSTD RAVQQMLDKA KREGIQTVWD RYEAMKPQCG FGETGLCCRH CLQGPCRINP 

        70         80         90        100        110        120 
FGDEPKVGIC GATAEVIVAR GLDRSIAAGA AGHSGHAKHL AHTLKKAVQG KAASYMIKDR 

       130        140        150        160        170        180 
TKLHSIAKRL GIPTEGQKDE DIALEVAKAA LADFHEKDTP VLWVTTVLPP SRVKVLSAHG 

       190        200        210        220        230        240 
LIPAGIDHEI AEIMHRTSMG CDADAQNLLL GGLRCSLADL AGCYMGTDLA DILFGTPAPV 

       250        260        270        280        290        300 
VTESNLGVLK ADAVNVAVHG HNPVLSDIIV SVSKEMENEA RAAGATGINV VGICCTGNEV 

       310        320        330        340        350        360 
LMRHGIPACT HSVSQEMAMI TGALDAMILD YQCIQPSVAT IAECTGTTVI TTMEMSKITG 

       370        380        390        400        410        420 
ATHVNFAEEA AVENAKQILR LAIDTFKRRK GKPVEIPNIK TKVVAGFSTE AIINALSKLN 

       430        440        450        460        470        480 
ANDPLKPLID NVVNGNIRGV CLFAGCNNVK VPQDQNFTTI ARKLLKQNVL VVATGCGAGA 

       490        500        510        520        530        540 
LMRHGFMDPA NVDELCGDGL KAVLTAIGEA NGLGGPLPPV LHMGSCVDNS RAVALVAALA 

       550        560        570        580        590        600 
NRLGVDLDRL PVVASAAEAM HEKAVAIGTW AVTIGLPTHI GVLPPITGSL PVTQILTSSV 

       610        620        630 
KDITGGYFIV ELDPETAADK LLAAINERRA GLGLPW

« Hide

References

« Hide 'large scale' references
[1]"Genetic analysis of Carboxydothermus hydrogenoformans carbon monoxide dehydrogenase genes cooF and cooS."
Gonzalez J.M., Robb F.T.
FEMS Microbiol. Lett. 191:243-247(2000) [PubMed: 11024270] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Life in hot carbon monoxide: the complete genome sequence of Carboxydothermus hydrogenoformans Z-2901."
Wu M., Ren Q., Durkin A.S., Daugherty S.C., Brinkac L.M., Dodson R.J., Madupu R., Sullivan S.A., Kolonay J.F., Nelson W.C., Tallon L.J., Jones K.M., Ulrich L.E., Gonzalez J.M., Zhulin I.B., Robb F.T., Eisen J.A.
PLoS Genet. 1:563-574(2005) [PubMed: 16311624] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Z-2901 / DSM 6008.
[3]"Two membrane-associated NiFeS-carbon monoxide dehydrogenases from the anaerobic carbon-monoxide-utilizing eubacterium Carboxydothermus hydrogenoformans."
Svetlitchnyi V., Peschel C., Acker G., Meyer O.
J. Bacteriol. 183:5134-5144(2001) [PubMed: 11489867] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-21, SUBCELLULAR LOCATION.
[4]"A genomic survey of the extreme thermophilic, CO-utilizing bacterium Carboxydothermus hydrogenoformans."
Gonzalez J.M., Robb F.T.
Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 217-429.
[5]"Crystal structure of a carbon monoxide dehydrogenase reveals a [Ni-4Fe-5S] cluster."
Dobbek H., Svetlitchnyi V., Gremer L., Huber R., Meyer O.
Science 293:1281-1285(2001) [PubMed: 11509720] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF249899 Genomic DNA. Translation: AAG29809.1.
CP000141 Genomic DNA. Translation: ABB15588.1.
AF244619 Genomic DNA. Translation: AAG23568.1.
RefSeqYP_358957.1. NC_007503.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1SU6X-ray1.64A2-635[»]
1SU7X-ray1.12A2-635[»]
1SU8X-ray1.10A2-635[»]
1SUFX-ray1.15A2-635[»]
3B51X-ray1.40X1-636[»]
3B52X-ray1.50X1-636[»]
3B53X-ray1.50X1-636[»]
3I39X-ray1.36X1-636[»]
ProteinModelPortalQ9F8A8.
SMRQ9F8A8. Positions 4-636.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ9F8A8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3727694.
GenomeReviewsGene locus CHY_0085 in contig CP000141_GR.
KEGGchy:CHY_0085.
NMPDRfig|246194.3.peg.655.
PATRIC21273367. VBICarHyd26463_0083.
TIGRCHY_0085.

Phylogenomic databases

eggNOGCOG1151.
HOGENOMHBG393174.
OMAGIPACTH.
ProtClustDBCLSK862738.

Enzyme and pathway databases

BioCycCHYD246194:CHY_0085-MONOMER.

Family and domain databases

InterProIPR016101. CO_DH_a-bundle.
IPR010047. CO_DH_cat.
IPR004137. Prismane.
IPR011254. Prismane-like.
IPR016099. Prismane-like_a/b-sand.
[Graphical view]
Gene3DG3DSA:1.20.1270.30. CO_DH_a-bundle. 1 hit.
G3DSA:3.40.50.2030. Prismane-like_a/b-sand. 2 hits.
KOK00198.
PfamPF03063. Prismane. 1 hit.
[Graphical view]
PIRSFPIRSF005023. CODH. 1 hit.
SUPFAMSSF56821. Prismane_like. 1 hit.
TIGRFAMsTIGR01702. CO_DH_cata. 1 hit.
ProtoNetSearch...

Entry information

Entry nameCOOS2_CARHZ
AccessionPrimary (citable) accession number: Q9F8A8
Secondary accession number(s): Q3AFX7, Q9F8L4
Entry history
Integrated into UniProtKB/Swiss-Prot: October 31, 2003
Last sequence update: January 23, 2007
Last modified: January 25, 2012
This is version 79 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents