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UniProtKB/Swiss-Prot entry Q9F8A8

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name COOS2_CARHZ
Primary accession number Q9F8A8
Secondary accession numbers Q3AFX7 Q9F8L4
Integrated into Swiss-Prot on October 31, 2003
Sequence was last modified on January 23, 2007 (Sequence version 4)
Annotations were last modified on    July 22, 2008 (Entry version 53)
Name and origin of the protein
Protein name Carbon monoxide dehydrogenase 2
Synonyms CODH 2
EC 1.2.99.2
Gene name
Name: cooS2
Synonyms: cooSII
OrderedLocusNames: CHY_0085
From
Carboxydothermus hydrogenoformans (strain Z-2901 / DSM 6008) [TaxID: 246194] [HAMAP proteome]
Taxonomy Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales; Thermoanaerobacteraceae; Carboxydothermus.
Protein existence 1: Evidence at protein level;
References
[1]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=11024270 [NCBI, ExPASy, EBI, Israel, Japan]
Gonzalez J.M., Robb F.T.;
"Genetic analysis of Carboxydothermus hydrogenoformans carbon monoxide dehydrogenase genes cooF and cooS.";
FEMS Microbiol. Lett. 191:243-247(2000).
[2]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1371/journal.pgen.0010065; PubMed=16311624 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Life in hot carbon monoxide: the complete genome sequence of Carboxydothermus hydrogenoformans Z-2901.";
PLoS Genet. 1:563-574(2005).
[3]
 PROTEIN SEQUENCE OF 2-21, AND SUBCELLULAR LOCATION.
DOI=10.1128/JB.183.17.5134-5144.2001; PubMed=11489867 [NCBI, ExPASy, EBI, Israel, Japan]
Svetlitchnyi V., Peschel C., Acker G., Meyer O.;
"Two membrane-associated NiFeS-carbon monoxide dehydrogenases from the anaerobic carbon-monoxide-utilizing eubacterium Carboxydothermus hydrogenoformans.";
J. Bacteriol. 183:5134-5144(2001).
[4]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 217-429.
Gonzalez J.M., Robb F.T.;
"A genomic survey of the extreme thermophilic, CO-utilizing bacterium Carboxydothermus hydrogenoformans.";
Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
[5]
 X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS).
DOI=10.1126/science.1061500; PubMed=11509720 [NCBI, ExPASy, EBI, Israel, Japan]
Dobbek H., Svetlitchnyi V., Gremer L., Huber R., Meyer O.;
"Crystal structure of a carbon monoxide dehydrogenase reveals a [Ni-4Fe-5S] cluster.";
Science 293:1281-1285(2001).
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.
  • COFACTOR: Binds 2 nickel-iron-sulfur clusters per homodimer.
  • ENZYME REGULATION: Inactivated by O(2).
  • SUBUNIT: Homodimer.
  • SUBCELLULAR LOCATION: Cytoplasm. Cell inner membrane; Peripheral membrane protein; Cytoplasmic side. Note=Loosely attached to the inner membrane, probably via cooF.
  • 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.
  • SIMILARITY: Belongs to the Ni-containing carbon monoxide dehydrogenase family.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AF249899; AAG29809.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CP000141; ABB15588.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF244619; AAG23568.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq YP_358957.1; -.
3D structure databases
PDB
1SU6; X-ray; 1.64 A; A=1-636.[ExPASy / RCSB / EBI]
1SU7; X-ray; 1.12 A; A=1-636.[ExPASy / RCSB / EBI]
1SU8; X-ray; 1.10 A; A=1-636.[ExPASy / RCSB / EBI]
1SUF; X-ray; 1.15 A; A=1-636.[ExPASy / RCSB / EBI]
3B51; X-ray; 1.40 A; X=1-636.[ExPASy / RCSB / EBI]
3B52; X-ray; 1.50 A; X=1-636.[ExPASy / RCSB / EBI]
3B53; X-ray; 1.50 A; X=1-636.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1SU6; -.
1SU7; -.
1SU8; -.
1SUF; -.
3B51; -.
3B52; -.
3B53; -.
ModBase Q9F8A8.
Enzyme and pathway databases
BioCyc CHYD246194:CHY_0085-MON; -.
Ontologies
GO
GO:0005886; Cellular component: plasma membrane (inferred from electronic annotation from UniProtKB-SubCell).
QuickGo view.
Family and domain databases
InterPro IPR016101; CO_DHase_a-bundle.
IPR010047; CO_DHase_cat.
IPR004137; Prismane.
IPR016099; Prismane-like_a/b-sand.
Graphical view of domain structure.
Gene3D G3DSA:1.20.1270.30; CO_DH_a-bundle; 1.
G3DSA:3.40.50.2030; Prismane-like_a/b-sand; 1.
Pfam PF03063; Prismane; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF005023; CODH; 1.
TIGRFAMs TIGR01702; CO_DH_cata; 1.
BLOCKS Q9F8A8.
Genome annotation databases
GeneID 3727694; -.
GenomeReviews CP000141_GR; CHY_0085.
KEGG chy:CHY_0085; -.
NMPDR fig|246194.3.peg.655; -.
TIGR CHY_0085; -.
Phylogenomic databases
HOGENOM Q9F8A8; -.
Other
ProtoNet Q9F8A8.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; 4Fe-4S; Cell inner membrane; Cell membrane; Complete proteome; Cytoplasm; Direct protein sequencing; Iron; Iron-sulfur; Membrane; Metal-binding; Nickel; Oxidoreductase.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed. 
CHAIN   2   636  635     Carbon monoxide dehydrogenase 2. PRO_0000157138
METAL   39    39        Iron-sulfur 1 (4Fe-4S) (shared with dimeric partner). 
METAL   47    47        Iron-sulfur 1 (4Fe-4S) (shared with dimeric partner). 
METAL   48    48        Iron-sulfur 2 (4Fe-4S). 
METAL   51    51        Iron-sulfur 2 (4Fe-4S). 
METAL   56    56        Iron-sulfur 2 (4Fe-4S). 
METAL   70    70        Iron-sulfur 2 (4Fe-4S). 
METAL   261   261        Nickel-iron-sulfur (Ni-4Fe-5S) (via tele nitrogen). 
METAL   295   295        Nickel-iron-sulfur (Ni-4Fe-5S). 
METAL   333   333        Nickel-iron-sulfur (Ni-4Fe-5S). 
METAL   446   446        Nickel-iron-sulfur (Ni-4Fe-5S). 
METAL   476   476        Nickel-iron-sulfur (Ni-4Fe-5S). 
METAL   526   526        Nickel-iron-sulfur (Ni-4Fe-5S). 
CONFLICT   528   528        D -> H (in Ref. 1; AAG29809). 
CONFLICT   532   532        A -> S (in Ref. 1; AAG29809). 
CONFLICT   544   544        G -> W (in Ref. 1; AAG29809). 
CONFLICT   547   547        L -> M (in Ref. 1; AAG29809). 
CONFLICT   558   558        E -> Q (in Ref. 1; AAG29809). 
CONFLICT   583   583        L -> F (in Ref. 1; AAG29809). 
CONFLICT   615   617        ETA -> VQQR (in Ref. 1; AAG29809). 
CONFLICT   636   636        W -> R (in Ref. 1; AAG29809). 
TURN   5     7  3      
HELIX   11    23  13      
HELIX   28    35  8      
HELIX   40    44  5      
STRAND   60    64  5      
HELIX   74   108  35      
HELIX   120   130  11      
HELIX   139   152  14      
HELIX   162   165  4      
HELIX   170   178  9      
HELIX   186   196  11      
HELIX   205   234  30      
STRAND   240   245  6      
HELIX   246   248  3      
STRAND   253   261  9      
HELIX   263   275  13      
HELIX   277   282  6      
STRAND   288   293  6      
HELIX   294   304  11      
STRAND   308   310  3      
HELIX   312   314  3      
HELIX   315   320  6      
STRAND   324   329  6      
STRAND   331   333  3      
HELIX   337   345  9      
STRAND   348   351  4      
STRAND   361   363  3      
HELIX   368   370  3      
HELIX   371   388  18      
TURN   389   391  3      
STRAND   401   405  5      
HELIX   409   417  9      
HELIX   425   434  10      
STRAND   435   437  3      
STRAND   440   443  4      
HELIX   455   466  12      
STRAND   470   474  5      
HELIX   475   483  9      
TURN   484   487  4      
HELIX   489   491  3      
HELIX   492   495  4      
HELIX   498   510  13      
STRAND   519   526  8      
HELIX   529   543  15      
HELIX   547   549  3      
STRAND   550   556  7      
HELIX   562   574  13      
STRAND   577   580  4      
TURN   585   588  4      
HELIX   590   597  8      
TURN   598   600  3      
HELIX   601   604  4      
STRAND   607   610  4      
HELIX   614   631  18      
Sequence information
Length: 636 AA [This is the length of the unprocessed precursor] Molecular weight: 66914 Da [This is the MW of the unprocessed precursor] CRC64: 61C1011E86022A63 [This is a checksum on the sequence] 
        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
Q9F8A8 in FASTA format

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