ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry P31896

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

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name COOS_RHORU
Primary accession number P31896
Secondary accession numbers None
Integrated into Swiss-Prot on July 1, 1993
Sequence was last modified on July 1, 1993 (Sequence version 1)
Annotations were last modified on    September 2, 2008 (Entry version 63)
Name and origin of the protein
Protein name Carbon monoxide dehydrogenase
Synonyms CODH
EC 1.2.99.2
Gene name
Name: cooS
From
Rhodospirillum rubrum [TaxID: 1085] 
Taxonomy Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales; Rhodospirillaceae; Rhodospirillum.
Protein existence 1: Evidence at protein level;
References
[1]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
STRAIN=UR1;
PubMed=1644755 [NCBI, ExPASy, EBI, Israel, Japan]
Kerby R.L., Hong S.S., Ensign S.A., Coppoc L.J., Ludden P.W., Roberts G.P.;
"Genetic and physiological characterization of the Rhodospirillum rubrum carbon monoxide dehydrogenase system.";
J. Bacteriol. 174:5284-5294(1992).
[2]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=UR1;
PubMed=8626276 [NCBI, ExPASy, EBI, Israel, Japan]
Fox J.D., Kerby R.L., Roberts G.P., Ludden P.W.;
"Characterization of the CO-induced, CO-tolerant hydrogenase from Rhodospirillum rubrum and the gene encoding the large subunit of the enzyme.";
J. Bacteriol. 178:1515-1524(1996).
[3]
 MUTAGENESIS OF HIS-265.
DOI=10.1074/jbc.273.7.4059; PubMed=9461598 [NCBI, ExPASy, EBI, Israel, Japan]
Spangler N.J., Meyers M.R., Gierke K.L., Kerby R.L., Roberts G.P., Ludden P.W.;
"Substitution of valine for histidine 265 in carbon monoxide dehydrogenase from Rhodospirillum rubrum affects activity and spectroscopic states.";
J. Biol. Chem. 273:4059-4064(1998).
[4]
 MUTAGENESIS OF CYS-531.
DOI=10.1128/JB.184.21.5894-5897.2002; PubMed=12374822 [NCBI, ExPASy, EBI, Israel, Japan]
Heo J., Wolfe M.T., Staples C.R., Ludden P.W.;
"Converting the NiFeS carbon monoxide dehydrogenase to a hydrogenase and a hydroxylamine reductase.";
J. Bacteriol. 184:5894-5897(2002).
[5]
 REVIEW.
DOI=10.1146/annurev.mi.49.100195.001513; PubMed=8561463 [NCBI, ExPASy, EBI, Israel, Japan]
Ferry J.G.;
"CO dehydrogenase.";
Annu. Rev. Microbiol. 49:305-333(1995).
[6]
 X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
DOI=10.1073/pnas.211429998; PubMed=11593006 [NCBI, ExPASy, EBI, Israel, Japan]
Drennan C.L., Heo J., Sintchak M.D., Schreiter E., Ludden P.W.;
"Life on carbon monoxide: X-ray structure of Rhodospirillum rubrum Ni-Fe-S carbon monoxide dehydrogenase.";
Proc. Natl. Acad. Sci. U.S.A. 98:11973-11978(2001).
Comments
  • FUNCTION: Allows growth in a CO-dependent manner in the dark. CODH oxidizes carbon monoxide coupled, via cooF, to the reduction of a hydrogen cation by a hydrogenase (possibly cooH).
  • CATALYTIC ACTIVITY: CO + H2O + A = CO2 + AH2.
  • COFACTOR: Binds 3 4Fe-4S clusters per homodimer.
  • COFACTOR: Binds 2 nickel-iron-sulfur clusters per homodimer.
  • SUBUNIT: Homodimer.
  • SUBCELLULAR LOCATION: Cytoplasm. Cell inner membrane; Peripheral membrane protein; Cytoplasmic side. Note=Loosely attached to the inner membrane, probably via cooF (By similarity).
  • INDUCTION: By carbon monoxide; under anaerobic conditions.
  • 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.
  • MISCELLANEOUS: Methyl viologen can act as acceptor. Inactivated by O(2).
  • 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
U65510; AAC45123.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR C42957; C42957.
3D structure databases
PDB
1JQK; X-ray; 2.80 A; A/B/C/D/E/F=1-639.[ExPASy / RCSB / EBI]
PDBsum 1JQK; -.
DisProt DP00239; -.
ModBase P31896.
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 P31896.
Other
ProtoNet P31896.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; 4Fe-4S; Cell inner membrane; Cell membrane; Cytoplasm; Direct protein sequencing; Iron; Iron-sulfur; Membrane; Metal-binding; Nickel; Oxidoreductase.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   639  639     Carbon monoxide dehydrogenase. PRO_0000157139
METAL   41    41        Iron-sulfur 1 (4Fe-4S); shared with dimeric partner. 
METAL   49    49        Iron-sulfur 1 (4Fe-4S); shared with dimeric partner. 
METAL   50    50        Iron-sulfur 2 (4Fe-4S). 
METAL   53    53        Iron-sulfur 2 (4Fe-4S). 
METAL   58    58        Iron-sulfur 2 (4Fe-4S). 
METAL   72    72        Iron-sulfur 2 (4Fe-4S). 
METAL   265   265        Nickel-iron-sulfur (Ni-4Fe-4S); via tele nitrogen. 
METAL   300   300        Nickel-iron-sulfur (Ni-4Fe-4S). 
METAL   338   338        Nickel-iron-sulfur (Ni-4Fe-4S). 
METAL   451   451        Nickel-iron-sulfur (Ni-4Fe-4S). 
METAL   481   481        Nickel-iron-sulfur (Ni-4Fe-4S). 
METAL   531   531        Nickel-iron-sulfur (Ni-4Fe-4S). 
MUTAGEN   265   265        H->V: Great decrease in activity; diminishes incorporation of nickel. Displays hydroxylamine reductase activity. 
MUTAGEN   531   531        C->A: Displays hydrogenase activity. 
HELIX   30    37  8      
HELIX   42    46  5      
STRAND   62    66  5      
HELIX   76   109  34      
TURN   110   112  3      
HELIX   122   131  10      
TURN   137   139  3      
HELIX   141   154  14      
TURN   155   157  3      
HELIX   166   171  6      
HELIX   174   183  10      
HELIX   190   200  11      
HELIX   209   238  30      
STRAND   244   250  7      
STRAND   257   265  9      
HELIX   267   279  13      
TURN   280   282  3      
HELIX   283   286  4      
STRAND   292   298  7      
HELIX   299   308  10      
STRAND   313   315  3      
TURN   318   321  4      
HELIX   322   325  4      
STRAND   331   334  4      
STRAND   336   338  3      
HELIX   343   348  6      
STRAND   353   356  4      
STRAND   366   368  3      
HELIX   373   375  3      
HELIX   376   391  16      
STRAND   406   410  5      
HELIX   414   422  9      
HELIX   430   439  10      
STRAND   440   442  3      
STRAND   444   448  5      
HELIX   460   471  12      
STRAND   474   479  6      
HELIX   480   489  10      
HELIX   494   500  7      
HELIX   503   515  13      
STRAND   518   520  3      
STRAND   524   531  8      
HELIX   534   547  14      
TURN   552   554  3      
STRAND   555   561  7      
HELIX   567   579  13      
STRAND   582   587  6      
TURN   590   593  4      
HELIX   595   602  8      
HELIX   604   608  5      
STRAND   612   615  4      
HELIX   619   635  17      
Sequence information
Length: 639 AA [This is the length of the unprocessed precursor] Molecular weight: 66854 Da [This is the MW of the unprocessed precursor] CRC64: DCADD7C13D8D85B8 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MTHHDCAHCS SDACATEMLN LAEANSIETA WHRYEKQQPQ CGFGSAGLCC RICLKGPCRI 

        70         80         90        100        110        120 
DPFGEGPKYG VCGADRDTIV ARHLVRMIAA GTAAHSEHGR HIALAMQHIS QGELHDYSIR 

       130        140        150        160        170        180 
DEAKLYAIAK TLGVATEGRG LLAIVGDLAA ITLGDFQNQD YDKPCAWLAA SLTPRRVKRL 

       190        200        210        220        230        240 
GDLGLLPHNI DASVAQTMSR THVGCDADPT NLILGGLRVA MADLDGSMLA TELSDALFGT 

       250        260        270        280        290        300 
PQPVVSAANL GVMKRGAVNI AVNGHNPMLS DIICDVAADL RDEAIAAGAA EGINIIGICC 

       310        320        330        340        350        360 
TGHEVMMRHG VPLATNYLSQ ELPILTGALE AMVVDVQCIM PSLPRIAECF HTQIITTDKH 

       370        380        390        400        410        420 
NKISGATHVP FDEHKAVETA KTIIRMAIAA FGRRDPNRVA IPAFKQKSIV GFSAEAVVAA 

       430        440        450        460        470        480 
LAKVNADDPL KPLVDNVVNG NIQGIVLFVG CNTTKVQQDS AYVDLAKSLA KRNVLVLATG 

       490        500        510        520        530        540 
CAAGAFAKAG LMTSEATTQY AGEGLKGVLS AIGTAAGLGG PLPLVMHMGS CVDNSRAVAL 

       550        560        570        580        590        600 
ATALANKLGV DLSDLPLVAS APECMSEKAL AIGSWAVTIG LPTHVGSVPP VIGSQIVTKL 

       610        620        630 
VTETAKDLVG GYFIVDTDPK SAGDKLYAAI QERRAGLGL
P31896 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA) 		Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Hosted by kr flag YPRC Korea Mirror sites: Australia Brazil Canada China Switzerland
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!