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UniProtKB/Swiss-Prot entry P19919

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

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Entry information
Entry name DCML_OLICA
Primary accession number P19919
Secondary accession number Q51325
Integrated into Swiss-Prot on February 1, 1991
Sequence was last modified on July 11, 2002 (Sequence version 2)
Annotations were last modified on    November 4, 2008 (Entry version 64)
Name and origin of the protein
Protein name Carbon monoxide dehydrogenase large chain
Synonyms CO dehydrogenase subunit L
CO-DH L
EC 1.2.99.2
Gene name
Name: coxL
From
Oligotropha carboxidovorans (Pseudomonas carboxydovorans) [TaxID: 40137] 
Encoded on Plasmid megaplasmid pHCG3.
Taxonomy Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; Bradyrhizobiaceae; Oligotropha.
Protein existence 1: Evidence at protein level;
References
[1]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=CH5 / OM5 / DSM 1227;
PubMed=7721710 [NCBI, ExPASy, EBI, Israel, Japan]
Schuebel U., Kraut M., Moersdorf G., Meyer O.;
"Molecular characterization of the gene cluster coxMSL encoding the molybdenum-containing carbon monoxide dehydrogenase of Oligotropha carboxidovorans.";
J. Bacteriol. 177:2197-2203(1995).
[2]
 PROTEIN SEQUENCE OF 1-13.
STRAIN=CH5 / OM5 / DSM 1227;
DOI=10.1007/BF00425170; PubMed=2818128 [NCBI, ExPASy, EBI, Israel, Japan]
Kraut M., Hugendieck I., Herwig S., Meyer O.;
"Homology and distribution of CO dehydrogenase structural genes in carboxydotrophic bacteria.";
Arch. Microbiol. 152:335-341(1989).
[3]
 CHARACTERIZATION OF ACTIVE SITE.
DOI=10.1021/bi026514n; PubMed=12515558 [NCBI, ExPASy, EBI, Israel, Japan]
Gnida M., Ferner R., Gremer L., Meyer O., Meyer-Klaucke W.;
"A novel binuclear [CuSMo] cluster at the active site of carbon monoxide dehydrogenase: characterization by X-ray absorption spectroscopy.";
Biochemistry 42:222-230(2003).
[4]
 X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
DOI=10.1073/pnas.96.16.8884; PubMed=10430865 [NCBI, ExPASy, EBI, Israel, Japan]
Dobbek H., Gremer L., Meyer O., Huber R.;
"Crystal structure and mechanism of CO dehydrogenase, a molybdo iron-sulfur flavoprotein containing S-selanylcysteine.";
Proc. Natl. Acad. Sci. U.S.A. 96:8884-8889(1999).
[5]
 X-RAY CRYSTALLOGRAPHY (1.09 ANGSTROMS).
DOI=10.1073/pnas.212640899; PubMed=12475995 [NCBI, ExPASy, EBI, Israel, Japan]
Dobbek H., Gremer L., Kiefersauer R., Huber R., Meyer O.;
"Catalysis at a dinuclear CuSMo(==O)OH cluster in a CO dehydrogenase resolved at 1.1-A resolution.";
Proc. Natl. Acad. Sci. U.S.A. 99:15971-15976(2002).
Comments
  • FUNCTION: Catalyzes the oxidation of carbon monoxide to carbon dioxide.
  • CATALYTIC ACTIVITY: CO + H2O + A = CO2 + AH2.
  • COFACTOR: Binds 1 Cu(+) ion per subunit.
  • COFACTOR: Binds 1 Mo(6+) ion per subunit.
  • COFACTOR: Binds 1 molybdopterin cytosine dinucleotide (MCD) per subunit.
  • SUBUNIT: Dimer of heterotrimers. Each heterotrimer consists of a large, a medium and a small subunit.
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
X82447; CAA57829.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR C56279; C56279.
RefSeq YP_015605.1; -.
3D structure databases
PDB
1N5W; X-ray; 1.50 A; B/E=1-809.[ExPASy / RCSB / EBI]
1N60; X-ray; 1.19 A; B/E=1-809.[ExPASy / RCSB / EBI]
1N61; X-ray; 1.30 A; B/E=1-809.[ExPASy / RCSB / EBI]
1N62; X-ray; 1.09 A; B/E=1-809.[ExPASy / RCSB / EBI]
1N63; X-ray; 1.21 A; B/E=1-809.[ExPASy / RCSB / EBI]
1ZXI; X-ray; 1.70 A; B/E=1-809.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1N5W; -.
1N60; -.
1N61; -.
1N62; -.
1N63; -.
1ZXI; -.
ModBase P19919.
Ontologies
GO
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR000674; Ald_Oxase/Xan_DHase_a/b.
IPR008274; AldOxase/xan_DHase_Mopterin-bd.
IPR012780; CO_Mo_DHase_lsu.
Graphical view of domain structure.
Gene3D G3DSA:3.30.365.10; Ald_xan_DH_mo_bd; 3.
G3DSA:3.90.1170.50; Aldxan_DH_hamm; 1.
Pfam PF01315; Ald_Xan_dh_C; 1.
PF02738; Ald_Xan_dh_C2; 1.
Pfam graphical view of domain structure.
TIGRFAMs TIGR02416; CO_dehy_Mo_lg; 1.
BLOCKS P19919.
ProtoNet P19919.
Genome annotation databases
GeneID 2807115; -.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Copper; Direct protein sequencing; Metal-binding; Molybdenum; Oxidoreductase; Plasmid.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   809  809     Carbon monoxide dehydrogenase large chain. PRO_0000079810
METAL   388   388        Copper. 
METAL   763   763        Molybdenum. 
CONFLICT   6     6        Missing (in Ref. 2; AA sequence). 
CONFLICT   11    12        SA -> AG (in Ref. 2; AA sequence). 
HELIX   11    18  8      
HELIX   30    33  4      
TURN   34    36  3      
HELIX   41    43  3      
STRAND   50    56  7      
STRAND   60    68  9      
HELIX   70    74  5      
STRAND   78    82  5      
HELIX   84    87  4      
HELIX   88    90  3      
STRAND   93    96  4      
STRAND   100   106  7      
STRAND   108   111  4      
STRAND   117   125  9      
HELIX   126   135  10      
STRAND   137   142  6      
HELIX   149   151  3      
HELIX   162   164  3      
STRAND   180   187  8      
HELIX   189   198  10      
STRAND   200   209  10      
STRAND   221   227  7      
TURN   228   231  4      
STRAND   232   237  6      
HELIX   242   253  12      
HELIX   257   259  3      
STRAND   260   263  4      
TURN   271   274  4      
HELIX   279   291  13      
STRAND   295   298  4      
HELIX   301   307  7      
STRAND   314   322  9      
STRAND   328   338  11      
TURN   352   355  4      
HELIX   356   358  3      
TURN   359   362  4      
STRAND   368   375  8      
STRAND   382   384  3      
TURN   389   391  3      
HELIX   392   410  19      
HELIX   414   421  8      
HELIX   425   427  3      
STRAND   429   431  3      
HELIX   443   454  12      
HELIX   456   472  17      
STRAND   476   487  12      
TURN   495   497  3      
STRAND   507   513  7      
STRAND   519   524  6      
STRAND   528   530  3      
HELIX   532   544  13      
HELIX   548   550  3      
STRAND   551   554  4      
TURN   558   560  3      
TURN   572   575  4      
HELIX   576   599  24      
HELIX   603   605  3      
STRAND   606   608  3      
STRAND   610   615  6      
STRAND   618   624  7      
HELIX   625   634  10      
STRAND   645   650  6      
STRAND   659   669  11      
TURN   670   672  3      
STRAND   675   685  11      
HELIX   692   711  20      
STRAND   723   725  3      
TURN   728   730  3      
TURN   736   738  3      
STRAND   743   746  4      
HELIX   764   782  19      
TURN   783   785  3      
HELIX   795   804  10      
TURN   805   808  4      
Sequence information
Length: 809 AA [This is the length of the unprocessed precursor] Molecular weight: 88739 Da [This is the MW of the unprocessed precursor] CRC64: 7F2F3D0EC996BDBD [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MNIQTTVEPT SAERAEKLQG MGCKRKRVED IRFTQGKGNY VDDVKLPGML FGDFVRSSHA 

        70         80         90        100        110        120 
HARIKSIDTS KAKALPGVFA VLTAADLKPL NLHYMPTLAG DVQAVLADEK VLFQNQEVAF 

       130        140        150        160        170        180 
VVAKDRYVAA DAIELVEVDY EPLPVLVDPF KAMEPDAPLL REDIKDKMTG AHGARKHHNH 

       190        200        210        220        230        240 
IFRWEIGDKE GTDATFAKAE VVSKDMFTYH RVHPSPLETC QCVASMDKIK GELTLWGTFQ 

       250        260        270        280        290        300 
APHVIRTVVS LISGLPEHKI HVIAPDIGGG FGNKVGAYSG YVCAVVASIV LGVPVKWVED 

       310        320        330        340        350        360 
RMENLSTTSF ARDYHMTTEL AATKDGKILA MRCHVLADHG AFDACADPSK WPAGFMNICT 

       370        380        390        400        410        420 
GSYDMPVAHL AVDGVYTNKA SGGVAYRCSF RVTEAVYAIE RAIETLAQRL EMDSADLRIK 

       430        440        450        460        470        480 
NFIQPEQFPY MAPLGWEYDS GNYPLAMKKA MDTVGYHQLR AEQKAKQEAF KRGETREIMG 

       490        500        510        520        530        540 
IGISFFTEIV GAGPSKNCDI LGVSMFDSAE IRIHPTGSVI ARMGTKSQGQ GHETTYAQII 

       550        560        570        580        590        600 
ATELGIPADD IMIEEGNTDT APYGLGTYGS RSTPTAGAAT AVAARKIKAK AQMIAAHMLE 

       610        620        630        640        650        660 
VHEGDLEWDV DRFRVKGLPE KFKTMKELAW ASYNSPPPNL EPGLEAVNYY DPPNMTYPFG 

       670        680        690        700        710        720 
AYFCIMDIDV DTGVAKTRRF YALDDCGTRI NPMIIEGQVH GGLTEAFAVA MGQEIRYDEQ 

       730        740        750        760        770        780 
GNVLGASFMD FFLPTAVETP KWETDYTVTP SPHHPIGAKG VGESPHVGGV PCFSNAVNDA 

       790        800 
YAFLNAGHIQ MPHDAWRLWK VGEQLGLHV
P19919 in FASTA format

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