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UniProtKB/Swiss-Prot entry P19913

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

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Entry information
Entry name DCML_HYDPS
Primary accession number P19913
Secondary accession number Q9RBR9
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 55)
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: cutL
From
Hydrogenophaga pseudoflava (Pseudomonas carboxydoflava) [TaxID: 47421] 
Taxonomy Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; Comamonadaceae; Hydrogenophaga.
Protein existence 1: Evidence at protein level;
References
[1]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA], COFACTOR, AND SUBUNIT.
PubMed=10482497 [NCBI, ExPASy, EBI, Israel, Japan]
Kang B.S., Kim Y.M.;
"Cloning and molecular characterization of the genes for carbon monoxide dehydrogenase and localization of molybdopterin, flavin adenine dinucleotide, and iron-sulfur centers in the enzyme of Hydrogenophaga pseudoflava.";
J. Bacteriol. 181:5581-5590(1999).
[2]
 PROTEIN SEQUENCE OF 1-9.
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]
 X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS).
DOI=10.1006/jmbi.2000.4023; PubMed=10966817 [NCBI, ExPASy, EBI, Israel, Japan]
Haenzelmann P., Dobbek H., Gremer L., Huber R., Meyer O.;
"The effect of intracellular molybdenum in Hydrogenophaga pseudoflava on the crystallographic structure of the seleno-molybdo-iron-sulfur flavoenzyme carbon monoxide dehydrogenase.";
J. Mol. Biol. 301:1221-1235(2000).
[4]
 REVIEW.
DOI=10.1515/BC.2000.108; PubMed=11076018 [NCBI, ExPASy, EBI, Israel, Japan]
Meyer O., Gremer L., Ferner R., Ferner M., Dobbek H., Gnida M., Meyer-Klaucke W., Huber R.;
"The role of Se, Mo and Fe in the structure and function of carbon monoxide dehydrogenase.";
Biol. Chem. 381:865-876(2000).
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
U80806; AAD00363.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR PL0139; PL0139.
3D structure databases
PDB
1FFU; X-ray; 2.35 A; B/E=1-803.[ExPASy / RCSB / EBI]
1FFV; X-ray; 2.25 A; B/E=1-803.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1FFU; -.
1FFV; -.
ModBase P19913.
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 P19913.
ProtoNet P19913.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Copper; Direct protein sequencing; Hydroxylation; Metal-binding; Molybdenum; Oxidoreductase.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   803  803     Carbon monoxide dehydrogenase large chain. PRO_0000079809
METAL   385   385        Copper. 
METAL   757   757        Molybdenum. 
MOD_RES   384   384        4-hydroxyarginine. 
HELIX   8    15  8      
TURN   16    16  1      
TURN   18    19  2      
HELIX   27    30  4      
TURN   31    33  3      
HELIX   38    40  3      
TURN   44    45  2      
STRAND   47    53  7      
STRAND   59    65  7      
HELIX   67    71  5      
TURN   73    74  2      
STRAND   75    79  5      
HELIX   81    84  4      
HELIX   85    87  3      
TURN   88    88  1      
STRAND   91    93  3      
TURN   95    96  2      
STRAND   99   101  3      
TURN   111   112  2      
STRAND   114   120  7      
HELIX   123   132  10      
STRAND   134   139  6      
HELIX   146   149  4      
TURN   150   150  1      
TURN   152   153  2      
HELIX   159   161  3      
TURN   162   163  2      
TURN   168   169  2      
TURN   175   176  2      
STRAND   177   184  8      
HELIX   186   195  10      
STRAND   198   206  9      
STRAND   218   224  7      
TURN   225   228  4      
STRAND   229   234  6      
HELIX   239   250  12      
HELIX   254   256  3      
STRAND   257   260  4      
TURN   268   271  4      
HELIX   276   288  13      
TURN   289   289  1      
STRAND   292   295  4      
HELIX   298   304  7      
STRAND   311   319  9      
TURN   321   322  2      
STRAND   325   335  11      
TURN   346   347  2      
TURN   349   352  4      
HELIX   353   355  3      
TURN   356   359  4      
STRAND   364   372  9      
TURN   386   388  3      
HELIX   389   407  19      
TURN   408   408  1      
TURN   411   412  2      
HELIX   413   418  6      
HELIX   422   424  3      
TURN   430   431  2      
HELIX   440   451  12      
TURN   452   452  1      
HELIX   453   465  13      
TURN   467   468  2      
STRAND   471   481  11      
TURN   489   491  3      
TURN   495   496  2      
STRAND   501   507  7      
TURN   509   510  2      
STRAND   513   517  5      
HELIX   526   538  13      
TURN   539   539  1      
HELIX   542   544  3      
STRAND   545   548  4      
TURN   552   554  3      
TURN   563   564  2      
HELIX   566   592  27      
TURN   593   594  2      
HELIX   597   599  3      
STRAND   600   602  3      
STRAND   606   609  4      
TURN   613   614  2      
STRAND   616   618  3      
HELIX   619   628  10      
TURN   632   633  2      
STRAND   638   644  7      
STRAND   653   663  11      
TURN   664   666  3      
STRAND   669   679  11      
HELIX   686   705  20      
TURN   706   706  1      
TURN   713   714  2      
TURN   722   724  3      
TURN   730   732  3      
STRAND   737   740  4      
TURN   746   747  2      
TURN   749   750  2      
TURN   756   757  2      
HELIX   758   775  18      
HELIX   776   778  3      
TURN   779   779  1      
HELIX   789   798  10      
TURN   799   800  2      
Sequence information
Length: 803 AA [This is the length of the unprocessed precursor] Molecular weight: 87229 Da [This is the MW of the unprocessed precursor] CRC64: 3CD5FE205DBE0712 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MNAPVQDAEA RELALAGMRP RACAKEDARF IQGKGNYVDD IKMPGMLHMD IVRAPIAHGR 

        70         80         90        100        110        120 
IKKIHKDAAL AMPGVHAVLT AEDLKPLKLH WMPTLAGDVA AVLADEKVHF QMQEVAIVIA 

       130        140        150        160        170        180 
DDRYIAADAV EAVKVEYDEL PVVIDPIDAL KPDAPVLRED LAGKTSGAHG PREHHNHIFT 

       190        200        210        220        230        240 
WGAGDKAATD AVFANAPVTV SQHMYYPRVH PCPLETCGCV ASFDPIKGDL TTYITSQAPH 

       250        260        270        280        290        300 
VVRTVVSMLS GIPESKVRIV SPDIGGGFGN KVGIYPGYVC AIVASIVLGR PVKWVEDRVE 

       310        320        330        340        350        360 
NISTTAFARD YHMDGELAAT PDGKILGLRV NVVADHGAFD ACADPTKFPA GLFHICSGSY 

       370        380        390        400        410        420 
DIPRAHCSVK GVYTNKAPGG VAYRCSFRVT EAVYLIERMV DVLAQKLNMD KAEIRAKNFI 

       430        440        450        460        470        480 
RKEQFPYTTQ FGFEYDSGDY HTALKKVLDA VDYPAWRAEQ AARRADPNSP TLMGIGLVTF 

       490        500        510        520        530        540 
TEVVGAGPSK MCDILGVGMF DSCEIRIHPT GSAIARMGTI TQGQGHQTTY AQIIATELGI 

       550        560        570        580        590        600 
PSEVIQVEEG DTSTAPYGLG TYGSRSTPVA GAAIALAARK IHAKARKIAA HMLEVNENDL 

       610        620        630        640        650        660 
DWEVDRFKVK GDDSKFKTMA DIAWQAYHQP PAGLEPGLEA VHYYDPPNFT YPFGIYLCVV 

       670        680        690        700        710        720 
DIDRATGETK VRRFYALDDC GTRINPMIIE GQIHGGLTEG YAVAMGQQMP FDAQGNLLGN 

       730        740        750        760        770        780 
TLMDYFLPTA VETPHWETDH TVTPSPHHPI GAKGVAESPH VGSIPTFTAA VVDAFAHVGV 

       790        800 
THLDMPHTSY RVWKSLKEHN LAL
P19913 in FASTA format

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