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Reviewed, UniProtKB/Swiss-Prot P19913 (DCML_HYDPS)

Last modified February 9, 2010. Version 61. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Carbon monoxide dehydrogenase large chain
      Short name=CO dehydrogenase subunit L
      Short name=CO-DH L
    EC=1.2.99.2
Gene names
Name: cutL
OrganismHydrogenophaga pseudoflava (Pseudomonas carboxydoflava)
Taxonomic identifier47421 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Comamonadaceae › Hydrogenophaga

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Protein attributes

Sequence length803 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level.

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General annotation (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. Ref.1

Binds 1 Mo6+ ion per subunit. Ref.1

Binds 1 molybdopterin cytosine dinucleotide (MCD) per subunit. Ref.1

Subunit structure

Dimer of heterotrimers. Each heterotrimer consists of a large, a medium and a small subunit. Ref.1

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 803803Carbon monoxide dehydrogenase large chain
PRO_0000079809

Sites

Metal binding3851Copper
Metal binding7571Molybdenum

Amino acid modifications

Modified residue38414-hydroxyarginine

Secondary structure

1 ............................................................................................................................................................................. 803
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
P19913-1 [UniParc].

Last modified July 11, 2002. Version 2.
Checksum: 3CD5FE205DBE0712

FASTA80387,229
        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

« Hide

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References

[1]"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."
Kang B.S., Kim Y.M.
J. Bacteriol. 181:5581-5590(1999) [PubMed: 10482497] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], COFACTOR, SUBUNIT.
[2]"Homology and distribution of CO dehydrogenase structural genes in carboxydotrophic bacteria."
Kraut M., Hugendieck I., Herwig S., Meyer O.
Arch. Microbiol. 152:335-341(1989) [PubMed: 2818128] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-9.
[3]"The effect of intracellular molybdenum in Hydrogenophaga pseudoflava on the crystallographic structure of the seleno-molybdo-iron-sulfur flavoenzyme carbon monoxide dehydrogenase."
Haenzelmann P., Dobbek H., Gremer L., Huber R., Meyer O.
J. Mol. Biol. 301:1221-1235(2000) [PubMed: 10966817] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS).
[4]"The role of Se, Mo and Fe in the structure and function of carbon monoxide dehydrogenase."
Meyer O., Gremer L., Ferner R., Ferner M., Dobbek H., Gnida M., Meyer-Klaucke W., Huber R.
Biol. Chem. 381:865-876(2000) [PubMed: 11076018] [Abstract]
Cited for: REVIEW.

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		U80806 Genomic DNA. Translation: AAD00363.1.
PIRPL0139.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1FFUX-ray2.35B/E1-803[»]
1FFVX-ray2.25B/E1-803[»]
ModBaseSearch...

Enzyme and pathway databases

BRENDA1.2.2.4. 2857.
1.2.99.2. 2857.

Family and domain databases

InterProIPR000674. Ald_Oxase/Xan_DH_a/b.
IPR008274. AldOxase/xan_DH_Mopterin-bd.
IPR012780. CO_Mo_DH_lsu.
[Graphical view]
Gene3DG3DSA:3.30.365.10. Ald_xan_DH_mo_bd. 3 hits.
G3DSA:3.90.1170.50. Aldxan_DH_hamm. 1 hit.
PfamPF01315. Ald_Xan_dh_C. 1 hit.
PF02738. Ald_Xan_dh_C2. 1 hit.
[Graphical view]
TIGRFAMsTIGR02416. CO_dehy_Mo_lg. 1 hit.
ProtoNetSearch...

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Entry information

Entry nameDCML_HYDPS
AccessionPrimary (citable) accession number: P19913
Secondary accession number(s): Q9RBR9
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: July 11, 2002
Last modified: February 9, 2010
This is version 61 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents