Skip Header

 
Contribute Send feedback
Read comments (1) or add your own

Reviewed, UniProtKB/Swiss-Prot P19919 (DCML_OLICO)

Last modified June 16, 2009. Version 69. 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

Hide | Top

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: coxL
Ordered Locus Names: OCAR_p_08034
Encoded onPlasmid megaplasmid pHCG3
OrganismOligotropha carboxidovorans (strain ATCC 49405 / DSM 1227 / OM5) [Complete proteome] [HAMAP]
Taxonomic identifier504832 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Bradyrhizobiaceae › Oligotropha

Hide | Top

Protein attributes

Sequence length809 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

Hide | Top

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.

Binds 1 Mo6+ ion per subunit.

Binds 1 molybdopterin cytosine dinucleotide (MCD) per subunit.

Subunit structure

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

Hide | Top

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 809809Carbon monoxide dehydrogenase large chain
PRO_0000079810

Sites

Metal binding3881Copper
Metal binding7631Molybdenum

Experimental info

Sequence conflict61Missing AA sequence Ref.3
Sequence conflict11 – 122SA → AG AA sequence Ref.3

Secondary structure

1 ..................................................................................................................................... 809
Helix Strand Turn

Details...

Hide | Top

Sequences

Sequence LengthMass (Da)Tools
P19919-1 [UniParc].

Last modified July 11, 2002. Version 2.
Checksum: 7F2F3D0EC996BDBD

FASTA80988,739
        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

« Hide

Hide | Top

References

« Hide 'large scale' references
[1]"Molecular characterization of the gene cluster coxMSL encoding the molybdenum-containing carbon monoxide dehydrogenase of Oligotropha carboxidovorans."
Schuebel U., Kraut M., Moersdorf G., Meyer O.
J. Bacteriol. 177:2197-2203(1995) [PubMed: 7721710] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Complete nucleotide sequence of the circular megaplasmid pHCG3 of Oligotropha carboxidovorans: function in the chemolithoautotrophic utilization of CO, H(2) and CO(2)."
Fuhrmann S., Ferner M., Jeffke T., Henne A., Gottschalk G., Meyer O.
Gene 322:67-75(2003) [PubMed: 14644498] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"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 1-13.
[4]"A novel binuclear [CuSMo] cluster at the active site of carbon monoxide dehydrogenase: characterization by X-ray absorption spectroscopy."
Gnida M., Ferner R., Gremer L., Meyer O., Meyer-Klaucke W.
Biochemistry 42:222-230(2003) [PubMed: 12515558] [Abstract]
Cited for: CHARACTERIZATION OF ACTIVE SITE.
[5]"Crystal structure and mechanism of CO dehydrogenase, a molybdo iron-sulfur flavoprotein containing S-selanylcysteine."
Dobbek H., Gremer L., Meyer O., Huber R.
Proc. Natl. Acad. Sci. U.S.A. 96:8884-8889(1999) [PubMed: 10430865] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
[6]"Catalysis at a dinuclear CuSMo(==O)OH cluster in a CO dehydrogenase resolved at 1.1-A resolution."
Dobbek H., Gremer L., Kiefersauer R., Huber R., Meyer O.
Proc. Natl. Acad. Sci. U.S.A. 99:15971-15976(2002) [PubMed: 12475995] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.09 ANGSTROMS).
+Additional computationally mapped references.

Hide | Top

Cross-references

Sequence databases

X82447 Genomic DNA. Translation: CAA57829.1.
PIRC56279.
RefSeqYP_015605.1.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1N5WX-ray1.50B/E1-809[»]
1N60X-ray1.19B/E1-809[»]
1N61X-ray1.30B/E1-809[»]
1N62X-ray1.09B/E1-809[»]
1N63X-ray1.21B/E1-809[»]
1ZXIX-ray1.70B/E1-809[»]
ModBaseSearch...

Genome annotation databases

GeneID2807115.
GenomeReviewsGene locus OCAR_p_08034 in contig X82447_GR.

Organism-specific databases

CMRSearch...

Enzyme and pathway databases

BRENDA1.2.99.2. 255922.

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...

Hide | Top

Entry information

Entry nameDCML_OLICO
AccessionPrimary (citable) accession number: P19919
Secondary accession number(s): Q51325
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: July 11, 2002
Last modified: June 16, 2009
This is version 69 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)

Hide | Top

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