Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q30XT2 (PYRF_DESAG) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 62. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Orotidine 5'-phosphate decarboxylase

EC=4.1.1.23
Alternative name(s):
OMP decarboxylase
Short name=OMPDCase
Short name=OMPdecase
Gene names
Name:pyrF
Ordered Locus Names:Dde_2718
OrganismDesulfovibrio alaskensis (strain G20) (Desulfovibrio desulfuricans (strain G20)) [Complete proteome] [HAMAP]
Taxonomic identifier207559 [NCBI]
Taxonomic lineageBacteriaProteobacteriaDeltaproteobacteriaDesulfovibrionalesDesulfovibrionaceaeDesulfovibrio

Protein attributes

Sequence length236 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the decarboxylation of orotidine 5'-monophosphate (OMP) to uridine 5'-monophosphate (UMP) By similarity. HAMAP-Rule MF_01200

Catalytic activity

Orotidine 5'-phosphate = UMP + CO2. HAMAP-Rule MF_01200

Pathway

Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 2/2. HAMAP-Rule MF_01200

Subunit structure

Homodimer By similarity. HAMAP-Rule MF_01200

Sequence similarities

Belongs to the OMP decarboxylase family. Type 1 subfamily.

Ontologies

Keywords
   Biological processPyrimidine biosynthesis
   Molecular functionDecarboxylase
Lyase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_process'de novo' UMP biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

'de novo' pyrimidine nucleobase biosynthetic process

Inferred from electronic annotation. Source: InterPro

   Molecular_functionorotidine-5'-phosphate decarboxylase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 236236Orotidine 5'-phosphate decarboxylase HAMAP-Rule MF_01200
PRO_0000241854

Regions

Region60 – 6910Substrate binding By similarity

Sites

Active site621Proton donor By similarity
Binding site111Substrate By similarity
Binding site331Substrate By similarity
Binding site1251Substrate By similarity
Binding site1851Substrate By similarity
Binding site1931Substrate By similarity
Binding site2131Substrate; via amide nitrogen By similarity
Binding site2141Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q30XT2 [UniParc].

Last modified December 6, 2005. Version 1.
Checksum: 81FA871E8D83AB03

FASTA23624,861
        10         20         30         40         50         60 
MMMPELVVAL DYPESEQAVA MAARLQGSCP WVKVGLELYT AAGPDILRRL KDMGFSVFLD 

        70         80         90        100        110        120 
LKFFDIPNTV RGAVRSSVCA GADMVNIHLL GGARMAQAAV QGLQEGCECK GLAAPPVLLG 

       130        140        150        160        170        180 
VTVLTSMAQQ DLPAGLDLPL DSVVDVLARS GREWGLNGVV CSGYEVESIK KSCGTDYICL 

       190        200        210        220        230 
TPGIRPAAAD DDQRRTMTPQ QAARAGSDYL VVGRPVTGAA DPAGAAYSIM ESVRQA 

« Hide

References

[1]"Complete genome sequence and updated annotation of Desulfovibrio alaskensis G20."
Hauser L.J., Land M.L., Brown S.D., Larimer F., Keller K.L., Rapp-Giles B.J., Price M.N., Lin M., Bruce D.C., Detter J.C., Tapia R., Han C.S., Goodwin L.A., Cheng J.F., Pitluck S., Copeland A., Lucas S., Nolan M. expand/collapse author list , Lapidus A.L., Palumbo A.V., Wall J.D.
J. Bacteriol. 193:4268-4269(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: G20.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000112 Genomic DNA. Translation: ABB39514.1.
RefSeqYP_389209.1. NC_007519.1.

3D structure databases

ProteinModelPortalQ30XT2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING207559.Dde_2718.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABB39514; ABB39514; Dde_2718.
GeneID3757741.
KEGGdde:Dde_2718.
PATRIC21744379. VBIDesDes50040_2685.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0284.
HOGENOMHOG000226070.
KOK01591.
OMAHAKEPRE.
OrthoDBEOG6N6815.

Enzyme and pathway databases

BioCycDALA207559:GH1L-2433-MONOMER.
UniPathwayUPA00070; UER00120.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
HAMAPMF_01200_B. OMPdecase_type1_B.
InterProIPR013785. Aldolase_TIM.
IPR014732. OMPdecase.
IPR018089. OMPdecase_AS.
IPR001754. OMPdeCOase_dom.
IPR011060. RibuloseP-bd_barrel.
[Graphical view]
PfamPF00215. OMPdecase. 1 hit.
[Graphical view]
SMARTSM00934. OMPdecase. 1 hit.
[Graphical view]
SUPFAMSSF51366. SSF51366. 1 hit.
TIGRFAMsTIGR01740. pyrF. 1 hit.
PROSITEPS00156. OMPDECASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePYRF_DESAG
AccessionPrimary (citable) accession number: Q30XT2
Entry history
Integrated into UniProtKB/Swiss-Prot: June 27, 2006
Last sequence update: December 6, 2005
Last modified: July 9, 2014
This is version 62 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways