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Q5WWS3 (PYRF_LEGPL) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 65. 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:lpl1376
OrganismLegionella pneumophila (strain Lens) [Complete proteome] [HAMAP]
Taxonomic identifier297245 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaLegionellalesLegionellaceaeLegionella

Protein attributes

Sequence length229 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 – 229229Orotidine 5'-phosphate decarboxylase HAMAP-Rule MF_01200
PRO_0000241871

Regions

Region59 – 6810Substrate binding By similarity

Sites

Active site611Proton donor By similarity
Binding site101Substrate By similarity
Binding site321Substrate By similarity
Binding site1191Substrate By similarity
Binding site1801Substrate By similarity
Binding site1891Substrate By similarity
Binding site2091Substrate; via amide nitrogen By similarity
Binding site2101Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5WWS3 [UniParc].

Last modified November 23, 2004. Version 1.
Checksum: 9B892022EB52B528

FASTA22925,230
        10         20         30         40         50         60 
MTPKLIVALD FDNQDNALQL VEKLDPNHCA LKVGSELFTL LGPQFVKELV RREFKVFLDL 

        70         80         90        100        110        120 
KFHDIPNTVA KACYSAAELG VWMINVHAIG GLKMLQAARE SLKTYGKDRP LLIAVTVLTS 

       130        140        150        160        170        180 
FEEGELASVG IRNTLPEQAT HLAMLAREAG LDGVVSSAHE VKIIKQKCGE NFITVTPGIR 

       190        200        210        220 
LPNNLKDDQS RVMTPQQAIR EGSDFLVIGR PITQASNPYE VVSALLRDL 

« Hide

References

[1]"Evidence in the Legionella pneumophila genome for exploitation of host cell functions and high genome plasticity."
Cazalet C., Rusniok C., Brueggemann H., Zidane N., Magnier A., Ma L., Tichit M., Jarraud S., Bouchier C., Vandenesch F., Kunst F., Etienne J., Glaser P., Buchrieser C.
Nat. Genet. 36:1165-1173(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Lens.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CR628337 Genomic DNA. Translation: CAH15616.1.
RefSeqYP_126726.1. NC_006369.1.

3D structure databases

ProteinModelPortalQ5WWS3.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING297245.lpl1376.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAH15616; CAH15616; lpl1376.
GeneID3114147.
KEGGlpf:lpl1376.
PATRIC22316411. VBILegPne33733_1534.

Organism-specific databases

LegioListlpl1376.
CMRSearch...

Phylogenomic databases

eggNOGCOG0284.
HOGENOMHOG000226071.
KOK01591.
OMARPITQSA.
OrthoDBEOG6N6815.

Enzyme and pathway databases

BioCycLPNE297245:GJD4-1484-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_LEGPL
AccessionPrimary (citable) accession number: Q5WWS3
Entry history
Integrated into UniProtKB/Swiss-Prot: June 27, 2006
Last sequence update: November 23, 2004
Last modified: May 14, 2014
This is version 65 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