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Q59654 (PYRF_PSEAE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 99. 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:PA2876
OrganismPseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) [Reference proteome] [HAMAP]
Taxonomic identifier208964 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

Protein attributes

Sequence length232 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the decarboxylation of orotidine 5'-monophosphate (OMP) to uridine 5'-monophosphate (UMP). 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.

Sequence similarities

Belongs to the OMP decarboxylase family. Type 1 subfamily.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 232232Orotidine 5'-phosphate decarboxylase HAMAP-Rule MF_01200
PRO_0000134565

Regions

Region62 – 7110Substrate binding By similarity

Sites

Active site641Proton donor By similarity
Binding site131Substrate By similarity
Binding site351Substrate By similarity
Binding site1221Substrate By similarity
Binding site1821Substrate By similarity
Binding site1911Substrate By similarity
Binding site2111Substrate; via amide nitrogen By similarity
Binding site2121Substrate By similarity

Experimental info

Sequence conflict1111P → A in CAA46564. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q59654 [UniParc].

Last modified December 8, 2000. Version 2.
Checksum: EE7218004DA944B5

FASTA23224,394
        10         20         30         40         50         60 
MSACQSPIIV ALDFPTREAA LALADQLDPK LCRVKVGKEL FTSCAAGIVE TLRGKGFEVF 

        70         80         90        100        110        120 
LDLKFHDIPN TTAMAVKAAA EMGVWMVNVH CSGGLRMMAA CRETLEAFSG PRPLLIGVTV 

       130        140        150        160        170        180 
LTSMEREDLA GIGLDIEPQE QVLRLAALAQ KAGMDGLVCS AQEAPALKAA HPGLQLVTPG 

       190        200        210        220        230 
IRPAGSAQDD QRRILTPRQA LDAGSDYLVI GRPISQAADP AKALAAIVAE LG 

« Hide

References

« Hide 'large scale' references
[1]"Orotidine-5'-monophosphate decarboxylase from Pseudomonas aeruginosa PAO1: cloning, overexpression, and enzyme characterization."
Strych U., Wohlfarth S., Winkler U.K.
Curr. Microbiol. 29:353-359(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION.
Strain: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228.
[2]"Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic pathogen."
Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P., Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M., Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y., Brody L.L., Coulter S.N., Folger K.R. expand/collapse author list , Kas A., Larbig K., Lim R.M., Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J., Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.
Nature 406:959-964(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X65613 Genomic DNA. Translation: CAA46564.1.
AE004091 Genomic DNA. Translation: AAG06264.1.
PIRB83285.
S43188.
RefSeqNP_251566.1. NC_002516.2.

3D structure databases

ProteinModelPortalQ59654.
SMRQ59654. Positions 8-231.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING208964.PA2876.

Protocols and materials databases

DNASU882585.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAG06264; AAG06264; PA2876.
GeneID882585.
KEGGpae:PA2876.
PATRIC19840295. VBIPseAer58763_3017.

Organism-specific databases

PseudoCAPPA2876.

Phylogenomic databases

eggNOGCOG0284.
HOGENOMHOG000226070.
KOK01591.
OMARPITQSA.
OrthoDBEOG6N6815.
PhylomeDBQ59654.

Enzyme and pathway databases

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_PSEAE
AccessionPrimary (citable) accession number: Q59654
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: December 8, 2000
Last modified: July 9, 2014
This is version 99 of the entry and version 2 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