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Q48KP5 (PYRF_PSE14) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 60. 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:PSPPH_1796
OrganismPseudomonas syringae pv. phaseolicola (strain 1448A / Race 6) [Complete proteome] [HAMAP]
Taxonomic identifier264730 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

Protein attributes

Sequence length232 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.

Sequence caution

The sequence AAZ34149.1 differs from that shown. Reason: Erroneous initiation.

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 – 232232Orotidine 5'-phosphate decarboxylase HAMAP-Rule MF_01200
PRO_0000241891

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

Sequences

Sequence LengthMass (Da)Tools
Q48KP5 [UniParc].

Last modified June 27, 2006. Version 2.
Checksum: 21D2E450E43D07AE

FASTA23224,632
        10         20         30         40         50         60 
MSACQTPVIV ALDFPTREAA LRLADQLDPK LCRVKVGKEL FISCAADIVE TLRNKGFEVF 

        70         80         90        100        110        120 
LDLKFHDIPN TTAMAVKAAA EMGVWMVNVH CSGGLRMMTA CREVLEQRSG PQPLLIGVTV 

       130        140        150        160        170        180 
LTSMEREDLA GIGLDIDPQV QVLRLAALAE KAGLDGLVCS ALEAQALKAA HPSLQLVTPG 

       190        200        210        220        230 
IRPAGSAQDD QRRILTPRQA LDAGSDHLVI GRPISQAADP AKALAAVVAE LA 

« Hide

References

[1]"Whole-genome sequence analysis of Pseudomonas syringae pv. phaseolicola 1448A reveals divergence among pathovars in genes involved in virulence and transposition."
Joardar V., Lindeberg M., Jackson R.W., Selengut J., Dodson R., Brinkac L.M., Daugherty S.C., DeBoy R.T., Durkin A.S., Gwinn Giglio M., Madupu R., Nelson W.C., Rosovitz M.J., Sullivan S.A., Crabtree J., Creasy T., Davidsen T.M., Haft D.H. expand/collapse author list , Zafar N., Zhou L., Halpin R., Holley T., Khouri H.M., Feldblyum T.V., White O., Fraser C.M., Chatterjee A.K., Cartinhour S., Schneider D., Mansfield J.W., Collmer A., Buell R.
J. Bacteriol. 187:6488-6498(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 1448A / Race 6.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000058 Genomic DNA. Translation: AAZ34149.1. Different initiation.
RefSeqYP_274030.1. NC_005773.3.

3D structure databases

ProteinModelPortalQ48KP5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING264730.PSPPH_1796.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAZ34149; AAZ34149; PSPPH_1796.
GeneID3556691.
KEGGpsp:PSPPH_1796.
PATRIC19972779. VBIPseSyr78478_1885.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0284.
HOGENOMHOG000226071.
KOK01591.
OrthoDBEOG6N6815.

Enzyme and pathway databases

BioCycPSAV264730:GKDE-1799-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_PSE14
AccessionPrimary (citable) accession number: Q48KP5
Entry history
Integrated into UniProtKB/Swiss-Prot: June 27, 2006
Last sequence update: June 27, 2006
Last modified: May 14, 2014
This is version 60 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