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Q4ZVD9 (PYRF_PSEU2) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 61. 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:Psyr_1836
OrganismPseudomonas syringae pv. syringae (strain B728a) [Complete proteome] [HAMAP]
Taxonomic identifier205918 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonasPseudomonas syringae

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 AAY36883.1 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_0000241892

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
Q4ZVD9 [UniParc].

Last modified June 27, 2006. Version 2.
Checksum: 7B7881BEB6620BC7

FASTA23224,627
        10         20         30         40         50         60 
MSACQTPVIV ALDFPTREAA LRLADQLDPK LCRVKVGKEL FTSCAADIVE TLRHRGFEVF 

        70         80         90        100        110        120 
LDLKFHDIPN TTAMAVKAAA EMGVWMVNVH CSGGLRMMAA CREVLEQRTG PQPLLIGVTV 

       130        140        150        160        170        180 
LTSMEREDLA GIGLDIDPQV QVLRLAALAG KAGMDGLVCS ALEAQALKAA HPSLQLVTPG 

       190        200        210        220        230 
IRPAGSAQDD QRRILTPRQA LDAGSDYLVI GRPISQAADP AKALAAVVAE LA 

« Hide

References

[1]"Comparison of the complete genome sequences of Pseudomonas syringae pv. syringae B728a and pv. tomato DC3000."
Feil H., Feil W.S., Chain P., Larimer F., Dibartolo G., Copeland A., Lykidis A., Trong S., Nolan M., Goltsman E., Thiel J., Malfatti S., Loper J.E., Lapidus A., Detter J.C., Land M., Richardson P.M., Kyrpides N.C., Ivanova N., Lindow S.E.
Proc. Natl. Acad. Sci. U.S.A. 102:11064-11069(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: B728a.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000075 Genomic DNA. Translation: AAY36883.1. Different initiation.
RefSeqYP_234921.1. NC_007005.1.

3D structure databases

ProteinModelPortalQ4ZVD9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING205918.Psyr_1836.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAY36883; AAY36883; Psyr_1836.
GeneID3367345.
KEGGpsb:Psyr_1836.
PATRIC19984211. VBIPseSyr42314_1880.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0284.
HOGENOMHOG000226071.
KOK01591.
OrthoDBEOG6N6815.

Enzyme and pathway databases

BioCycPSYR205918:GJ94-1870-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_PSEU2
AccessionPrimary (citable) accession number: Q4ZVD9
Entry history
Integrated into UniProtKB/Swiss-Prot: June 27, 2006
Last sequence update: June 27, 2006
Last modified: May 14, 2014
This is version 61 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