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P77888 (PYRF_LACPL) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 93. 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:lp_2698
OrganismLactobacillus plantarum (strain ATCC BAA-793 / NCIMB 8826 / WCFS1) [Reference proteome] [HAMAP]
Taxonomic identifier220668 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliLactobacillalesLactobacillaceaeLactobacillus

Protein attributes

Sequence length237 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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 237237Orotidine 5'-phosphate decarboxylase HAMAP-Rule MF_01200
PRO_0000134551

Regions

Region60 – 6910Substrate binding By similarity

Sites

Active site621Proton donor By similarity
Binding site101Substrate By similarity
Binding site331Substrate By similarity
Binding site1241Substrate By similarity
Binding site1861Substrate By similarity
Binding site1951Substrate By similarity
Binding site2151Substrate; via amide nitrogen By similarity
Binding site2161Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
P77888 [UniParc].

Last modified March 25, 2003. Version 2.
Checksum: FB3A5D24FD4D47E7

FASTA23724,949
        10         20         30         40         50         60 
MKRPIIIALD FPTAERALAF LDQFPADLHV TVKIGMELFY AAGPSIVTDV QARGHAVFLD 

        70         80         90        100        110        120 
LKLHDIPNTV ESAMRVIGRL GVTYTTVHAA GGHVMLSAAK RGLVAGAMAA GVTAPKLLAI 

       130        140        150        160        170        180 
TQLTSTNQAI LNQDQQIMGT VRASVVHYAK LARASDCDGV ICSAQEVQAI HTAVGADFLG 

       190        200        210        220        230 
ITPGIRPASA QSDDQQRVMT PAAAAKAGSN GLVIGRPITQ AAEPVQAYRD IMTEWSN 

« Hide

References

« Hide 'large scale' references
[1]"Structure and organisation of the pyrimidine biosynthesis pathway genes in Lactobacillus plantarum: a PCR strategy for sequencing without cloning."
Elagoez A., Abdi A., Hubert J.-C., Kammerer B.
Gene 182:37-43(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 8014 / CCM 1904 / DSM 20205 / NCDO 82 / NCIB 6376.
[2]Kammerer B., Elagoz A., Abdi A., Hubert J.-C., Bringel F.
Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION.
[3]"Complete genome sequence of Lactobacillus plantarum WCFS1."
Kleerebezem M., Boekhorst J., van Kranenburg R., Molenaar D., Kuipers O.P., Leer R., Tarchini R., Peters S.A., Sandbrink H.M., Fiers M.W.E.J., Stiekema W., Klein Lankhorst R.M., Bron P.A., Hoffer S.M., Nierop Groot M.N., Kerkhoven R., De Vries M., Ursing B., De Vos W.M., Siezen R.J.
Proc. Natl. Acad. Sci. U.S.A. 100:1990-1995(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-793 / NCIMB 8826 / WCFS1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z54240 Genomic DNA. Translation: CAA91007.2.
AL935263 Genomic DNA. Translation: CCC79819.1.
RefSeqYP_004890333.1. NC_004567.2.

3D structure databases

ProteinModelPortalP77888.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING220668.lp_2698.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCCC79819; CCC79819; lp_2698.
GeneID1062962.
KEGGlpl:lp_2698.
PATRIC22251301. VBILacPla27411_2258.

Phylogenomic databases

eggNOGCOG0284.
HOGENOMHOG000226071.
KOK01591.
OMASAYHAIK.

Enzyme and pathway databases

BioCycLPLA220668-WGS:GSPK-2310-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_LACPL
AccessionPrimary (citable) accession number: P77888
Secondary accession number(s): F9URI0
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: March 25, 2003
Last modified: July 9, 2014
This is version 93 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