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B8DDS0 (PYRF_LISMH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 34. 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:LMHCC_0724
OrganismListeria monocytogenes serotype 4a (strain HCC23) [Complete proteome] [HAMAP]
Taxonomic identifier552536 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesListeriaceaeListeria

Protein attributes

Sequence length233 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 – 233233Orotidine 5'-phosphate decarboxylase HAMAP-Rule MF_01200
PRO_1000164574

Regions

Region58 – 6710Substrate binding By similarity

Sites

Active site601Proton donor By similarity
Binding site91Substrate By similarity
Binding site311Substrate By similarity
Binding site1201Substrate 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
B8DDS0 [UniParc].

Last modified March 3, 2009. Version 1.
Checksum: 1E8D076A62016669

FASTA23325,135
        10         20         30         40         50         60 
MNKPIIALDF QTYEEVEQFL AKFSGEALSV KVGMELFYSN GPIIVEKIKQ QNHEIFLDLK 

        70         80         90        100        110        120 
LHDIPNTVKS AMVGLAKLGV DMVNVHAAGG KNMMEAALEG LEIGSGSGKR PKIIAVTQLT 

       130        140        150        160        170        180 
STSEASMQSE QLIKTSLLES VLHYSALTNQ AGLNGVVCSA LEAEAIKQQN GADFLRVTPG 

       190        200        210        220        230 
IRLASDAADD QIRVVTPEKA RLIGSTDIVV GRSITRANDP VAAYNQVLKE WNV 

« Hide

References

[1]"Genome sequence of lineage III Listeria monocytogenes strain HCC23."
Steele C.L., Donaldson J.R., Paul D., Banes M.M., Arick T., Bridges S.M., Lawrence M.L.
J. Bacteriol. 193:3679-3680(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: HCC23.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001175 Genomic DNA. Translation: ACK39079.1.
RefSeqYP_002349693.1. NC_011660.1.

3D structure databases

ProteinModelPortalB8DDS0.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING552536.LMHCC_0724.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACK39079; ACK39079; LMHCC_0724.
GeneID7078530.
KEGGlmh:LMHCC_0724.
PATRIC20316521. VBILisMon86872_0719.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0284.
HOGENOMHOG000226071.
KOK01591.
OMAGANGDTN.
OrthoDBEOG6N6815.

Enzyme and pathway databases

BioCycLMON552536:GIW4-739-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_LISMH
AccessionPrimary (citable) accession number: B8DDS0
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: March 3, 2009
Last modified: May 14, 2014
This is version 34 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