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C0M7X0 (PYRF_STRE4) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 31. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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:SEQ_1350
OrganismStreptococcus equi subsp. equi (strain 4047) [Complete proteome] [HAMAP]
Taxonomic identifier553482 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacilli › Lactobacillales › Streptococcaceae › Streptococcus ›

Protein attributes

Sequence length230 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.

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: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 230230Orotidine 5'-phosphate decarboxylase HAMAP-Rule MF_01200
PRO_1000164579

Regions

Region61 – 7010Substrate binding By similarity

Sites

Active site631Proton donor By similarity
Binding site111Substrate By similarity
Binding site341Substrate By similarity
Binding site1171Substrate By similarity
Binding site1791Substrate By similarity
Binding site1881Substrate By similarity
Binding site2081Substrate; via amide nitrogen By similarity
Binding site2091Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
C0M7X0 [UniParc].

Last modified May 5, 2009. Version 1.
Checksum: 103BF7BA64203C78

FASTA23025,318
        10         20         30         40         50         60 
MREERPIIAL DFPSFEEVKS FLSLFPADER LYVKIGMELY YAEGPDIVRY VKSLGHSVFL 

        70         80         90        100        110        120 
DLKLHDIPNT VKSTMAVLSR LGIDMTTVQA AGGVEMLRAA REGLGQGPIL IAVTQLTSTS 

       130        140        150        160        170        180 
EEQMREDQNI QSTLLASVLH YAKRTAQAKL DGVVCSAHEV KAIKSEVPAG FVCLTPGIRP 

       190        200        210        220        230 
TGADIGDQKR VMTPHQARAI GSDYIVLGRP ITQATDPVKA YHQIKAEWNR

« Hide

References

[1]"Genomic evidence for the evolution of Streptococcus equi: host restriction, increased virulence, and genetic exchange with human pathogens."
Holden M.T.G., Heather Z., Paillot R., Steward K.F., Webb K., Ainslie F., Jourdan T., Bason N.C., Holroyd N.E., Mungall K., Quail M.A., Sanders M., Simmonds M., Willey D., Brooks K., Aanensen D.M., Spratt B.G., Jolley K.A. expand/collapse author list , Maiden M.C.J., Kehoe M., Chanter N., Bentley S.D., Robinson C., Maskell D.J., Parkhill J., Waller A.S.
PLoS Pathog. 5:E1000346-E1000346(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 4047.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		FM204883 Genomic DNA. Translation: CAW94161.1.
RefSeqYP_002746628.1. NC_012471.1.

3D structure databases

ProteinModelPortalC0M7X0.
ModBaseSearch...

Protein-protein interaction databases

STRING553482.SEQ_1350.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAW94161; CAW94161; SEQ_1350.
GeneID7696617.
KEGGseu:SEQ_1350.
PATRIC19647502. VBIStrEqu13040_1367.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0284.
HOGENOMHOG000226071.
KOK01591.
OMANFKIFLD.
ProtClustDBPRK00230.

Enzyme and pathway databases

BioCycSEQU553482:GJOY-1338-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. RibP_bind_barrel. 1 hit.
TIGRFAMsTIGR01740. pyrF. 1 hit.
PROSITEPS00156. OMPDECASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePYRF_STRE4
AccessionPrimary (citable) accession number: C0M7X0
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: May 5, 2009
Last modified: May 1, 2013
This is version 31 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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