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P0DC81 (PYRF_STRPQ) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 21. 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:SPs1237
OrganismStreptococcus pyogenes serotype M3 (strain SSI-1) [Complete proteome] [HAMAP]
Taxonomic identifier193567 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus

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. 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 – 230230Orotidine 5'-phosphate decarboxylase HAMAP-Rule MF_01200
PRO_0000411428

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
P0DC81 [UniParc].

Last modified July 27, 2011. Version 1.
Checksum: 926DC74C4E2F46C6

FASTA23024,928
        10         20         30         40         50         60 
MKEERPIIAL DFSSFEETKA FLDLFPAEEK LYVKIGMELY YAQGPDIVRS IKSLGHNVFL 

        70         80         90        100        110        120 
DLKLHDIPNT VRAAMAVLKE LDIDMATVHA AGGVEMLKAA REGLGQGPTL IAVTQLTSTS 

       130        140        150        160        170        180 
EDQMRGDQNI QTSLLESVLH YSKGAAKAQL DGVVCSAQEV EAIKAVTPTG FTCLTPGIRP 

       190        200        210        220        230 
KGSNIGDQKR VMTPNQARRI GSDYIVVGRP ITQAKDPVAA YQAIKAEWAG 

« Hide

References

[1]"Genome sequence of an M3 strain of Streptococcus pyogenes reveals a large-scale genomic rearrangement in invasive strains and new insights into phage evolution."
Nakagawa I., Kurokawa K., Yamashita A., Nakata M., Tomiyasu Y., Okahashi N., Kawabata S., Yamazaki K., Shiba T., Yasunaga T., Hayashi H., Hattori M., Hamada S.
Genome Res. 13:1042-1055(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: SSI-1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000034 Genomic DNA. Translation: BAC64332.1.
RefSeqNP_802499.1. NC_004606.1.

3D structure databases

ProteinModelPortalP0DC81.
SMRP0DC81. Positions 1-230.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAC64332; BAC64332; BAC64332.
GeneID1066661.
KEGGsps:SPs1237.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000226071.
KOK01591.
OMAGANGDTN.
OrthoDBEOG6N6815.

Enzyme and pathway databases

BioCycSPYO193567:GHDO-1296-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_STRPQ
AccessionPrimary (citable) accession number: P0DC81
Secondary accession number(s): Q8K7V3
Entry history
Integrated into UniProtKB/Swiss-Prot: July 27, 2011
Last sequence update: July 27, 2011
Last modified: May 14, 2014
This is version 21 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