Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q8E5F0 (PYRF_STRA3) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 70. 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:gbs1082
OrganismStreptococcus agalactiae serotype III (strain NEM316) [Complete proteome] [HAMAP]
Taxonomic identifier211110 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus

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_0000134584

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 site1891Substrate By similarity
Binding site2091Substrate; via amide nitrogen By similarity
Binding site2101Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8E5F0 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: 41073AEE79C8722B

FASTA23326,034
        10         20         30         40         50         60 
MLEKCPIIAL DFSDLASVTT FLEHFPKEEL LFVKIGMELY YSEGPSIIRY IKSLGHRIFL 

        70         80         90        100        110        120 
DLKLHDIPNT VRSSMSVLAK LGIDMTNVHA AGGVEMMKAA REGLGEGPIL LAVTQLTSTS 

       130        140        150        160        170        180 
QEQMQVDQHI NLSVVDSVCH YAQKAQEAGL DGVVASAQEV KQIKKQTNEH FICLTPGIRP 

       190        200        210        220        230 
PQTNQLDDQK RTMTPEQARI VGADYIVVGR PITKAENPYQ AYLEIKEEWN RIK 

« Hide

References

[1]"Genome sequence of Streptococcus agalactiae, a pathogen causing invasive neonatal disease."
Glaser P., Rusniok C., Buchrieser C., Chevalier F., Frangeul L., Msadek T., Zouine M., Couve E., Lalioui L., Poyart C., Trieu-Cuot P., Kunst F.
Mol. Microbiol. 45:1499-1513(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: NEM316.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL766848 Genomic DNA. Translation: CAD46741.1.
RefSeqNP_735528.1. NC_004368.1.

3D structure databases

ProteinModelPortalQ8E5F0.
SMRQ8E5F0. Positions 1-232.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING211110.gbs1082.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAD46741; CAD46741; CAD46741.
GeneID1030080.
KEGGsan:gbs1082.
PATRIC19638040. VBIStrAga3577_1112.

Organism-specific databases

GenoListgbs1082.
CMRSearch...

Phylogenomic databases

eggNOGCOG0284.
HOGENOMHOG000226071.
KOK01591.
OMARPITQSA.
OrthoDBEOG6N6815.

Enzyme and pathway databases

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_STRA3
AccessionPrimary (citable) accession number: Q8E5F0
Entry history
Integrated into UniProtKB/Swiss-Prot: May 23, 2003
Last sequence update: March 1, 2003
Last modified: May 14, 2014
This is version 70 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