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

Q04LJ3 (PYRF_STRP2) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 51. 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:SPD_0608
OrganismStreptococcus pneumoniae serotype 2 (strain D39 / NCTC 7466) [Complete proteome] [HAMAP]
Taxonomic identifier373153 [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_1000065945

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
Q04LJ3 [UniParc].

Last modified November 14, 2006. Version 1.
Checksum: 29AAED8BCBF7B4C9

FASTA23325,437
        10         20         30         40         50         60 
MREHRPIIAL DFPSFEAVKE FLALFPAEES LYLKVGMELY YAAGPEIVSY LKGLGHSVFL 

        70         80         90        100        110        120 
DLKLHDIPNT VKSAMKILSQ LGVDMTNVHA AGGVEMMKAA REGLGSQAKL IAVTQLTSTS 

       130        140        150        160        170        180 
EAQMQEFQNI QTSLQESVIH YAKKTAEAGL DGVVCSAQEV QVIKQATNPD FICLTPGIRP 

       190        200        210        220        230 
AGVAVGDQKR VMTPADAYQI GSDYIVVGRP ITQAEEPVAA YHAIKDEWTQ DWN 

« Hide

References

[1]"Genome sequence of Avery's virulent serotype 2 strain D39 of Streptococcus pneumoniae and comparison with that of unencapsulated laboratory strain R6."
Lanie J.A., Ng W.-L., Kazmierczak K.M., Andrzejewski T.M., Davidsen T.M., Wayne K.J., Tettelin H., Glass J.I., Winkler M.E.
J. Bacteriol. 189:38-51(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: D39 / NCTC 7466.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000410 Genomic DNA. Translation: ABJ54645.1.
RefSeqYP_816105.1. NC_008533.1.

3D structure databases

ProteinModelPortalQ04LJ3.
SMRQ04LJ3. Positions 1-229.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING373153.SPD_0608.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABJ54645; ABJ54645; SPD_0608.
GeneID4442951.
KEGGspd:SPD_0608.
PATRIC19682298. VBIStrPne27904_0689.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0284.
HOGENOMHOG000226071.
KOK01591.
OMARPITQSA.
OrthoDBEOG6N6815.

Enzyme and pathway databases

BioCycSPNE373153:GIX6-608-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_STRP2
AccessionPrimary (citable) accession number: Q04LJ3
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: November 14, 2006
Last modified: May 14, 2014
This is version 51 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