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B2IN86 (PYRF_STRPS) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 42. 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:SPCG_0653
OrganismStreptococcus pneumoniae (strain CGSP14) [Complete proteome] [HAMAP]
Taxonomic identifier516950 [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_1000138564

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
B2IN86 [UniParc].

Last modified June 10, 2008. 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 evolution driven by host adaptations results in a more virulent and antimicrobial-resistant Streptococcus pneumoniae serotype 14."
Ding F., Tang P., Hsu M.-H., Cui P., Hu S., Yu J., Chiu C.-H.
BMC Genomics 10:158-158(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CGSP14.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001033 Genomic DNA. Translation: ACB89905.1.
RefSeqYP_001835370.1. NC_010582.1.

3D structure databases

ProteinModelPortalB2IN86.
SMRB2IN86. Positions 1-229.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING516950.SPCG_0653.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACB89905; ACB89905; SPCG_0653.
GeneID6217327.
KEGGspw:SPCG_0653.
PATRIC19677500. VBIStrPne123335_0710.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0284.
HOGENOMHOG000226071.
KOK01591.
OMARPITQSA.
OrthoDBEOG6N6815.

Enzyme and pathway databases

BioCycSPNE516950:GI38-659-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_STRPS
AccessionPrimary (citable) accession number: B2IN86
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: June 10, 2008
Last modified: May 14, 2014
This is version 42 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