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A4VV36 (PYRF_STRSY) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 43. 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:SSU05_1009
OrganismStreptococcus suis (strain 05ZYH33) [Complete proteome] [HAMAP]
Taxonomic identifier391295 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacilli › Lactobacillales › Streptococcaceae › Streptococcus ›

Protein attributes

Sequence length231 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 – 231231Orotidine 5'-phosphate decarboxylase HAMAP-Rule MF_01200
PRO_1000065953

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
A4VV36 [UniParc].

Last modified May 29, 2007. Version 1.
Checksum: 9C56B18F85C60C17

FASTA23125,339
        10         20         30         40         50         60 
MKETRPIIAL DFAGKEEVQS FLEQFPPDEK LYVKVGMELY YAEGPGIINY LKDCGHSIFL 

        70         80         90        100        110        120 
DLKLHDIPNT VESAMKVLAK LGVDMTNVHA AGGVEMMRAA RRGLGKDAVL IAVTQLTSTS 

       130        140        150        160        170        180 
EEQMRTDQNI QTSLQEAVVH YAQRAQEAGL DGVVCSAHEV ALIKDATSSD FVCLTPGIRP 

       190        200        210        220        230 
TGGEVGDQKR VMTPADAARI GSDYIVVGRP ITKSEHPYQT YLSIKEEWNR G

« Hide

References

[1]"A glimpse of streptococcal toxic shock syndrome from comparative genomics of S. suis 2 Chinese isolates."
Chen C., Tang J., Dong W., Wang C., Feng Y., Wang J., Zheng F., Pan X., Liu D., Li M., Song Y., Zhu X., Sun H., Feng T., Guo Z., Ju A., Ge J., Dong Y. expand/collapse author list , Sun W., Jiang Y., Wang J., Yan J., Yang H., Wang X., Gao G.F., Yang R., Wang J., Yu J.
PLoS ONE 2:E315-E315(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 05ZYH33.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000407 Genomic DNA. Translation: ABP89975.1.
RefSeqYP_001198375.1. NC_009442.1.

3D structure databases

ProteinModelPortalA4VV36.
SMRA4VV36. Positions 1-230.
ModBaseSearch...

Protein-protein interaction databases

STRING391295.SSU05_1009.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABP89975; ABP89975; SSU05_1009.
GeneID5100867.
KEGGssu:SSU05_1009.
PATRIC19773787. VBIStrSui128929_0991.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0284.
HOGENOMHOG000226071.
KOK01591.
OMANFKIFLD.
ProtClustDBPRK00230.

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. RibP_bind_barrel. 1 hit.
TIGRFAMsTIGR01740. pyrF. 1 hit.
PROSITEPS00156. OMPDECASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePYRF_STRSY
AccessionPrimary (citable) accession number: A4VV36
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: May 29, 2007
Last modified: May 1, 2013
This is version 43 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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