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B2FU58 (PYRF_STRMK) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 41. 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:Smlt0099
OrganismStenotrophomonas maltophilia (strain K279a) [Complete proteome] [HAMAP]
Taxonomic identifier522373 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaXanthomonadalesXanthomonadaceaeStenotrophomonasStenotrophomonas maltophilia group

Protein attributes

Sequence length241 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 – 241241Orotidine 5'-phosphate decarboxylase HAMAP-Rule MF_01200
PRO_1000138561

Regions

Region69 – 7810Substrate binding By similarity

Sites

Active site711Proton donor By similarity
Binding site191Substrate By similarity
Binding site411Substrate By similarity
Binding site1241Substrate By similarity
Binding site1851Substrate By similarity
Binding site1941Substrate By similarity
Binding site2141Substrate; via amide nitrogen By similarity
Binding site2151Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
B2FU58 [UniParc].

Last modified June 10, 2008. Version 1.
Checksum: BC112A89E65788B9

FASTA24125,618
        10         20         30         40         50         60 
MSRAPLPLRD DERLIFALDV PDRAQALEWV DRLGDSVAFY KIGMELLASG EYFQVLDELA 

        70         80         90        100        110        120 
RRDKRVFVDL KFFDIPATAA AVIKRLSQWP VSYATIHGWH PAMMEACAAA NSSDMRLLAV 

       130        140        150        160        170        180 
TVLTSMGRPD LAQMGIDREP VDVVVERALA AQAAGIDGVI ASGQEAGPIR AATGAGFSIV 

       190        200        210        220        230        240 
CPGIRPGGPV GDDQKRTVGV AQAFADGADA IVVGRPIRLA TDPQAAARAI QQEIASALAA 


R 

« Hide

References

[1]"The complete genome, comparative and functional analysis of Stenotrophomonas maltophilia reveals an organism heavily shielded by drug resistance determinants."
Crossman L.C., Gould V.C., Dow J.M., Vernikos G.S., Okazaki A., Sebaihia M., Saunders D., Arrowsmith C., Carver T., Peters N., Adlem E., Kerhornou A., Lord A., Murphy L., Seeger K., Squares R., Rutter S., Quail M.A. expand/collapse author list , Rajandream M.A., Harris D., Churcher C., Bentley S.D., Parkhill J., Thomson N.R., Avison M.B.
Genome Biol. 9:R74.1-R74.13(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K279a.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM743169 Genomic DNA. Translation: CAQ43710.1.
RefSeqYP_001970025.1. NC_010943.1.

3D structure databases

ProteinModelPortalB2FU58.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING522373.Smlt0099.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAQ43710; CAQ43710; Smlt0099.
GeneID6392146.
KEGGsml:Smlt0099.
PATRIC23695935. VBISteMal45202_0087.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0284.
HOGENOMHOG000226070.
KOK01591.
OMARPITQSA.
OrthoDBEOG6N6815.

Enzyme and pathway databases

BioCycSMAL522373:GJE8-91-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_STRMK
AccessionPrimary (citable) accession number: B2FU58
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: June 10, 2008
Last modified: May 14, 2014
This is version 41 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