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B4SRN9 (PYRF_STRM5) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 39. 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:Smal_0054
OrganismStenotrophomonas maltophilia (strain R551-3) [Complete proteome] [HAMAP]
Taxonomic identifier391008 [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_1000138560

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
B4SRN9 [UniParc].

Last modified September 23, 2008. Version 1.
Checksum: E7E94319016C0430

FASTA24125,630
        10         20         30         40         50         60 
MSRAPLPLRD DERLIFALDV PDRVQALDWV ERLGDSVAFY 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 IVIGRPIRLA ADPQAAARAI QQEIASALAA 


R 

« Hide

References

[1]"Complete sequence of Stenotrophomonas maltophilia R551-3."
US DOE Joint Genome Institute
Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Lang D., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N. expand/collapse author list , Taghavi S., Monchy S., Newman L., Vangronsveld J., van der Lelie D., Richardson P.
Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: R551-3.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001111 Genomic DNA. Translation: ACF49759.1.
RefSeqYP_002026442.1. NC_011071.1.

3D structure databases

ProteinModelPortalB4SRN9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING391008.Smal_0054.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACF49759; ACF49759; Smal_0054.
GeneID6477603.
KEGGsmt:Smal_0054.
PATRIC23704900. VBISteMal40512_0054.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0284.
HOGENOMHOG000226070.
KOK01591.
OMAHAKEPRE.
OrthoDBEOG6N6815.

Enzyme and pathway databases

BioCycSMAL391008:GH1H-54-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_STRM5
AccessionPrimary (citable) accession number: B4SRN9
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: September 23, 2008
Last modified: May 14, 2014
This is version 39 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