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B4EW04 (PYRF_PROMH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 38. 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:PMI1313
OrganismProteus mirabilis (strain HI4320) [Complete proteome] [HAMAP]
Taxonomic identifier529507 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeProteus

Protein attributes

Sequence length248 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 – 248248Orotidine 5'-phosphate decarboxylase HAMAP-Rule MF_01200
PRO_1000138547

Regions

Region71 – 8010Substrate binding By similarity

Sites

Active site731Proton donor By similarity
Binding site221Substrate By similarity
Binding site441Substrate By similarity
Binding site1311Substrate By similarity
Binding site1921Substrate By similarity
Binding site2011Substrate By similarity
Binding site2211Substrate; via amide nitrogen By similarity
Binding site2221Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
B4EW04 [UniParc].

Last modified September 23, 2008. Version 1.
Checksum: 07F162D9A7BF5531

FASTA24826,869
        10         20         30         40         50         60 
MSFDCDKKSP SSTCAPVIVA LDYEDQKSAL DFAQLIDPSS CRLKIGKEMF TRFGPQFVTQ 

        70         80         90        100        110        120 
LQQQGFDIFL DLKFHDIPNT VARAVAAAAD LGVWMVNVHA SGGSRMMRAA KESLRSFGKE 

       130        140        150        160        170        180 
APLLTAVTVL TSMDQSDLTE LGINLTPAEQ AERLALLAKA CGLDGVVCSA HEATRFKQVC 

       190        200        210        220        230        240 
GDDFLLVTPG IRPAGSEVGD QRRVMTPEQA IVAGVDYMVI GRPITRSENP LETLQQINRS 


IQGVVQHG 

« Hide

References

[1]"Complete genome sequence of uropathogenic Proteus mirabilis, a master of both adherence and motility."
Pearson M.M., Sebaihia M., Churcher C., Quail M.A., Seshasayee A.S., Luscombe N.M., Abdellah Z., Arrosmith C., Atkin B., Chillingworth T., Hauser H., Jagels K., Moule S., Mungall K., Norbertczak H., Rabbinowitsch E., Walker D., Whithead S. expand/collapse author list , Thomson N.R., Rather P.N., Parkhill J., Mobley H.L.T.
J. Bacteriol. 190:4027-4037(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: HI4320.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM942759 Genomic DNA. Translation: CAR42784.1.
RefSeqYP_002151044.1. NC_010554.1.

3D structure databases

ProteinModelPortalB4EW04.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING529507.PMI1313.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAR42784; CAR42784; PMI1313.
GeneID6801095.
KEGGpmr:PMI1313.
PATRIC20517249. VBIProMir120933_1262.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0284.
HOGENOMHOG000226071.
KOK01591.
OMARPITQSA.
OrthoDBEOG6N6815.

Enzyme and pathway databases

BioCycPMIR529507:GJIW-1321-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_PROMH
AccessionPrimary (citable) accession number: B4EW04
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: September 23, 2008
Last modified: May 14, 2014
This is version 38 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