Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q5WFJ5 (PYRF_BACSK) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 66. 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:ABC2330
OrganismBacillus clausii (strain KSM-K16) [Complete proteome] [HAMAP]
Taxonomic identifier66692 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Protein attributes

Sequence length239 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 – 239239Orotidine 5'-phosphate decarboxylase HAMAP-Rule MF_01200
PRO_0000241846

Regions

Region59 – 6810Substrate binding By similarity

Sites

Active site611Proton donor By similarity
Binding site101Substrate By similarity
Binding site321Substrate By similarity
Binding site1221Substrate By similarity
Binding site1841Substrate By similarity
Binding site1931Substrate By similarity
Binding site2131Substrate; via amide nitrogen By similarity
Binding site2141Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5WFJ5 [UniParc].

Last modified November 23, 2004. Version 1.
Checksum: CD0341040D33F2FC

FASTA23926,288
        10         20         30         40         50         60 
MNRPFFIALD FDEHAKRQRF LESFAAETLD VKIGMELFYR EGLSVVHELK EAGYRLFLDL 

        70         80         90        100        110        120 
KLHDIPNTVG RTMRALAELD VDVVNVHAAG GKAMMEAALE GLDAGTRAGK QRPKLIAVTQ 

       130        140        150        160        170        180 
LTSTDSRMLA EELLIDKAMD EVVVRYAQLA QESGLDGVVC SAHEVPLIRA ACSDRFLTVT 

       190        200        210        220        230 
PGIRRQVDQV GDQVRVVTPG EAKALGSWAI VVGRSITAAA DPLAVYREMN QDWKGATEH 

« Hide

References

[1]"The complete genome sequence of the alkaliphilic Bacillus clausii KSM-K16."
Takaki Y., Kageyama Y., Shimamura S., Suzuki H., Nishi S., Hatada Y., Kawai S., Ito S., Horikoshi K.
Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: KSM-K16.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP006627 Genomic DNA. Translation: BAD64865.1.
RefSeqYP_175826.1. NC_006582.1.

3D structure databases

ProteinModelPortalQ5WFJ5.
SMRQ5WFJ5. Positions 1-235.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING66692.ABC2330.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAD64865; BAD64865; ABC2330.
GeneID3202829.
KEGGbcl:ABC2330.
PATRIC18924248. VBIBacCla58185_2487.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0284.
HOGENOMHOG000226071.
KOK01591.
OMARPITQSA.
OrthoDBEOG6N6815.

Enzyme and pathway databases

BioCycBCLA66692:GHMP-2398-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_BACSK
AccessionPrimary (citable) accession number: Q5WFJ5
Entry history
Integrated into UniProtKB/Swiss-Prot: June 27, 2006
Last sequence update: November 23, 2004
Last modified: May 14, 2014
This is version 66 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