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

B0KUJ6 (PYRF_PSEPG) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 42. 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:PputGB1_1394
OrganismPseudomonas putida (strain GB-1) [Complete proteome] [HAMAP]
Taxonomic identifier76869 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

Protein attributes

Sequence length233 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 – 233233Orotidine 5'-phosphate decarboxylase HAMAP-Rule MF_01200
PRO_1000085494

Regions

Region62 – 7110Substrate binding By similarity

Sites

Active site641Proton donor By similarity
Binding site131Substrate By similarity
Binding site351Substrate By similarity
Binding site1221Substrate By similarity
Binding site1821Substrate By similarity
Binding site1911Substrate By similarity
Binding site2111Substrate; via amide nitrogen By similarity
Binding site2121Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
B0KUJ6 [UniParc].

Last modified March 18, 2008. Version 1.
Checksum: 9EC76B359E7DAD93

FASTA23324,551
        10         20         30         40         50         60 
MSACQTPLIV ALDFPTREAA LKLADQLDPA LCRVKVGKEL FTSSASGIVE TLCDKGFEVF 

        70         80         90        100        110        120 
LDLKFHDIPN TTAMAVKAAA EMGVWMVNVH CSGGLRMMAA CREELAKRSG PQPLLIGVTV 

       130        140        150        160        170        180 
LTSMEREDLA GIGLDVDPQE QVLRLAALAQ KAGMDGLVCS ALEAPALKAA HPSLQLVTPG 

       190        200        210        220        230 
IRPAGSAQDD QRRILTPRQA LDAGSDYLVI GRPISQAADP AQALAAVVAE IRG 

« Hide

References

[1]"Complete sequence of Pseudomonas putida GB-1."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Bruce D., Goodwin L., Chertkov O., Brettin T., Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M. expand/collapse author list , Hauser L., Kyrpides N., Kim E., McCarthy J.K., Richardson P.
Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: GB-1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000926 Genomic DNA. Translation: ABY97301.1.
RefSeqYP_001667637.1. NC_010322.1.

3D structure databases

ProteinModelPortalB0KUJ6.
SMRB0KUJ6. Positions 5-232.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING76869.PputGB1_1394.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABY97301; ABY97301; PputGB1_1394.
GeneID5869158.
KEGGppg:PputGB1_1394.
PATRIC19929769. VBIPsePut76638_1400.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0284.
HOGENOMHOG000226070.
KOK01591.
OMARPITQSA.
OrthoDBEOG6N6815.

Enzyme and pathway databases

BioCycPPUT76869:GIXB-1429-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_PSEPG
AccessionPrimary (citable) accession number: B0KUJ6
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: March 18, 2008
Last modified: May 14, 2014
This is version 42 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