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Q13E64 (PYRF_RHOPS) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 53. 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:RPD_0387
OrganismRhodopseudomonas palustris (strain BisB5) [Complete proteome] [HAMAP]
Taxonomic identifier316057 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBradyrhizobiaceaeRhodopseudomonas

Protein attributes

Sequence length235 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 – 235235Orotidine 5'-phosphate decarboxylase HAMAP-Rule MF_01200
PRO_1000065939

Regions

Region66 – 7510Substrate binding By similarity

Sites

Active site681Proton donor By similarity
Binding site171Substrate By similarity
Binding site391Substrate By similarity
Binding site1211Substrate 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
Q13E64 [UniParc].

Last modified October 31, 2006. Version 1.
Checksum: 38B6A5DD7945B55B

FASTA23524,286
        10         20         30         40         50         60 
MAQADPADRD RLIVALDVPS VDAANAMIEK LGDSVGFYKI GYQLAYAGGL PLVEKLARAG 

        70         80         90        100        110        120 
KKVFVDLKLH DIGNTVARGV ESLNSLGATF LTVHAYPQTM KAAVAARGDS GLKILAVTVL 

       130        140        150        160        170        180 
TSYDDSDLAD AGYRFGVRDL VEARARQALA IGVDGLVCSP EEAANLRGIV GPDMALVTPG 

       190        200        210        220        230 
IRPAGAAAGD QKRIMTPARA IAAGASHLVV GRPVMEAADP KQAAEAIVAE IAQAT 

« Hide

References

[1]"Complete sequence of Rhodopseudomonas palustris BisB5."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M. expand/collapse author list , Hauser L., Pelletier D.A., Kyrpides N., Lykidis A., Oda Y., Harwood C.S., Richardson P.
Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: BisB5.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000283 Genomic DNA. Translation: ABE37625.1.
RefSeqYP_567526.1. NC_007958.1.

3D structure databases

ProteinModelPortalQ13E64.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING316057.RPD_0387.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABE37625; ABE37625; RPD_0387.
GeneID4020853.
KEGGrpd:RPD_0387.
PATRIC23275621. VBIRhoPal120395_0399.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0284.
HOGENOMHOG000226070.
KOK01591.
OMAHAKEPRE.
OrthoDBEOG6N6815.

Enzyme and pathway databases

BioCycRPAL316057:GHDC-399-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_RHOPS
AccessionPrimary (citable) accession number: Q13E64
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: October 31, 2006
Last modified: May 14, 2014
This is version 53 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