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Q5HW86 (PYRF_CAMJR) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 62. 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:CJE0430
OrganismCampylobacter jejuni (strain RM1221) [Complete proteome] [HAMAP]
Taxonomic identifier195099 [NCBI]
Taxonomic lineageBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesCampylobacteraceaeCampylobacter

Protein attributes

Sequence length279 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 – 279279Orotidine 5'-phosphate decarboxylase HAMAP-Rule MF_01200
PRO_0000241851

Regions

Region58 – 6710Substrate binding By similarity

Sites

Active site601Proton donor By similarity
Binding site81Substrate By similarity
Binding site301Substrate By similarity
Binding site1171Substrate By similarity
Binding site1771Substrate By similarity
Binding site1861Substrate By similarity
Binding site2061Substrate; via amide nitrogen By similarity
Binding site2071Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5HW86 [UniParc].

Last modified February 15, 2005. Version 1.
Checksum: DAA1D9B30D0CA6AE

FASTA27932,242
        10         20         30         40         50         60 
MKLCVALDLS TKEECLQLAK ELKNLDIWLK VGLRAYLRDG FKFIEELKKV DDFKIFLDLK 

        70         80         90        100        110        120 
IHDIPNTMAD ACEEVSKLGV DMINIHASAG KIAIQEVMTR LSKFSKRPLV LAVSALTSFD 

       130        140        150        160        170        180 
EENFFSIYRQ KIEEAVINFS KISYENGLDG MVCSVFESKK IKEHTSSNFL TLTPGIRPFG 

       190        200        210        220        230        240 
ETSDDQKRVA NLAMARENLS DYIVVGRPIY KNENPRAVCE KILNKIHRKN ISENDIEQNY 

       250        260        270 
EVIQQKEWDM CNHFEEWIKT QPDKEHALKE FYAKCGIKY 

« Hide

References

[1]"Major structural differences and novel potential virulence mechanisms from the genomes of multiple Campylobacter species."
Fouts D.E., Mongodin E.F., Mandrell R.E., Miller W.G., Rasko D.A., Ravel J., Brinkac L.M., DeBoy R.T., Parker C.T., Daugherty S.C., Dodson R.J., Durkin A.S., Madupu R., Sullivan S.A., Shetty J.U., Ayodeji M.A., Shvartsbeyn A., Schatz M.C. expand/collapse author list , Badger J.H., Fraser C.M., Nelson K.E.
PLoS Biol. 3:72-85(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: RM1221.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000025 Genomic DNA. Translation: AAW35019.1.
RefSeqYP_178449.1. NC_003912.7.

3D structure databases

ProteinModelPortalQ5HW86.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING195099.CJE0430.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAW35019; AAW35019; CJE0430.
GeneID3231192.
KEGGcjr:CJE0430.
PATRIC20042560. VBICamJej134361_0429.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0284.
HOGENOMHOG000226071.
KOK01591.
OMAHAKEPRE.
OrthoDBEOG6N6815.

Enzyme and pathway databases

BioCycCJEJ195099:GJC0-435-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_CAMJR
AccessionPrimary (citable) accession number: Q5HW86
Entry history
Integrated into UniProtKB/Swiss-Prot: June 27, 2006
Last sequence update: February 15, 2005
Last modified: May 14, 2014
This is version 62 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