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Q757S1 (PYRF_ASHGO) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 67. 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
Uridine 5'-monophosphate synthase
Short name=UMP synthase
Gene names
Name:URA3
Ordered Locus Names:AEL059W
OrganismAshbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056) (Yeast) (Eremothecium gossypii) [Reference proteome]
Taxonomic identifier284811 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeEremothecium

Protein attributes

Sequence length267 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

Orotidine 5'-phosphate = UMP + CO2.

Pathway

Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 2/2.

Sequence similarities

Belongs to the OMP decarboxylase family.

Ontologies

Keywords
   Biological processPyrimidine biosynthesis
   Molecular functionDecarboxylase
Lyase
   Technical termComplete proteome
Reference 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

   Cellular_componentcytosol

Inferred from electronic annotation. Source: EnsemblFungi

   Molecular_functionorotidine-5'-phosphate decarboxylase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 267267Orotidine 5'-phosphate decarboxylase
PRO_0000134639

Regions

Region59 – 613Substrate binding By similarity
Region91 – 10010Substrate binding By similarity

Sites

Active site931Proton donor By similarity
Binding site371Substrate By similarity
Binding site2171Substrate By similarity
Binding site2351Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q757S1 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: 6DA3A796CAF1EF8D

FASTA26729,210
        10         20         30         40         50         60 
MSTKSYAERA KAHNSPVARK LLALMHEKKT NLCASLDVRT SRKLLELADT LGPHICLLKT 

        70         80         90        100        110        120 
HVDILTDFDI ETTVKPLQQL AAKHNFMIFE DRKFADIGNT VKLQYSSGVY RIAEWADITN 

       130        140        150        160        170        180 
AHGVTGPGVI AGLKEAAKLA SQEPRGLLML AELSSQGSLA RGDYTAGVVE MAKLDKDFVI 

       190        200        210        220        230        240 
GFIAQRDMGG RADGFDWLIM TPGVGLDDKG DGLGQQYRTV DEVVSDGTDV IIVGRGLFDK 

       250        260 
GRDPNVEGAR YRKAGWEAYL RRIGETS 

« Hide

References

« Hide 'large scale' references
[1]"The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces cerevisiae genome."
Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S., Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A., Gaffney T.D., Philippsen P.
Science 304:304-307(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056.
[2]"Genomes of Ashbya fungi isolated from insects reveal four mating-type loci, numerous translocations, lack of transposons, and distinct gene duplications."
Dietrich F.S., Voegeli S., Kuo S., Philippsen P.
G3 (Bethesda) 3:1225-1239(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE016818 Genomic DNA. Translation: AAS52626.1.
RefSeqNP_984802.1. NM_210156.1.

3D structure databases

ProteinModelPortalQ757S1.
SMRQ757S1. Positions 1-265.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING33169.AGOS_AEL059W.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiAAS52626; AAS52626; AGOS_AEL059W.
GeneID4620994.
KEGGago:AGOS_AEL059W.

Phylogenomic databases

eggNOGCOG0284.
HOGENOMHOG000213905.
KOK01591.
OMAMGQQYRT.
OrthoDBEOG7CVQ76.

Enzyme and pathway databases

UniPathwayUPA00070; UER00120.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
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_ASHGO
AccessionPrimary (citable) accession number: Q757S1
Entry history
Integrated into UniProtKB/Swiss-Prot: August 31, 2004
Last sequence update: July 5, 2004
Last modified: July 9, 2014
This is version 67 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways