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P15188 (PYRF_USTMA) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 92. 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:PYR6
ORF Names:UM04214
OrganismUstilago maydis (strain 521 / FGSC 9021) (Corn smut fungus) [Reference proteome]
Taxonomic identifier237631 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaBasidiomycotaUstilaginomycotinaUstilaginomycetesUstilaginalesUstilaginaceaeUstilago

Protein attributes

Sequence length283 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

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 – 283283Orotidine 5'-phosphate decarboxylase
PRO_0000134689

Regions

Region62 – 643Substrate binding By similarity
Region93 – 10210Substrate binding By similarity

Sites

Active site951Proton donor By similarity
Binding site401Substrate By similarity
Binding site2201Substrate By similarity
Binding site2391Substrate By similarity

Experimental info

Sequence conflict2441A → T Ref.1

Sequences

Sequence LengthMass (Da)Tools
P15188 [UniParc].

Last modified December 12, 2006. Version 2.
Checksum: 7C2F0DBB3C7DDF47

FASTA28330,864
        10         20         30         40         50         60 
MSSITLQSYA SRAAKQPNPA AKALLECMER KQTNLCVSID VTNKQDLLDV CEAVGRNVCL 

        70         80         90        100        110        120 
VKTHIDIVED FDMDLVHQLT QLSEKHDFLI FEDRKFADIG NTVSLQYSAG VHKIASWSHI 

       130        140        150        160        170        180 
TNAHLVPGPS VISGLAKVGQ PLGRGLLLLA EMSSEGALTK GDYTQACVDE AHKDTTGFVC 

       190        200        210        220        230        240 
GFIAMSRVDE RERANTHRDL LILTPGVGLD VKGDGLGQQY RTPDQVIRES GCDVIIVGRG 

       250        260        270        280 
IYGALTTEEG KADKKAAFAK VSEQGERYKT AGWDAYLKRI GQK 

« Hide

References

« Hide 'large scale' references
[1]"Isolation of metabolic genes and demonstration of gene disruption in the phytopathogenic fungus Ustilago maydis."
Kronstad J.W., Wang J., Covert S.F., Holden D.W., McKnight G.L., Leong S.A.
Gene 79:97-106(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Insights from the genome of the biotrophic fungal plant pathogen Ustilago maydis."
Kaemper J., Kahmann R., Boelker M., Ma L.-J., Brefort T., Saville B.J., Banuett F., Kronstad J.W., Gold S.E., Mueller O., Perlin M.H., Woesten H.A.B., de Vries R., Ruiz-Herrera J., Reynaga-Pena C.G., Snetselaar K., McCann M., Perez-Martin J. expand/collapse author list , Feldbruegge M., Basse C.W., Steinberg G., Ibeas J.I., Holloman W., Guzman P., Farman M.L., Stajich J.E., Sentandreu R., Gonzalez-Prieto J.M., Kennell J.C., Molina L., Schirawski J., Mendoza-Mendoza A., Greilinger D., Muench K., Roessel N., Scherer M., Vranes M., Ladendorf O., Vincon V., Fuchs U., Sandrock B., Meng S., Ho E.C.H., Cahill M.J., Boyce K.J., Klose J., Klosterman S.J., Deelstra H.J., Ortiz-Castellanos L., Li W., Sanchez-Alonso P., Schreier P.H., Haeuser-Hahn I., Vaupel M., Koopmann E., Friedrich G., Voss H., Schlueter T., Margolis J., Platt D., Swimmer C., Gnirke A., Chen F., Vysotskaia V., Mannhaupt G., Gueldener U., Muensterkoetter M., Haase D., Oesterheld M., Mewes H.-W., Mauceli E.W., DeCaprio D., Wade C.M., Butler J., Young S.K., Jaffe D.B., Calvo S.E., Nusbaum C., Galagan J.E., Birren B.W.
Nature 444:97-101(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 521 / FGSC 9021.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M27247 Unassigned DNA. No translation available.
AACP01000149 Genomic DNA. Translation: EAK85218.1.
PIRDCUSOP. JQ0013.
RefSeqXP_760361.1. XM_755268.1.

3D structure databases

ProteinModelPortalP15188.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING5270.UM04214.1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiUM04214T0; UM04214P0; UM04214.
GeneID3632319.
KEGGuma:UM04214.1.

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_USTMA
AccessionPrimary (citable) accession number: P15188
Secondary accession number(s): Q4P6P9
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: December 12, 2006
Last modified: November 13, 2013
This is version 92 of the entry and version 2 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