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P0A1F7 (UDP_SALTI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 66. 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:
Uridine phosphorylase

Short name=UPase
Short name=UrdPase
EC=2.4.2.3
Gene names
Name:udp
Ordered Locus Names:STY3591, t3329
OrganismSalmonella typhi [Complete proteome] [HAMAP]
Taxonomic identifier90370 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella

Protein attributes

Sequence length253 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the reversible phosphorylytic cleavage of uridine and deoxyuridine to uracil and ribose- or deoxyribose-1-phosphate. The produced molecules are then utilized as carbon and energy sources or in the rescue of pyrimidine bases for nucleotide synthesis By similarity.

Catalytic activity

Uridine + phosphate = uracil + alpha-D-ribose 1-phosphate.

Pathway

Pyrimidine metabolism; UMP biosynthesis via salvage pathway; uracil from uridine (phosphorylase route): step 1/1.

Subunit structure

Homohexamer By similarity.

Subcellular location

Cytoplasm By similarity.

Sequence similarities

Belongs to the PNP/UDP phosphorylase family.

Ontologies

Keywords
   Cellular componentCytoplasm
   Molecular functionGlycosyltransferase
Transferase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processUMP salvage

Inferred from electronic annotation. Source: UniProtKB-UniPathway

nucleotide catabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionuridine phosphorylase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 253252Uridine phosphorylase
PRO_0000063184

Sequences

Sequence LengthMass (Da)Tools
P0A1F7 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 63F26AFB8427BED2

FASTA25327,139
        10         20         30         40         50         60 
MSKSDVFHLG LTKNDLQGAQ LAIVPGDPER VEKIAALMDK PVKLASHREF TSWRAELDGK 

        70         80         90        100        110        120 
AVIVCSTGIG GPSTSIAVEE LAQLGIRTFL RIGTTGAIQP HINVGDVLVT TASVRLDGAS 

       130        140        150        160        170        180 
LHFAPMEFPA VADFACTTAL VEAAKSIGAT THVGVTASSD TFYPGQERYD TYSGRVVRRF 

       190        200        210        220        230        240 
KGSMEEWQAM GVMNYEMESA TLLTMCASQG LRAGMVAGVI VNRTQQEIPN AETMKQTESH 

       250 
AVKIVVEAAR RLL 

« Hide

References

[1]"Complete genome sequence of a multiple drug resistant Salmonella enterica serovar Typhi CT18."
Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J., Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M., Baker S., Basham D., Brooks K., Chillingworth T., Connerton P., Cronin A., Davis P. expand/collapse author list , Davies R.M., Dowd L., White N., Farrar J., Feltwell T., Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K., Krogh A., Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C., Quail M.A., Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S., Barrell B.G.
Nature 413:848-852(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CT18.
[2]"Comparative genomics of Salmonella enterica serovar Typhi strains Ty2 and CT18."
Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J., Burland V., Kodoyianni V., Schwartz D.C., Blattner F.R.
J. Bacteriol. 185:2330-2337(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700931 / Ty2.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL513382 Genomic DNA. Translation: CAD07924.1.
AE014613 Genomic DNA. Translation: AAO70857.1.
RefSeqNP_457783.1. NC_003198.1.
NP_806997.1. NC_004631.1.

3D structure databases

ProteinModelPortalP0A1F7.
SMRP0A1F7. Positions 1-253.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING220341.STY3591.

Proteomic databases

PRIDEP0A1F7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAO70857; AAO70857; t3329.
CAD07924; CAD07924; CAD07924.
GeneID1249846.
KEGGsty:STY3591.
PATRIC18545288. VBISalEnt120419_3658.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG2820.
HOGENOMHOG000274897.
KOK00757.
OMANVMNFEM.
OrthoDBEOG676Z3T.

Enzyme and pathway databases

UniPathwayUPA00574; UER00633.

Family and domain databases

Gene3D3.40.50.1580. 1 hit.
InterProIPR018017. Nucleoside_phosphorylase.
IPR018016. Nucleoside_phosphorylase_CS.
IPR000845. Nucleoside_phosphorylase_d.
IPR010058. Uridine_phosphorylase.
[Graphical view]
PANTHERPTHR21234. PTHR21234. 1 hit.
PfamPF01048. PNP_UDP_1. 1 hit.
[Graphical view]
SUPFAMSSF53167. SSF53167. 1 hit.
TIGRFAMsTIGR01718. Uridine-psphlse. 1 hit.
PROSITEPS01232. PNP_UDP_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameUDP_SALTI
AccessionPrimary (citable) accession number: P0A1F7
Secondary accession number(s): O08432, O33808, Q9L6M8
Entry history
Integrated into UniProtKB/Swiss-Prot: March 1, 2005
Last sequence update: January 23, 2007
Last modified: May 14, 2014
This is version 66 of the entry and version 2 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