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P0A1F6 (UDP_SALTY) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 55. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:STM3968
ORF Names:STMD1.21
OrganismSalmonella typhimurium
Taxonomic identifier90371 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella

Protein attributes

Sequence length253 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

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 term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological processnucleoside metabolic process

Inferred from electronic annotation. Source: InterPro

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: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 253252Uridine phosphorylase
PRO_0000063185

Experimental info

Sequence conflict2001A → R in CAA73795. Ref.2

Secondary structure

............................................. 253
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0A1F6 [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

« Hide 'large scale' references
[1]"Structure and expression of the gene encoding uridine phosphorylase (udp) in Salmonella typhimurium."
Errais L.L., Ukhabotina L.S., Eremina S.Y., Evdokimova A.A., Mironov A.S.
Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: LT2.
[2]"Protein engineering of uridine phosphorylase from Escherichia coli K-12. I. Cloning and expression of uridine phosphorylase genes from Klebsiella aerogenes and Salmonella typhimurium in E. coli."
Veiko V.P., Chebotaev D.V., Ovcharova I.V., Gul'Ko L.B.
Bioorg. Khim. 24:381-387(1998) [PubMed: 9661793] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: LT2.
[3]"Complete genome sequence of Salmonella enterica serovar Typhimurium LT2."
McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P., Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D., Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E. expand/collapse author list , Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R., Wilson R.K.
Nature 413:852-856(2001) [PubMed: 11677609] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: LT2 / SGSC1412 / ATCC 700720.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Y14282 Genomic DNA. Translation: CAA74658.2.
Y13360 Genomic DNA. Translation: CAA73795.1.
AF233324 Genomic DNA. Translation: AAF33424.1.
AE006468 Genomic DNA. Translation: AAL22812.1.
RefSeqNP_462853.1. NC_003197.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1RYZX-ray2.90A/B/C/D/E/F1-253[»]
1SJ9X-ray2.50A/B/C/D/E/F1-253[»]
1Y1QX-ray2.35A/B/C/D/E/F1-253[»]
1Y1RX-ray2.11A/B/C/D/E/F1-253[»]
1Y1SX-ray2.55A/B/C/D/E/F1-253[»]
1Y1TX-ray1.77A/F1-253[»]
1ZL2X-ray1.85A/B/C/D/E/F1-253[»]
2HN9X-ray2.12A/B/C/D/E/F1-253[»]
2HRDX-ray1.70A/B/C/D/E/F1-253[»]
2HSWX-ray1.99A/B1-253[»]
2HWUX-ray2.91A/B/C/D/E/F1-253[»]
2I8AX-ray1.64A/B/C/D/E/F2-252[»]
2IQ5X-ray1.90A/B2-252[»]
2OECX-ray2.19A/B/C/D/E/F2-252[»]
2OXFX-ray1.76A/F4-253[»]
2PGAX-ray1.74A/B/C/D/E/F1-253[»]
2QDKX-ray1.62A/B/C/D/E/F2-253[»]
2RJ3X-ray2.51A/B/C/D/E/F2-253[»]
3C74X-ray2.38A/B/C/D/E/F2-253[»]
3DDOX-ray1.50A/B/C/D/E/F1-253[»]
3DPSX-ray1.80A/F1-253[»]
3FWPX-ray1.86A/B/C/D/E/F1-253[»]
ProteinModelPortalP0A1F6.
SMRP0A1F6. Positions 1-253.
ModBaseSearch...

Proteomic databases

PRIDEP0A1F6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1255494.
GenomeReviewsGene locus STM3968 in contig AE006468_GR.
KEGGstm:STM3968.
PATRIC32386803. VBISalEnt20916_4187.

Phylogenomic databases

HOGENOMHBG617197.
OMASTREFTS.
ProtClustDBPRK11178.

Enzyme and pathway databases

BioCycSTYP99287:STM3968-MONOMER.

Family and domain databases

InterProIPR018017. Nucleoside_phosphorylase.
IPR018016. Nucleoside_phosphorylase_CS.
IPR000845. Nucleoside_phosphorylase_d.
IPR010058. Uridine_phosphorylase.
[Graphical view]
KOK00757.
PANTHERPTHR21234. PNP_UDP. 1 hit.
PfamPF01048. PNP_UDP_1. 1 hit.
[Graphical view]
TIGRFAMsTIGR01718. Uridine-psphlse. 1 hit.
PROSITEPS01232. PNP_UDP_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameUDP_SALTY
AccessionPrimary (citable) accession number: P0A1F6
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: January 25, 2012
This is version 55 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families