UDP_KLEAE
ID UDP_KLEAE Reviewed; 253 AA.
AC O08444;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Uridine phosphorylase;
DE Short=UPase;
DE Short=UrdPase;
DE EC=2.4.2.3;
GN Name=udp;
OS Klebsiella aerogenes (Enterobacter aerogenes).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX NCBI_TaxID=548;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=4140;
RX PubMed=9661793;
RA Veiko V.P., Chebotaev D.V., Ovcharova I.V., Gul'Ko L.B.;
RT "Protein engineering of uridine phosphorylase from Escherichia coli K-12.
RT I. Cloning and expression of uridine phosphorylase genes from Klebsiella
RT aerogenes and Salmonella typhimurium in E. coli.";
RL Bioorg. Khim. 24:381-387(1998).
CC -!- FUNCTION: Catalyzes the reversible phosphorylytic cleavage of uridine
CC and deoxyuridine to uracil and ribose- or deoxyribose-1-phosphate. The
CC produced molecules are then utilized as carbon and energy sources or in
CC the rescue of pyrimidine bases for nucleotide synthesis (By
CC similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=phosphate + uridine = alpha-D-ribose 1-phosphate + uracil;
CC Xref=Rhea:RHEA:24388, ChEBI:CHEBI:16704, ChEBI:CHEBI:17568,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57720; EC=2.4.2.3;
CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via salvage pathway;
CC uracil from uridine (phosphorylase route): step 1/1.
CC -!- SUBUNIT: Homohexamer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the PNP/UDP phosphorylase family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; Y13414; CAA73838.1; -; Genomic_DNA.
DR PIR; T46830; T46830.
DR AlphaFoldDB; O08444; -.
DR SMR; O08444; -.
DR STRING; 548.EAG7_03989; -.
DR UniPathway; UPA00574; UER00633.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004850; F:uridine phosphorylase activity; IEA:UniProtKB-EC.
DR GO; GO:0009164; P:nucleoside catabolic process; IEA:UniProt.
DR GO; GO:0009166; P:nucleotide catabolic process; IEA:InterPro.
DR GO; GO:0044206; P:UMP salvage; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.40.50.1580; -; 1.
DR InterPro; IPR018016; Nucleoside_phosphorylase_CS.
DR InterPro; IPR000845; Nucleoside_phosphorylase_d.
DR InterPro; IPR035994; Nucleoside_phosphorylase_sf.
DR InterPro; IPR010058; Uridine_phosphorylase.
DR Pfam; PF01048; PNP_UDP_1; 1.
DR SUPFAM; SSF53167; SSF53167; 1.
DR TIGRFAMs; TIGR01718; Uridine-psphlse; 1.
DR PROSITE; PS01232; PNP_UDP_1; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Glycosyltransferase; Transferase.
FT CHAIN 1..253
FT /note="Uridine phosphorylase"
FT /id="PRO_0000063187"
SQ SEQUENCE 253 AA; 27034 MW; 617A62F00386A405 CRC64;
MSKSDVFHLG LTKNDLQGAT LAIVPGDPER VEKIAALMDK PVKLASHREF TSWRAELDGK
PVIVCSTGIG GPSTSIAVEE LAHVGVRTFL RIGTTGAIQP HINVGDVLVT TGSVRLDGAS
LHFAPMEFPA VADFACTTAL VEAAKSIGAT THIGVTASSD TFYPGQERYD TFSGRVVSRF
KGSMEEWQAM GVMNYEMESA TLLTMCASQG LRAGMVAGVI VNRTQQEIPN AETMKQTESH
AVKIVVEAAR RLL