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   13-SEP-2023, entry version 94.
DE   RecName: Full=Uridine phosphorylase {ECO:0000250|UniProtKB:P12758};
DE            Short=UPase {ECO:0000250|UniProtKB:P12758};
DE            Short=UrdPase {ECO:0000250|UniProtKB:P12758};
DE            EC=2.4.2.3 {ECO:0000250|UniProtKB:P12758};
GN   Name=udp;
OS   Klebsiella aerogenes (Enterobacter aerogenes).
OC   Bacteria; Pseudomonadota; 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       to uracil and ribose-1-phosphate. {ECO:0000250|UniProtKB:P12758}.
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         Evidence={ECO:0000250|UniProtKB:P12758};
CC   -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via salvage pathway;
CC       uracil from uridine (phosphorylase route): step 1/1.
CC   -!- SUBUNIT: Homohexamer. {ECO:0000250|UniProtKB:P12758}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P12758}.
CC   -!- SIMILARITY: Belongs to the PNP/UDP phosphorylase family. {ECO:0000305}.
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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   CDD; cd17767; UP_EcUdp-like; 1.
DR   Gene3D; 3.40.50.1580; Nucleoside phosphorylase domain; 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   NCBIfam; TIGR01718; Uridine-psphlse; 1.
DR   PANTHER; PTHR43691:SF11; FI09636P-RELATED; 1.
DR   PANTHER; PTHR43691; URIDINE PHOSPHORYLASE; 1.
DR   Pfam; PF01048; PNP_UDP_1; 1.
DR   SUPFAM; SSF53167; Purine and uridine phosphorylases; 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
//