ID   UDP_TREPA               Reviewed;         258 AA.
AC   O83990;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   03-AUG-2022, entry version 120.
DE   RecName: Full=Uridine phosphorylase;
DE            Short=UPase;
DE            Short=UrdPase;
DE            EC=2.4.2.3;
GN   Name=udp; OrderedLocusNames=TP_1027;
OS   Treponema pallidum (strain Nichols).
OC   Bacteria; Spirochaetes; Spirochaetales; Treponemataceae; Treponema.
OX   NCBI_TaxID=243276;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Nichols;
RX   PubMed=9665876; DOI=10.1126/science.281.5375.375;
RA   Fraser C.M., Norris S.J., Weinstock G.M., White O., Sutton G.G.,
RA   Dodson R.J., Gwinn M.L., Hickey E.K., Clayton R.A., Ketchum K.A.,
RA   Sodergren E., Hardham J.M., McLeod M.P., Salzberg S.L., Peterson J.D.,
RA   Khalak H.G., Richardson D.L., Howell J.K., Chidambaram M., Utterback T.R.,
RA   McDonald L.A., Artiach P., Bowman C., Cotton M.D., Fujii C., Garland S.A.,
RA   Hatch B., Horst K., Roberts K.M., Sandusky M., Weidman J.F., Smith H.O.,
RA   Venter J.C.;
RT   "Complete genome sequence of Treponema pallidum, the syphilis spirochete.";
RL   Science 281:375-388(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}.
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DR   EMBL; AE000520; AAC65977.1; -; Genomic_DNA.
DR   PIR; F71251; F71251.
DR   RefSeq; WP_010882471.1; NC_021490.2.
DR   AlphaFoldDB; O83990; -.
DR   SMR; O83990; -.
DR   STRING; 243276.TPANIC_1027; -.
DR   EnsemblBacteria; AAC65977; AAC65977; TP_1027.
DR   GeneID; 57879539; -.
DR   KEGG; tpa:TP_1027; -.
DR   eggNOG; COG2820; Bacteria.
DR   HOGENOM; CLU_068457_0_0_12; -.
DR   OMA; NLVEGTQ; -.
DR   OrthoDB; 1028277at2; -.
DR   UniPathway; UPA00574; UER00633.
DR   Proteomes; UP000000811; Chromosome.
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; Reference proteome; Transferase.
FT   CHAIN           1..258
FT                   /note="Uridine phosphorylase"
FT                   /id="PRO_0000063190"
SQ   SEQUENCE   258 AA;  27920 MW;  247ABA619316D72D CRC64;
     MKLVYSTDCE YHIGLKASDI GHYVILPGDP ARSEKIAQHF SHPHKVGHNR EYVTYTGTLC
     ETPVSVMSTG IGGPSTAIGV EELIHLGAHT FIRVGTSGGM QPDILAGTVV IATGAIRFEG
     TSKEYAPVEF PAVPDFTVTA ALKHAAEDVQ VRHALGVVQC KDNFYGQHSP HTMPVHAELT
     QKWHAWIACN TLASEMESAA LFVLGSVRRV RTGAVLLVIG NQTRRAQGLE DIQVHDTENA
     IRVAVEAVKL LITQDSPR