SWISSPROT: A0A0E1NRK8_YERPA

ID   A0A0E1NRK8_YERPA        Unreviewed;       253 AA.
AC   A0A0E1NRK8;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   08-MAY-2019, entry version 28.
DE   RecName: Full=Uridine phosphorylase {ECO:0000256|RuleBase:RU361131};
DE            EC=2.4.2.3 {ECO:0000256|RuleBase:RU361131};
GN   OrderedLocusNames=YPA_0238 {ECO:0000313|EMBL:ABG12207.1};
OS   Yersinia pestis bv. Antiqua (strain Antiqua).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=360102 {ECO:0000313|EMBL:ABG12207.1, ECO:0000313|Proteomes:UP000001971};
RN   [1] {ECO:0000313|EMBL:ABG12207.1, ECO:0000313|Proteomes:UP000001971}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Antiqua {ECO:0000313|EMBL:ABG12207.1,
RC   ECO:0000313|Proteomes:UP000001971};
RX   PubMed=16740952; DOI=10.1128/JB.00124-06;
RA   Chain P.S., Hu P., Malfatti S.A., Radnedge L., Larimer F.,
RA   Vergez L.M., Worsham P., Chu M.C., Andersen G.L.;
RT   "Complete genome sequence of Yersinia pestis strains Antiqua and
RT   Nepal516: evidence of gene reduction in an emerging pathogen.";
RL   J. Bacteriol. 188:4453-4463(2006).
CC   -!- FUNCTION: Catalyzes the reversible phosphorylytic cleavage of
CC       uridine and deoxyuridine to uracil and ribose- or deoxyribose-1-
CC       phosphate. The produced molecules are then utilized as carbon and
CC       energy sources or in the rescue of pyrimidine bases for nucleotide
CC       synthesis. {ECO:0000256|RuleBase:RU361131}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=phosphate + uridine = alpha-D-ribose 1-phosphate +
CC         uracil; Xref=Rhea:RHEA:24388, ChEBI:CHEBI:16704,
CC         ChEBI:CHEBI:17568, ChEBI:CHEBI:43474, ChEBI:CHEBI:57720;
CC         EC=2.4.2.3; Evidence={ECO:0000256|RuleBase:RU361131};
CC   -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via salvage
CC       pathway; uracil from uridine (phosphorylase route): step 1/1.
CC       {ECO:0000256|RuleBase:RU361131}.
CC   -!- SUBUNIT: Homohexamer. {ECO:0000256|SAAS:SAAS01083847}.
CC   -!- SIMILARITY: Belongs to the PNP/UDP phosphorylase family.
CC       {ECO:0000256|RuleBase:RU361131, ECO:0000256|SAAS:SAAS00886275}.
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DR   EMBL; CP000308; ABG12207.1; -; Genomic_DNA.
DR   RefSeq; WP_002211528.1; NZ_CP009906.1.
DR   SMR; A0A0E1NRK8; -.
DR   EnsemblBacteria; ABG12207; ABG12207; YPA_0238.
DR   EnsemblBacteria; AJJ77913; AJJ77913; CH58_3083.
DR   KEGG; ypa:YPA_0238; -.
DR   PATRIC; fig|360102.15.peg.3234; -.
DR   KO; K00757; -.
DR   OMA; MSDVFHL; -.
DR   UniPathway; UPA00574; UER00633.
DR   Proteomes; UP000001971; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0004850; F:uridine phosphorylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009116; P:nucleoside metabolic process; IEA:InterPro.
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   PANTHER; PTHR43691:SF7; PTHR43691:SF7; 1.
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;
DR   PRODOM; A0A0E1NRK8.
DR   SWISS-2DPAGE; A0A0E1NRK8.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001971};
KW   Glycosyltransferase {ECO:0000256|RuleBase:RU361131,
KW   ECO:0000256|SAAS:SAAS00886268};
KW   Transferase {ECO:0000256|RuleBase:RU361131,
KW   ECO:0000256|SAAS:SAAS00886295}.
FT   DOMAIN       21    243       PNP_UDP_1. {ECO:0000259|Pfam:PF01048}.
SQ   SEQUENCE   253 AA;  27095 MW;  FAAC318B147C1C03 CRC64;
     MAKSDVFHLG LTKNDLQGAT LAIVPGDPQR VEKIAKLMDN PVHLASHREF TSWRAELDGK
     AVIVCSTGIG GPSTSIAVEE LAQLGVRTFL RIGTTGAIQP HINVGDVLVT TAAVRLDGAS
     LHFAPMEFPA VADFSCTTAL VNAAKSVGAT THIGITASSD TFYPGQERYD TFSGRVVRHF
     KGSMEEWQSM GVMNYEMESA TLLTMCASQG LRAGMVAGVI VNRTQQEIPN EETMKATESH
     AVKIVVEAAR HLL
//