UDP_SALTY
ID UDP_SALTY Reviewed; 253 AA.
AC P0A1F6; O08432; O33808; Q9L6M8;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Uridine phosphorylase;
DE Short=UPase;
DE Short=UrdPase;
DE EC=2.4.2.3;
GN Name=udp; OrderedLocusNames=STM3968; ORFNames=STMD1.21;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=LT2;
RA Errais L.L., Ukhabotina L.S., Eremina S.Y., Evdokimova A.A., Mironov A.S.;
RT "Structure and expression of the gene encoding uridine phosphorylase (udp)
RT in Salmonella typhimurium.";
RL Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=LT2;
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).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
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; Y14282; CAA74658.2; -; Genomic_DNA.
DR EMBL; Y13360; CAA73795.1; -; Genomic_DNA.
DR EMBL; AF233324; AAF33424.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL22812.1; -; Genomic_DNA.
DR RefSeq; NP_462853.1; NC_003197.2.
DR RefSeq; WP_000045169.1; NC_003197.2.
DR PDB; 1RYZ; X-ray; 2.90 A; A/B/C/D/E/F=1-253.
DR PDB; 1SJ9; X-ray; 2.50 A; A/B/C/D/E/F=1-253.
DR PDB; 1Y1Q; X-ray; 2.35 A; A/B/C/D/E/F=1-253.
DR PDB; 1Y1R; X-ray; 2.11 A; A/B/C/D/E/F=1-253.
DR PDB; 1Y1S; X-ray; 2.55 A; A/B/C/D/E/F=1-253.
DR PDB; 1Y1T; X-ray; 1.77 A; A/F=1-253.
DR PDB; 1ZL2; X-ray; 1.85 A; A/B/C/D/E/F=1-253.
DR PDB; 2HN9; X-ray; 2.12 A; A/B/C/D/E/F=1-253.
DR PDB; 2HRD; X-ray; 1.70 A; A/B/C/D/E/F=1-253.
DR PDB; 2HSW; X-ray; 1.99 A; A/B=1-253.
DR PDB; 2HWU; X-ray; 2.91 A; A/B/C/D/E/F=1-253.
DR PDB; 2I8A; X-ray; 1.64 A; A/B/C/D/E/F=2-253.
DR PDB; 2IQ5; X-ray; 1.90 A; A/B=2-253.
DR PDB; 2OEC; X-ray; 2.19 A; A/B/C/D/E/F=2-253.
DR PDB; 2OXF; X-ray; 1.76 A; A/F=4-253.
DR PDB; 2PGA; X-ray; 1.74 A; A/B/C/D/E/F=1-253.
DR PDB; 2QDK; X-ray; 1.62 A; A/B/C/D/E/F=2-253.
DR PDB; 2RJ3; X-ray; 2.51 A; A/B/C/D/E/F=2-253.
DR PDB; 3C74; X-ray; 2.38 A; A/B/C/D/E/F=2-253.
DR PDB; 3DDO; X-ray; 1.50 A; A/B/C/D/E/F=1-253.
DR PDB; 3DPS; X-ray; 1.80 A; A/F=1-253.
DR PDB; 3FWP; X-ray; 1.86 A; A/B/C/D/E/F=1-253.
DR PDB; 4E1V; X-ray; 2.15 A; A/B/C/D/E/F/G/H/I=1-253.
DR PDB; 4OGK; X-ray; 2.40 A; A/B/C/D/E/F=1-253.
DR PDBsum; 1RYZ; -.
DR PDBsum; 1SJ9; -.
DR PDBsum; 1Y1Q; -.
DR PDBsum; 1Y1R; -.
DR PDBsum; 1Y1S; -.
DR PDBsum; 1Y1T; -.
DR PDBsum; 1ZL2; -.
DR PDBsum; 2HN9; -.
DR PDBsum; 2HRD; -.
DR PDBsum; 2HSW; -.
DR PDBsum; 2HWU; -.
DR PDBsum; 2I8A; -.
DR PDBsum; 2IQ5; -.
DR PDBsum; 2OEC; -.
DR PDBsum; 2OXF; -.
DR PDBsum; 2PGA; -.
DR PDBsum; 2QDK; -.
DR PDBsum; 2RJ3; -.
DR PDBsum; 3C74; -.
DR PDBsum; 3DDO; -.
DR PDBsum; 3DPS; -.
DR PDBsum; 3FWP; -.
DR PDBsum; 4E1V; -.
DR PDBsum; 4OGK; -.
DR AlphaFoldDB; P0A1F6; -.
DR SMR; P0A1F6; -.
DR STRING; 99287.STM3968; -.
DR DrugBank; DB04627; Cyclouridine.
DR PaxDb; P0A1F6; -.
DR EnsemblBacteria; AAL22812; AAL22812; STM3968.
DR GeneID; 1255494; -.
DR GeneID; 66758248; -.
DR KEGG; stm:STM3968; -.
DR PATRIC; fig|99287.12.peg.4187; -.
DR HOGENOM; CLU_068457_0_0_6; -.
DR OMA; MSDVFHL; -.
DR PhylomeDB; P0A1F6; -.
DR BioCyc; SENT99287:STM3968-MON; -.
DR BRENDA; 2.4.2.3; 5542.
DR UniPathway; UPA00574; UER00633.
DR EvolutionaryTrace; P0A1F6; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0004850; F:uridine phosphorylase activity; IBA:GO_Central.
DR GO; GO:0009166; P:nucleotide catabolic process; IEA:InterPro.
DR GO; GO:0044206; P:UMP salvage; IEA:UniProtKB-UniPathway.
DR GO; GO:0006218; P:uridine catabolic process; IBA:GO_Central.
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 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Glycosyltransferase; Reference proteome;
KW Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..253
FT /note="Uridine phosphorylase"
FT /id="PRO_0000063185"
FT CONFLICT 200
FT /note="A -> R (in Ref. 2; CAA73795)"
FT /evidence="ECO:0000305"
FT TURN 7..9
FT /evidence="ECO:0007829|PDB:3DDO"
FT HELIX 13..16
FT /evidence="ECO:0007829|PDB:3DDO"
FT STRAND 21..26
FT /evidence="ECO:0007829|PDB:3DDO"
FT HELIX 28..30
FT /evidence="ECO:0007829|PDB:3DDO"
FT HELIX 31..35
FT /evidence="ECO:0007829|PDB:3DDO"
FT STRAND 38..47
FT /evidence="ECO:0007829|PDB:3DDO"
FT STRAND 50..57
FT /evidence="ECO:0007829|PDB:3DDO"
FT STRAND 60..65
FT /evidence="ECO:0007829|PDB:3DDO"
FT HELIX 71..83
FT /evidence="ECO:0007829|PDB:3DDO"
FT STRAND 88..95
FT /evidence="ECO:0007829|PDB:3DDO"
FT STRAND 107..118
FT /evidence="ECO:0007829|PDB:3DDO"
FT HELIX 119..122
FT /evidence="ECO:0007829|PDB:3DDO"
FT STRAND 126..128
FT /evidence="ECO:0007829|PDB:1RYZ"
FT HELIX 134..146
FT /evidence="ECO:0007829|PDB:3DDO"
FT STRAND 151..160
FT /evidence="ECO:0007829|PDB:3DDO"
FT HELIX 164..166
FT /evidence="ECO:0007829|PDB:3DDO"
FT STRAND 171..173
FT /evidence="ECO:0007829|PDB:3DDO"
FT HELIX 178..180
FT /evidence="ECO:0007829|PDB:3DDO"
FT HELIX 183..189
FT /evidence="ECO:0007829|PDB:3DDO"
FT STRAND 194..198
FT /evidence="ECO:0007829|PDB:3DDO"
FT HELIX 199..207
FT /evidence="ECO:0007829|PDB:3DDO"
FT TURN 208..210
FT /evidence="ECO:0007829|PDB:3DDO"
FT STRAND 212..219
FT /evidence="ECO:0007829|PDB:3DDO"
FT TURN 223..225
FT /evidence="ECO:0007829|PDB:2HRD"
FT HELIX 231..234
FT /evidence="ECO:0007829|PDB:3DDO"
FT TURN 235..239
FT /evidence="ECO:0007829|PDB:1SJ9"
FT HELIX 240..252
FT /evidence="ECO:0007829|PDB:3DDO"
SQ SEQUENCE 253 AA; 27139 MW; 63F26AFB8427BED2 CRC64;
MSKSDVFHLG LTKNDLQGAQ LAIVPGDPER VEKIAALMDK PVKLASHREF TSWRAELDGK
AVIVCSTGIG GPSTSIAVEE LAQLGIRTFL RIGTTGAIQP HINVGDVLVT TASVRLDGAS
LHFAPMEFPA VADFACTTAL VEAAKSIGAT THVGVTASSD TFYPGQERYD TYSGRVVRRF
KGSMEEWQAM GVMNYEMESA TLLTMCASQG LRAGMVAGVI VNRTQQEIPN AETMKQTESH
AVKIVVEAAR RLL
