ID UDP_ECOLI Reviewed; 253 AA.
AC P12758; Q2M8D6;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 01-MAY-2013, entry version 137.
DE RecName: Full=Uridine phosphorylase;
DE Short=UPase;
DE Short=UrdPase;
DE EC=2.4.2.3;
GN Name=udp; OrderedLocusNames=b3831, JW3808;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=2674901; DOI=10.1093/nar/17.16.6741;
RA Walton L., Richards C.A., Elwell L.P.;
RT "Nucleotide sequence of the Escherichia coli uridine phosphorylase
RT (udp) gene.";
RL Nucleic Acids Res. 17:6741-6741(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=1379743; DOI=10.1126/science.1379743;
RA Daniels D.L., Plunkett G. III, Burland V.D., Blattner F.R.;
RT "Analysis of the Escherichia coli genome: DNA sequence of the region
RT from 84.5 to 86.5 minutes.";
RL Science 257:771-778(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
RA Mau B., Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1474(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains
RT MG1655 and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP PROTEIN SEQUENCE OF 2-18.
RX PubMed=8506346; DOI=10.1073/pnas.90.11.5011;
RA Henzel W.J., Billeci T.M., Stults J.T., Wong S.C., Grimley C.,
RA Watanabe C.;
RT "Identifying proteins from two-dimensional gels by molecular mass
RT searching of peptide fragments in protein sequence databases.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:5011-5015(1993).
RN [6]
RP PROTEIN SEQUENCE OF 2-12.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RA Frutiger S., Hughes G.J., Pasquali C., Hochstrasser D.F.;
RL Submitted (FEB-1996) to UniProtKB.
RN [7]
RP PROTEIN SEQUENCE OF 2-16.
RC STRAIN=K12;
RX PubMed=8899705; DOI=10.1111/j.1365-2958.1996.tb02652.x;
RA Gonzalez-Gil G., Bringmann P., Kahmann R.;
RT "FIS is a regulator of metabolism in Escherichia coli.";
RL Mol. Microbiol. 22:21-29(1996).
RN [8]
RP MUTAGENESIS OF ASP-5.
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-
RT 12. I. Cloning and expression of uridine phosphorylase genes from
RT Klebsiella aerogenes and Salmonella typhimurium in E. coli.";
RL Bioorg. Khim. 24:381-387(1998).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
RX PubMed=7796917; DOI=10.1016/0014-5793(95)00489-V;
RA Morgunova E.Y., Mikhailov A.M., Popov A.N., Blagova E.V.,
RA Smirnova E.A., Vainshtein B.K., Mao C., Armstrong S.H.R., Ealick S.E.,
RA Komissarov A.A., Linkova E.V., Burlakova A.A., Mironov A.S.,
RA Debabov V.G.;
RT "Atomic structure at 2.5-A resolution of uridine phosphorylase from E.
RT coli as refined in the monoclinic crystal lattice.";
RL FEBS Lett. 367:183-187(1995).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RX PubMed=12499542;
RA Burling F.T., Kniewel R., Buglino J.A., Chadha T., Beckwith A.,
RA Lima C.D.;
RT "Structure of Escherichia coli uridine phosphorylase at 2.0 A.";
RL Acta Crystallogr. D 59:73-76(2003).
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.
CC -!- CATALYTIC ACTIVITY: Uridine + phosphate = uracil + alpha-D-ribose
CC 1-phosphate.
CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via salvage
CC pathway; uracil from uridine (phosphorylase route): step 1/1.
CC -!- SUBUNIT: Homohexamer. The homohexamer shows 4-fold, 6-fold or 8-
CC fold symmetry.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the PNP/UDP phosphorylase family.
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DR EMBL; X15689; CAA33724.1; -; Genomic_DNA.
DR EMBL; M87049; AAA67626.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76834.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77470.1; -; Genomic_DNA.
DR PIR; S05491; S05491.
DR RefSeq; NP_418275.1; NC_000913.2.
DR RefSeq; YP_491611.1; NC_007779.1.
DR PDB; 1K3F; X-ray; 2.50 A; A/B/C/D/E/F=1-253.
DR PDB; 1LX7; X-ray; 2.00 A; A/B=1-253.
DR PDB; 1RXC; X-ray; 2.35 A; A/B/C/D/E/F/G/H/I/J/K/L=1-253.
DR PDB; 1RXS; X-ray; 2.80 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/a/b/c/d/e/h/i/j/k/l/m/o=1-253.
DR PDB; 1RXU; X-ray; 3.10 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R=1-253.
DR PDB; 1RXY; X-ray; 1.70 A; A/B=1-253.
DR PDB; 1T0U; X-ray; 2.20 A; A/B=1-253.
DR PDB; 1TGV; X-ray; 2.20 A; A/B=1-253.
DR PDB; 1TGY; X-ray; 2.20 A; A/B=1-253.
DR PDB; 1U1C; X-ray; 2.20 A; A/B/C/D/E/F=2-252.
DR PDB; 1U1D; X-ray; 2.00 A; A/B/C/D/E/F=2-252.
DR PDB; 1U1E; X-ray; 2.00 A; A/B/C/D/E/F=2-252.
DR PDB; 1U1F; X-ray; 2.30 A; A/B/C/D/E/F=2-252.
DR PDB; 1U1G; X-ray; 1.95 A; A/B/C/D/E/F=2-252.
DR PDB; 3KVV; X-ray; 1.80 A; A/B/C/D/E/F=1-253.
DR PDBsum; 1K3F; -.
DR PDBsum; 1LX7; -.
DR PDBsum; 1RXC; -.
DR PDBsum; 1RXS; -.
DR PDBsum; 1RXU; -.
DR PDBsum; 1RXY; -.
DR PDBsum; 1T0U; -.
DR PDBsum; 1TGV; -.
DR PDBsum; 1TGY; -.
DR PDBsum; 1U1C; -.
DR PDBsum; 1U1D; -.
DR PDBsum; 1U1E; -.
DR PDBsum; 1U1F; -.
DR PDBsum; 1U1G; -.
DR PDBsum; 3KVV; -.
DR ProteinModelPortal; P12758; -.
DR SMR; P12758; 4-253.
DR DIP; DIP-11075N; -.
DR IntAct; P12758; 3.
DR STRING; 511145.b3831; -.
DR SWISS-2DPAGE; P12758; -.
DR PaxDb; P12758; -.
DR PRIDE; P12758; -.
DR EnsemblBacteria; AAC76834; AAC76834; b3831.
DR EnsemblBacteria; BAE77470; BAE77470; BAE77470.
DR GeneID; 12934305; -.
DR GeneID; 948987; -.
DR KEGG; ecj:Y75_p3347; -.
DR KEGG; eco:b3831; -.
DR PATRIC; 32123163; VBIEscCol129921_3947.
DR EchoBASE; EB1038; -.
DR EcoGene; EG11045; udp.
DR eggNOG; COG2820; -.
DR HOGENOM; HOG000274897; -.
DR KO; K00757; -.
DR OMA; ICVEELA; -.
DR ProtClustDB; PRK11178; -.
DR BioCyc; EcoCyc:URPHOS-MONOMER; -.
DR BioCyc; ECOL316407:JW3808-MONOMER; -.
DR BioCyc; MetaCyc:URPHOS-MONOMER; -.
DR UniPathway; UPA00574; UER00633.
DR DrugBank; DB00544; Fluorouracil.
DR EvolutionaryTrace; P12758; -.
DR Genevestigator; P12758; -.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR GO; GO:0004850; F:uridine phosphorylase activity; IEA:EC.
DR GO; GO:0009166; P:nucleotide catabolic process; IEA:InterPro.
DR GO; GO:0006974; P:response to DNA damage stimulus; IEP:EcoliWiki.
DR GO; GO:0044206; P:UMP salvage; IEA:UniProtKB-UniPathway.
DR InterPro; IPR018017; Nucleoside_phosphorylase.
DR InterPro; IPR018016; Nucleoside_phosphorylase_CS.
DR InterPro; IPR000845; Nucleoside_phosphorylase_d.
DR InterPro; IPR010058; Uridine_phosphorylase.
DR PANTHER; PTHR21234; PTHR21234; 1.
DR Pfam; PF01048; PNP_UDP_1; 1.
DR TIGRFAMs; TIGR01718; Uridine-psphlse; 1.
DR PROSITE; PS01232; PNP_UDP_1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Complete proteome; Cytoplasm; Direct protein sequencing;
KW Glycosyltransferase; Reference proteome; Transferase.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 253 Uridine phosphorylase.
FT /FTId=PRO_0000063183.
FT MUTAGEN 5 5 D->A,E,N: No change in activity.
FT CONFLICT 11 11 L -> Y (in Ref. 7; AA sequence).
FT CONFLICT 15 15 D -> Y (in Ref. 7; AA sequence).
FT STRAND 6 9
FT HELIX 13 16
FT STRAND 21 23
FT HELIX 28 30
FT HELIX 31 35
FT STRAND 38 47
FT STRAND 50 57
FT STRAND 60 65
FT HELIX 71 83
FT STRAND 88 97
FT STRAND 107 116
FT HELIX 119 122
FT HELIX 134 146
FT STRAND 151 160
FT HELIX 164 166
FT STRAND 171 173
FT HELIX 178 180
FT HELIX 183 189
FT STRAND 194 198
FT HELIX 199 207
FT TURN 208 210
FT STRAND 212 222
FT TURN 223 225
FT HELIX 231 251
SQ SEQUENCE 253 AA; 27159 MW; 7446DE45BA04D88D CRC64;
MSKSDVFHLG LTKNDLQGAT LAIVPGDPDR VEKIAALMDK PVKLASHREF TTWRAELDGK
PVIVCSTGIG GPSTSIAVEE LAQLGIRTFL RIGTTGAIQP HINVGDVLVT TASVRLDGAS
LHFAPLEFPA VADFECTTAL VEAAKSIGAT THVGVTASSD TFYPGQERYD TYSGRVVRHF
KGSMEEWQAM GVMNYEMESA TLLTMCASQG LRAGMVAGVI VNRTQQEIPN AETMKQTESH
AVKIVVEAAR RLL
//
