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Database: UniProt
Entry: P12758
LinkDB: P12758
Original site: P12758 
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   09-JUL-2014, entry version 146.
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 277:1453-1462(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_000913.3.
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=2-253.
DR   PDB; 1U1D; X-ray; 2.00 A; A/B/C/D/E/F=2-253.
DR   PDB; 1U1E; X-ray; 2.00 A; A/B/C/D/E/F=2-253.
DR   PDB; 1U1F; X-ray; 2.30 A; A/B/C/D/E/F=2-253.
DR   PDB; 1U1G; X-ray; 1.95 A; A/B/C/D/E/F=2-253.
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; 4.
DR   MINT; MINT-6478293; -.
DR   STRING; 511145.b3831; -.
DR   DrugBank; DB00544; Fluorouracil.
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; NVMNFEM; -.
DR   OrthoDB; EOG676Z3T; -.
DR   PhylomeDB; P12758; -.
DR   BioCyc; EcoCyc:URPHOS-MONOMER; -.
DR   BioCyc; ECOL316407:JW3808-MONOMER; -.
DR   BioCyc; MetaCyc:URPHOS-MONOMER; -.
DR   UniPathway; UPA00574; UER00633.
DR   EvolutionaryTrace; P12758; -.
DR   PRO; PR:P12758; -.
DR   Genevestigator; P12758; -.
DR   GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR   GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR   GO; GO:0042802; F:identical protein binding; IDA:EcoCyc.
DR   GO; GO:0004850; F:uridine phosphorylase activity; IDA:EcoCyc.
DR   GO; GO:0006974; P:cellular response to DNA damage stimulus; IEP:EcoliWiki.
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; 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   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; 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
//
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