(data stored in SCRATCH zone)

SWISSPROT: A8FQF1_SHESH

ID   A8FQF1_SHESH            Unreviewed;       252 AA.
AC   A8FQF1;
DT   13-NOV-2007, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2007, sequence version 1.
DT   07-JUN-2017, entry version 65.
DE   RecName: Full=Uridine phosphorylase {ECO:0000256|RuleBase:RU361131};
DE            EC=2.4.2.3 {ECO:0000256|RuleBase:RU361131};
GN   OrderedLocusNames=Ssed_0461 {ECO:0000313|EMBL:ABV35074.1};
OS   Shewanella sediminis (strain HAW-EB3).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=425104 {ECO:0000313|EMBL:ABV35074.1, ECO:0000313|Proteomes:UP000002015};
RN   [1] {ECO:0000313|EMBL:ABV35074.1, ECO:0000313|Proteomes:UP000002015}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HAW-EB3 {ECO:0000313|EMBL:ABV35074.1,
RC   ECO:0000313|Proteomes:UP000002015};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T.,
RA   Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D.,
RA   Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Kim E., Zhao J.-S., Richardson P.;
RT   "Complete sequence of Shewanella sediminis HAW-EB3.";
RL   Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases.
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: Uridine + phosphate = uracil + alpha-D-ribose
CC       1-phosphate. {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:SAAS00675091}.
CC   -!- SIMILARITY: Belongs to the PNP/UDP phosphorylase family.
CC       {ECO:0000256|RuleBase:RU361131, ECO:0000256|SAAS:SAAS00675087}.
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DR   EMBL; CP000821; ABV35074.1; -; Genomic_DNA.
DR   RefSeq; WP_012140811.1; NC_009831.1.
DR   ProteinModelPortal; A8FQF1; -.
DR   STRING; 425104.Ssed_0461; -.
DR   EnsemblBacteria; ABV35074; ABV35074; Ssed_0461.
DR   KEGG; sse:Ssed_0461; -.
DR   eggNOG; ENOG4108I5U; Bacteria.
DR   eggNOG; COG2820; LUCA.
DR   HOGENOM; HOG000274897; -.
DR   KO; K00757; -.
DR   OMA; MSDVFHL; -.
DR   OrthoDB; POG091H05D0; -.
DR   BioCyc; SSED425104:GH7Q-483-MONOMER; -.
DR   UniPathway; UPA00574; UER00633.
DR   Proteomes; UP000002015; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0004850; F:uridine phosphorylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009166; P:nucleotide catabolic process; IEA:InterPro.
DR   GO; GO:0044206; P:UMP salvage; IEA:UniProtKB-UniPathway.
DR   InterPro; IPR018016; Nucleoside_phosphorylase_CS.
DR   InterPro; IPR000845; Nucleoside_phosphorylase_d.
DR   InterPro; IPR010058; Uridine_phosphorylase.
DR   PANTHER; PTHR43691:SF6; PTHR43691:SF6; 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; A8FQF1.
DR   SWISS-2DPAGE; A8FQF1.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002015};
KW   Glycosyltransferase {ECO:0000256|RuleBase:RU361131,
KW   ECO:0000256|SAAS:SAAS00675086};
KW   Transferase {ECO:0000256|RuleBase:RU361131,
KW   ECO:0000256|SAAS:SAAS00675084}.
FT   DOMAIN       19    232       PNP_UDP_1. {ECO:0000259|Pfam:PF01048}.
SQ   SEQUENCE   252 AA;  27049 MW;  6B5279918BEA5579 CRC64;
     MSDVFHLGLT KKMLDGANLA IVPGDPERVK RIAELMEGAT FLASHREYTS YLAYIDGKAV
     VVCSTGIGGP STSIAVEELA QLGVTTFLRV GTTGAIQPQV NVGDVIVTQA SVRLDGASLH
     FAPMEYPAVA NFECTTAMVE ATRDAGLEPH IGITASSDTF YPGQDRYDTV SGRVTRQYRG
     MMQEWQDLGV LNYEMESSTL FTMCASQGWR AACVAGVIVN RTQQEIPDEA TMKKTEVSAV
     SIVVAAAKKL LA
//

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