(data stored in ACNUC30630 zone)

SWISSPROT: UPP_BIFAA

ID   UPP_BIFAA               Reviewed;         213 AA.
AC   A0ZZM2;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   11-DEC-2019, entry version 84.
DE   RecName: Full=Uracil phosphoribosyltransferase {ECO:0000255|HAMAP-Rule:MF_01218};
DE            EC=2.4.2.9 {ECO:0000255|HAMAP-Rule:MF_01218};
DE   AltName: Full=UMP pyrophosphorylase {ECO:0000255|HAMAP-Rule:MF_01218};
DE   AltName: Full=UPRTase {ECO:0000255|HAMAP-Rule:MF_01218};
GN   Name=upp {ECO:0000255|HAMAP-Rule:MF_01218}; OrderedLocusNames=BAD_0124;
OS   Bifidobacterium adolescentis (strain ATCC 15703 / DSM 20083 / NCTC 11814 /
OS   E194a).
OC   Bacteria; Actinobacteria; Bifidobacteriales; Bifidobacteriaceae;
OC   Bifidobacterium.
OX   NCBI_TaxID=367928;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15703 / DSM 20083 / NCTC 11814 / E194a;
RA   Suzuki T., Tsuda Y., Kanou N., Inoue T., Kumazaki K., Nagano S., Hirai S.,
RA   Tanaka K., Watanabe K.;
RT   "Bifidobacterium adolescentis complete genome sequence.";
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the conversion of uracil and 5-phospho-alpha-D-
CC       ribose 1-diphosphate (PRPP) to UMP and diphosphate. {ECO:0000255|HAMAP-
CC       Rule:MF_01218}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=diphosphate + UMP = 5-phospho-alpha-D-ribose 1-diphosphate +
CC         uracil; Xref=Rhea:RHEA:13017, ChEBI:CHEBI:17568, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:57865, ChEBI:CHEBI:58017; EC=2.4.2.9;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01218};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01218};
CC       Note=Binds 1 Mg(2+) ion per subunit. The magnesium is bound as Mg-PRPP.
CC       {ECO:0000255|HAMAP-Rule:MF_01218};
CC   -!- ACTIVITY REGULATION: Allosterically activated by GTP.
CC       {ECO:0000255|HAMAP-Rule:MF_01218}.
CC   -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via salvage pathway;
CC       UMP from uracil: step 1/1. {ECO:0000255|HAMAP-Rule:MF_01218}.
CC   -!- SIMILARITY: Belongs to the UPRTase family. {ECO:0000255|HAMAP-
CC       Rule:MF_01218}.
DR   EMBL; AP009256; BAF38905.1; -; Genomic_DNA.
DR   RefSeq; WP_003807463.1; NC_008618.1.
DR   SMR; A0ZZM2; -.
DR   PRIDE; A0ZZM2; -.
DR   EnsemblBacteria; BAF38905; BAF38905; BAD_0124.
DR   GeneID; 4556737; -.
DR   KEGG; bad:BAD_0124; -.
DR   eggNOG; ENOG4105CZ5; Bacteria.
DR   eggNOG; COG0035; LUCA.
DR   HOGENOM; HOG000262754; -.
DR   KO; K00761; -.
DR   OMA; TYATRMP; -.
DR   BioCyc; BADO367928:G1G2R-138-MONOMER; -.
DR   UniPathway; UPA00574; UER00636.
DR   Proteomes; UP000008702; Chromosome.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004845; F:uracil phosphoribosyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0009116; P:nucleoside metabolic process; IEA:InterPro.
DR   GO; GO:0044206; P:UMP salvage; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006223; P:uracil salvage; IEA:InterPro.
DR   CDD; cd06223; PRTases_typeI; 1.
DR   Gene3D; 3.40.50.2020; -; 1.
DR   HAMAP; MF_01218_B; Upp_B; 1.
DR   InterPro; IPR000836; PRibTrfase_dom.
DR   InterPro; IPR029057; PRTase-like.
DR   InterPro; IPR034332; Upp_B.
DR   InterPro; IPR005765; Ura_phspho_trans.
DR   SUPFAM; SSF53271; SSF53271; 1.
DR   TIGRFAMs; TIGR01091; upp; 1.
PE   3: Inferred from homology;
DR   PRODOM; A0ZZM2.
DR   SWISS-2DPAGE; A0ZZM2.
KW   Allosteric enzyme; Glycosyltransferase; GTP-binding; Magnesium;
KW   Nucleotide-binding; Reference proteome; Transferase.
FT   CHAIN           1..213
FT                   /note="Uracil phosphoribosyltransferase"
FT                   /id="PRO_1000053678"
FT   REGION          131..139
FT                   /note="5-phospho-alpha-D-ribose 1-diphosphate binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01218"
FT   REGION          202..204
FT                   /note="Uracil binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01218"
FT   BINDING         78
FT                   /note="5-phospho-alpha-D-ribose 1-diphosphate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01218"
FT   BINDING         103
FT                   /note="5-phospho-alpha-D-ribose 1-diphosphate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01218"
FT   BINDING         197
FT                   /note="Uracil; via amide nitrogen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01218"
FT   BINDING         203
FT                   /note="5-phospho-alpha-D-ribose 1-diphosphate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01218"
SQ   SEQUENCE   213 AA;  23218 MW;  49A53843EF7DA7B7 CRC64;
     MDIHVLNHPL VDHKLTVLRD KNTPSSTFRE LVSELVMLEA YEATRDIEVV DKPIETPVAP
     MIGKHIAAPA PIIVPVLRAG LGMLDGMTKM IPSAEVGFLG MKRDEENPTQ QITYANRLPE
     DLTGRQCFLI DPMLATGGTL VAATHYLAER GAKDITAVCI LGAPEGLKFV EENLDPSIKF
     KLVLCAVDEK LNDKCYIVPG LGDAGDRLYG VID
//

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