(data stored in ACNUC7421 zone)

SWISSPROT: UPP_HISS2

ID   UPP_HISS2               Reviewed;         208 AA.
AC   B0UW86;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   11-DEC-2019, entry version 73.
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=HSM_0281;
OS   Histophilus somni (strain 2336) (Haemophilus somnus).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Histophilus.
OX   NCBI_TaxID=228400;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2336;
RG   US DOE Joint Genome Institute;
RA   Siddaramappa S., Duncan A.J., Challacombe J.F., Rainey D., Gillaspy A.F.,
RA   Carson M., Gipson J., Gipson M., Bruce D., Detter J.C., Han C.S., Land M.,
RA   Tapia R., Thompson L.S., Orvis J., Zaitshik J., Barnes G., Brettin T.S.,
RA   Dyer D.W., Inzana T.J.;
RT   "Complete sequence of Haemophilus somnus 2336.";
RL   Submitted (FEB-2008) 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; CP000947; ACA31911.1; -; Genomic_DNA.
DR   RefSeq; WP_011609495.1; NC_010519.1.
DR   SMR; B0UW86; -.
DR   EnsemblBacteria; ACA31911; ACA31911; HSM_0281.
DR   GeneID; 31486563; -.
DR   KEGG; hsm:HSM_0281; -.
DR   HOGENOM; HOG000262754; -.
DR   KO; K00761; -.
DR   OMA; TYATRMP; -.
DR   OrthoDB; 1581906at2; -.
DR   BioCyc; HSOM228400:G1GB8-294-MONOMER; -.
DR   UniPathway; UPA00574; UER00636.
DR   Proteomes; UP000008543; 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; B0UW86.
DR   SWISS-2DPAGE; B0UW86.
KW   Allosteric enzyme; Glycosyltransferase; GTP-binding; Magnesium;
KW   Nucleotide-binding; Reference proteome; Transferase.
FT   CHAIN           1..208
FT                   /note="Uracil phosphoribosyltransferase"
FT                   /id="PRO_1000085628"
FT   REGION          130..138
FT                   /note="5-phospho-alpha-D-ribose 1-diphosphate binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01218"
FT   REGION          198..200
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         193
FT                   /note="Uracil; via amide nitrogen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01218"
FT   BINDING         199
FT                   /note="5-phospho-alpha-D-ribose 1-diphosphate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01218"
SQ   SEQUENCE   208 AA;  22578 MW;  DDA368E4E68B3E6B CRC64;
     MKIVEVKHPL VKHKLGLMRV ADITTKDFRE LATEVGSLLT YEATSDLETE KVIIDGWCGA
     VEIDRIKGKK VTVVPILRAG LGMMDGVLEH VPSARISVVG MYRDEETLEP VPYFQKLASD
     LDERLAIVVD PMLATGGSMI ATINLLKAKG CQHIKVLVLV AAPEGIKALE AVHPDVELYT
     ASIDSHLNEH GYIIPGLGDA GDKIFGTK
//

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