(data stored in ACNUC7421 zone)

SWISSPROT: UPP_RHOJR

ID   UPP_RHOJR               Reviewed;         209 AA.
AC   Q0SK44;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   07-JUN-2017, entry version 82.
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};
GN   OrderedLocusNames=RHA1_ro00256;
OS   Rhodococcus jostii (strain RHA1).
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae;
OC   Rhodococcus.
OX   NCBI_TaxID=101510;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RHA1;
RX   PubMed=17030794; DOI=10.1073/pnas.0607048103;
RA   McLeod M.P., Warren R.L., Hsiao W.W.L., Araki N., Myhre M.,
RA   Fernandes C., Miyazawa D., Wong W., Lillquist A.L., Wang D.,
RA   Dosanjh M., Hara H., Petrescu A., Morin R.D., Yang G., Stott J.M.,
RA   Schein J.E., Shin H., Smailus D., Siddiqui A.S., Marra M.A.,
RA   Jones S.J.M., Holt R., Brinkman F.S.L., Miyauchi K., Fukuda M.,
RA   Davies J.E., Mohn W.W., Eltis L.D.;
RT   "The complete genome of Rhodococcus sp. RHA1 provides insights into a
RT   catabolic powerhouse.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15582-15587(2006).
CC   -!- FUNCTION: Catalyzes the conversion of uracil and 5-phospho-alpha-
CC       D-ribose 1-diphosphate (PRPP) to UMP and diphosphate.
CC       {ECO:0000255|HAMAP-Rule:MF_01218}.
CC   -!- CATALYTIC ACTIVITY: UMP + diphosphate = uracil + 5-phospho-alpha-
CC       D-ribose 1-diphosphate. {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-
CC       PRPP. {ECO:0000255|HAMAP-Rule:MF_01218};
CC   -!- ENZYME REGULATION: Allosterically activated by GTP.
CC       {ECO:0000255|HAMAP-Rule:MF_01218}.
CC   -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via salvage
CC       pathway; UMP from uracil: step 1/1. {ECO:0000255|HAMAP-
CC       Rule:MF_01218}.
CC   -!- SIMILARITY: Belongs to the UPRTase family. {ECO:0000255|HAMAP-
CC       Rule:MF_01218}.
DR   EMBL; CP000431; ABG92092.1; -; Genomic_DNA.
DR   RefSeq; WP_009472812.1; NC_008268.1.
DR   ProteinModelPortal; Q0SK44; -.
DR   SMR; Q0SK44; -.
DR   STRING; 101510.RHA1_ro00256; -.
DR   PRIDE; Q0SK44; -.
DR   EnsemblBacteria; ABG92092; ABG92092; RHA1_ro00256.
DR   GeneID; 4217948; -.
DR   KEGG; rha:RHA1_ro00256; -.
DR   eggNOG; ENOG4105CZ5; Bacteria.
DR   eggNOG; COG0035; LUCA.
DR   HOGENOM; HOG000262754; -.
DR   KO; K00761; -.
DR   OMA; VVYAKFP; -.
DR   OrthoDB; POG091H02GN; -.
DR   UniPathway; UPA00574; UER00636.
DR   Proteomes; UP000008710; Chromosome.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004845; F:uracil phosphoribosyltransferase activity; IEA:UniProtKB-EC.
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   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   PANTHER; PTHR10285:SF104; PTHR10285:SF104; 1.
DR   SUPFAM; SSF53271; SSF53271; 1.
DR   TIGRFAMs; TIGR01091; upp; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q0SK44.
DR   SWISS-2DPAGE; Q0SK44.
KW   Allosteric enzyme; Complete proteome; Glycosyltransferase;
KW   GTP-binding; Magnesium; Nucleotide-binding; Reference proteome;
KW   Transferase.
FT   CHAIN         1    209       Uracil phosphoribosyltransferase.
FT                                /FTId=PRO_1000053773.
FT   REGION      131    139       5-phospho-alpha-D-ribose 1-diphosphate
FT                                binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_01218}.
FT   REGION      199    201       Uracil binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_01218}.
FT   BINDING      79     79       5-phospho-alpha-D-ribose 1-diphosphate.
FT                                {ECO:0000255|HAMAP-Rule:MF_01218}.
FT   BINDING     104    104       5-phospho-alpha-D-ribose 1-diphosphate.
FT                                {ECO:0000255|HAMAP-Rule:MF_01218}.
FT   BINDING     194    194       Uracil; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01218}.
FT   BINDING     200    200       5-phospho-alpha-D-ribose 1-diphosphate.
FT                                {ECO:0000255|HAMAP-Rule:MF_01218}.
SQ   SEQUENCE   209 AA;  22895 MW;  EAA07EE9BB64D49B CRC64;
     MGTVHVIEHP LVQHKLTMMR RKDASTNSFR RLANEISALM TYEVLRDIPM QEIDVETPLE
     FTTGKVIDGK KLVFVSILRA GTGILDGMLT IVPGARVGHI GLYRDPKTLG AVEYYFKMPG
     DLQERDVVVI DPMLATGNSA VAAVERLKEC GPKSIKFVCL LTCPEGVAAL HKAHPDVPIY
     TAAVDRQLDE HGYILPGIGD AGDRLFGTK
//

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