(data stored in ACNUC7421 zone)

SWISSPROT: UPP_RHOOB

ID   UPP_RHOOB               Reviewed;         209 AA.
AC   C1ARF7;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   26-MAY-2009, sequence version 1.
DT   07-JUN-2017, entry version 58.
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=ROP_03870;
OS   Rhodococcus opacus (strain B4).
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae;
OC   Rhodococcus.
OX   NCBI_TaxID=632772;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B4;
RA   Takarada H., Sekine M., Hosoyama A., Yamada R., Fujisawa T., Omata S.,
RA   Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.;
RT   "Comparison of the complete genome sequences of Rhodococcus
RT   erythropolis PR4 and Rhodococcus opacus B4.";
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
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; AP011115; BAH48634.1; -; Genomic_DNA.
DR   RefSeq; WP_012687641.1; NC_012522.1.
DR   ProteinModelPortal; C1ARF7; -.
DR   SMR; C1ARF7; -.
DR   STRING; 632772.ROP_03870; -.
DR   EnsemblBacteria; BAH48634; BAH48634; ROP_03870.
DR   KEGG; rop:ROP_03870; -.
DR   PATRIC; fig|632772.20.peg.433; -.
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; UP000002212; 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; C1ARF7.
DR   SWISS-2DPAGE; C1ARF7.
KW   Allosteric enzyme; Complete proteome; Glycosyltransferase;
KW   GTP-binding; Magnesium; Nucleotide-binding; Transferase.
FT   CHAIN         1    209       Uracil phosphoribosyltransferase.
FT                                /FTId=PRO_1000164832.
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;  22928 MW;  CC0040F5BE2E03A4 CRC64;
     MGTVHLIDHP LVQHKLTMMR RKDASTNSFR RLANEISALM TYEVLRDIPM QEIEIETPLE
     VTTGRVIDGK KLVFVSILRA GTGILDGMLT IVPGARVGHI GLYRDPRTLV AVEYYFKMPG
     DLHERDVVVV DPLLATGNSA VAAVERLKEC GPKSIKFVCL LTCPEGVAAL DKAHPDVPIY
     TAAVDRQLDE HGYILPGIGD AGDRIFGTK
//

If you have problems or comments...

PBIL Back to PBIL home page