(data stored in ACNUC7421 zone)

SWISSPROT: B8ICB9_METNO

ID   B8ICB9_METNO            Unreviewed;       220 AA.
AC   B8ICB9;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   07-JUN-2017, entry version 70.
DE   RecName: Full=Uracil phosphoribosyltransferase {ECO:0000256|HAMAP-Rule:MF_01218, ECO:0000256|SAAS:SAAS00709136};
DE            EC=2.4.2.9 {ECO:0000256|HAMAP-Rule:MF_01218, ECO:0000256|SAAS:SAAS00766734};
DE   AltName: Full=UMP pyrophosphorylase {ECO:0000256|HAMAP-Rule:MF_01218};
DE   AltName: Full=UPRTase {ECO:0000256|HAMAP-Rule:MF_01218};
GN   Name=upp {ECO:0000256|HAMAP-Rule:MF_01218};
GN   OrderedLocusNames=Mnod_0465 {ECO:0000313|EMBL:ACL55507.1};
OS   Methylobacterium nodulans (strain LMG 21967 / CNCM I-2342 / ORS 2060).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Methylobacteriaceae; Methylobacterium.
OX   NCBI_TaxID=460265 {ECO:0000313|EMBL:ACL55507.1, ECO:0000313|Proteomes:UP000008207};
RN   [1] {ECO:0000313|EMBL:ACL55507.1, ECO:0000313|Proteomes:UP000008207}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 21967 / CNCM I-2342 / ORS 2060
RC   {ECO:0000313|Proteomes:UP000008207};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T.,
RA   Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Ivanova N., Marx C.J., Richardson P.;
RT   "Complete sequence of chromosome of Methylobacterium nodulans ORS
RT   2060.";
RL   Submitted (JAN-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:0000256|HAMAP-Rule:MF_01218, ECO:0000256|SAAS:SAAS00709092}.
CC   -!- CATALYTIC ACTIVITY: UMP + diphosphate = uracil + 5-phospho-alpha-
CC       D-ribose 1-diphosphate. {ECO:0000256|HAMAP-Rule:MF_01218,
CC       ECO:0000256|SAAS:SAAS00766714}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01218};
CC       Note=Binds 1 Mg(2+) ion per subunit. The magnesium is bound as Mg-
CC       PRPP. {ECO:0000256|HAMAP-Rule:MF_01218};
CC   -!- ENZYME REGULATION: Allosterically activated by GTP.
CC       {ECO:0000256|HAMAP-Rule:MF_01218}.
CC   -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via salvage
CC       pathway; UMP from uracil: step 1/1. {ECO:0000256|HAMAP-
CC       Rule:MF_01218, ECO:0000256|SAAS:SAAS00766740}.
CC   -!- SIMILARITY: Belongs to the UPRTase family. {ECO:0000256|HAMAP-
CC       Rule:MF_01218, ECO:0000256|SAAS:SAAS00766750}.
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DR   EMBL; CP001349; ACL55507.1; -; Genomic_DNA.
DR   RefSeq; WP_015927218.1; NC_011894.1.
DR   ProteinModelPortal; B8ICB9; -.
DR   STRING; 460265.Mnod_0465; -.
DR   EnsemblBacteria; ACL55507; ACL55507; Mnod_0465.
DR   KEGG; mno:Mnod_0465; -.
DR   eggNOG; ENOG4105CZ5; Bacteria.
DR   eggNOG; COG0035; LUCA.
DR   HOGENOM; HOG000262754; -.
DR   KO; K00761; -.
DR   OMA; RICGYEI; -.
DR   OrthoDB; POG091H02GN; -.
DR   UniPathway; UPA00574; UER00636.
DR   Proteomes; UP000008207; Chromosome.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0004845; F:uracil phosphoribosyltransferase activity; IEA:UniProtKB-HAMAP.
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; B8ICB9.
DR   SWISS-2DPAGE; B8ICB9.
KW   Allosteric enzyme {ECO:0000256|HAMAP-Rule:MF_01218};
KW   Complete proteome {ECO:0000313|Proteomes:UP000008207};
KW   Glycosyltransferase {ECO:0000256|HAMAP-Rule:MF_01218,
KW   ECO:0000256|SAAS:SAAS00766747, ECO:0000313|EMBL:ACL55507.1};
KW   GTP-binding {ECO:0000256|HAMAP-Rule:MF_01218,
KW   ECO:0000256|SAAS:SAAS00766729};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_01218,
KW   ECO:0000256|SAAS:SAAS00709102};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01218,
KW   ECO:0000256|SAAS:SAAS00766721};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008207};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01218,
KW   ECO:0000256|SAAS:SAAS00766742, ECO:0000313|EMBL:ACL55507.1}.
FT   REGION      142    150       5-phospho-alpha-D-ribose 1-diphosphate
FT                                binding. {ECO:0000256|HAMAP-Rule:
FT                                MF_01218}.
FT   REGION      210    212       Uracil binding. {ECO:0000256|HAMAP-Rule:
FT                                MF_01218}.
FT   BINDING      90     90       5-phospho-alpha-D-ribose 1-diphosphate.
FT                                {ECO:0000256|HAMAP-Rule:MF_01218}.
FT   BINDING     115    115       5-phospho-alpha-D-ribose 1-diphosphate.
FT                                {ECO:0000256|HAMAP-Rule:MF_01218}.
FT   BINDING     205    205       Uracil; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01218}.
FT   BINDING     211    211       5-phospho-alpha-D-ribose 1-diphosphate.
FT                                {ECO:0000256|HAMAP-Rule:MF_01218}.
SQ   SEQUENCE   220 AA;  23755 MW;  493266CFEDB1910C CRC64;
     MQGASTRETT GAAPVTVVSH PLVQHKLTLM RDKARSTKGF RQLLNEIGTL LAYEVTRDLP
     LEPIEVETPL VTMQGVQIAG KKLVLAPILR AGIGFLDGML SLVPSARVAH VGLYRDPDSL
     QAVEYYFKAP SDLADRTVLV LDPMLATANS AIAAVDRLKE RGARDLRIVC LIAAPEGLAK
     FRGAHPDVPV WTAAIDSHLD EHGYIIPGLG DAGDRMYGTR
//

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