ID   GALU_ECOL6              Reviewed;         302 AA.
AC   P0AEP4; P25520;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   27-MAR-2024, entry version 88.
DE   RecName: Full=UTP--glucose-1-phosphate uridylyltransferase;
DE            EC=2.7.7.9;
DE   AltName: Full=Alpha-D-glucosyl-1-phosphate uridylyltransferase;
DE   AltName: Full=UDP-glucose pyrophosphorylase;
DE            Short=UDPGP;
DE   AltName: Full=Uridine diphosphoglucose pyrophosphorylase;
GN   Name=galU; OrderedLocusNames=c1700;
OS   Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=199310;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFT073 / ATCC 700928 / UPEC;
RX   PubMed=12471157; DOI=10.1073/pnas.252529799;
RA   Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA   Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA   Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA   Donnenberg M.S., Blattner F.R.;
RT   "Extensive mosaic structure revealed by the complete genome sequence of
RT   uropathogenic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
CC   -!- FUNCTION: May play a role in stationary phase survival. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=alpha-D-glucose 1-phosphate + H(+) + UTP = diphosphate + UDP-
CC         alpha-D-glucose; Xref=Rhea:RHEA:19889, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:46398, ChEBI:CHEBI:58601,
CC         ChEBI:CHEBI:58885; EC=2.7.7.9;
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC   -!- SUBUNIT: Homotetramer or homopentamer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the UDPGP type 2 family. {ECO:0000305}.
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DR   EMBL; AE014075; AAN80167.1; -; Genomic_DNA.
DR   RefSeq; WP_000718995.1; NZ_CP051263.1.
DR   AlphaFoldDB; P0AEP4; -.
DR   SMR; P0AEP4; -.
DR   STRING; 199310.c1700; -.
DR   GeneID; 75203349; -.
DR   KEGG; ecc:c1700; -.
DR   eggNOG; COG1210; Bacteria.
DR   HOGENOM; CLU_029499_1_1_6; -.
DR   BioCyc; ECOL199310:C1700-MONOMER; -.
DR   Proteomes; UP000001410; Chromosome.
DR   GO; GO:0003983; F:UTP:glucose-1-phosphate uridylyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR   GO; GO:0006011; P:UDP-glucose metabolic process; IEA:InterPro.
DR   CDD; cd02541; UGPase_prokaryotic; 1.
DR   InterPro; IPR005771; GalU_uridylyltTrfase_bac/arc.
DR   InterPro; IPR005835; NTP_transferase_dom.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   NCBIfam; TIGR01099; galU; 1.
DR   PANTHER; PTHR43197; UTP--GLUCOSE-1-PHOSPHATE URIDYLYLTRANSFERASE; 1.
DR   PANTHER; PTHR43197:SF1; UTP--GLUCOSE-1-PHOSPHATE URIDYLYLTRANSFERASE; 1.
DR   Pfam; PF00483; NTP_transferase; 1.
DR   SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
PE   3: Inferred from homology;
KW   Magnesium; Nucleotidyltransferase; Reference proteome; Transferase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..302
FT                   /note="UTP--glucose-1-phosphate uridylyltransferase"
FT                   /id="PRO_0000201356"
SQ   SEQUENCE   302 AA;  32942 MW;  ADEAEB3F6A1194CB CRC64;
     MAAINTKVKK AVIPVAGLGT RMLPATKAIP KEMLPLVDKP LIQYVVNECI AAGITEIVLV
     THSSKNSIEN HFDTSFELEA MLEKRVKRQL LDEVQSICPP HVTIMQVRQG LAKGLGHAVL
     CAHPVVGDEP VAVILPDVIL DEYESDLSQD NLAEMIRRFD ETGHSQIMVE PVADVTAYGV
     VDCKGVELAP GESVPMVGVV EKPKADVAPS NLAIVGRYVL SADIWPLLAK TPPGAGDEIQ
     LTDAIDMLIE KETVEAYHMK GKSHDCGNKL GYMQAFVEYG IRHNTLGTEF KAWLEEEMGI
     KK
//