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Database: UniProt
Entry: B7NC76_ECOLU
LinkDB: B7NC76_ECOLU
Original site: B7NC76_ECOLU 
ID   B7NC76_ECOLU            Unreviewed;       297 AA.
AC   B7NC76;
DT   10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT   10-FEB-2009, sequence version 1.
DT   27-MAR-2024, entry version 62.
DE   RecName: Full=UTP--glucose-1-phosphate uridylyltransferase {ECO:0000256|ARBA:ARBA00019048};
DE            EC=2.7.7.9 {ECO:0000256|ARBA:ARBA00012415};
DE   AltName: Full=Alpha-D-glucosyl-1-phosphate uridylyltransferase {ECO:0000256|ARBA:ARBA00031455};
DE   AltName: Full=UDP-glucose pyrophosphorylase {ECO:0000256|ARBA:ARBA00031959};
DE   AltName: Full=Uridine diphosphoglucose pyrophosphorylase {ECO:0000256|ARBA:ARBA00032341};
GN   Name=galF {ECO:0000313|EMBL:CAR13566.1};
GN   OrderedLocusNames=ECUMN_2378 {ECO:0000313|EMBL:CAR13566.1};
OS   Escherichia coli O17:K52:H18 (strain UMN026 / ExPEC).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585056 {ECO:0000313|EMBL:CAR13566.1, ECO:0000313|Proteomes:UP000007097};
RN   [1] {ECO:0000313|Proteomes:UP000007097}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UMN026 / ExPEC {ECO:0000313|Proteomes:UP000007097};
RX   PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA   Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA   Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H.,
RA   Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.,
RA   Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C.,
RA   Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S.,
RA   Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J.,
RA   Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT   "Organised genome dynamics in the Escherichia coli species results in
RT   highly diverse adaptive paths.";
RL   PLoS Genet. 5:E1000344-E1000344(2009).
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         Evidence={ECO:0000256|ARBA:ARBA00000872};
CC   -!- PATHWAY: Carbohydrate metabolism; nucleotide-sugar metabolism.
CC       {ECO:0000256|ARBA:ARBA00005136}.
CC   -!- SIMILARITY: Belongs to the UDPGP type 2 family.
CC       {ECO:0000256|ARBA:ARBA00006890}.
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DR   EMBL; CU928163; CAR13566.1; -; Genomic_DNA.
DR   RefSeq; WP_000183065.1; NC_011751.1.
DR   RefSeq; YP_002413094.1; NC_011751.1.
DR   AlphaFoldDB; B7NC76; -.
DR   STRING; 585056.ECUMN_2378; -.
DR   KEGG; eum:ECUMN_2378; -.
DR   PATRIC; fig|585056.7.peg.2559; -.
DR   HOGENOM; CLU_029499_1_1_6; -.
DR   UniPathway; UPA00215; -.
DR   Proteomes; UP000007097; Chromosome.
DR   GO; GO:0030234; F:enzyme regulator activity; IEA:InterPro.
DR   GO; GO:0003983; F:UTP:glucose-1-phosphate uridylyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009103; P:lipopolysaccharide biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0006011; P:UDP-glucose metabolic process; IEA:InterPro.
DR   CDD; cd02541; UGPase_prokaryotic; 1.
DR   InterPro; IPR005774; GalF.
DR   InterPro; IPR005771; GalU_uridylyltTrfase_bac/arc.
DR   InterPro; IPR005835; NTP_transferase_dom.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   NCBIfam; TIGR01105; galF; 1.
DR   PANTHER; PTHR43197; UTP--GLUCOSE-1-PHOSPHATE URIDYLYLTRANSFERASE; 1.
DR   PANTHER; PTHR43197:SF2; 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   Lipopolysaccharide biosynthesis {ECO:0000256|ARBA:ARBA00022985}.
FT   DOMAIN          5..276
FT                   /note="Nucleotidyl transferase"
FT                   /evidence="ECO:0000259|Pfam:PF00483"
SQ   SEQUENCE   297 AA;  32855 MW;  DB9816BB07D5C5B5 CRC64;
     MTNLKAVIPV AGLGMHMLPA TKAIPKEMLP IVDKPMIQYI VDEIVAAGIK EILLVTHASK
     NAVENHFDTS YELESLLEQR VKRQLLAEVQ SICPPGVTIM NVRQGEPLGL GHSILCARPA
     IGDNPFVVVL PDVVIDDASA DPLRYNLAAM IARFNETGRS QVLAKRMPGD LSEYSVIQTK
     EPLDREGKVS RIVEFIEKPD QPQTLDSDIM AVGRYVLSAD IWPELERTQP GAWGRIQLTD
     AIAELAKKQS VDAMLMTGDS YDCGKKMGYM QAFVKYGLRN LKEGPKFRKS IEKLLGE
//
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