ID   GALU_HAEDU              Reviewed;         295 AA.
AC   Q9F664;
DT   14-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   25-MAY-2022, entry version 98.
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=HD_1431;
OS   Haemophilus ducreyi (strain 35000HP / ATCC 700724).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=233412;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Sun S., Gibson B.W., Campagnari A.A., Munson R.S. Jr.;
RT   "Haemophilus ducreyi strain Hd9 strain produces a truncated
RT   lipooligosaccharide due to a mutation in UDP-glucose pyrophosphorylase
RT   (galU).";
RL   Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=35000HP / ATCC 700724;
RA   Munson R.S. Jr., Ray W.C., Mahairas G., Sabo P., Mungur R., Johnson L.,
RA   Nguyen D., Wang J., Forst C., Hood L.;
RT   "The complete genome sequence of Haemophilus ducreyi.";
RL   Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
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   -!- SIMILARITY: Belongs to the UDPGP type 2 family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AF297520; AAG23691.1; -; Genomic_DNA.
DR   EMBL; AE017143; AAP96237.1; -; Genomic_DNA.
DR   RefSeq; WP_010945286.1; NC_002940.2.
DR   AlphaFoldDB; Q9F664; -.
DR   SMR; Q9F664; -.
DR   STRING; 233412.HD_1431; -.
DR   PRIDE; Q9F664; -.
DR   EnsemblBacteria; AAP96237; AAP96237; HD_1431.
DR   KEGG; hdu:HD_1431; -.
DR   eggNOG; COG1210; Bacteria.
DR   HOGENOM; CLU_029499_1_2_6; -.
DR   OMA; FSATIWD; -.
DR   Proteomes; UP000001022; 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   Gene3D; 3.90.550.10; -; 1.
DR   InterPro; IPR005771; GalU_uridylyltTrfase_bac/arc.
DR   InterPro; IPR005835; NTP_transferase_dom.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   PANTHER; PTHR43197; PTHR43197; 1.
DR   Pfam; PF00483; NTP_transferase; 1.
DR   SUPFAM; SSF53448; SSF53448; 1.
DR   TIGRFAMs; TIGR01099; galU; 1.
PE   3: Inferred from homology;
KW   Nucleotidyltransferase; Reference proteome; Transferase.
FT   CHAIN           1..295
FT                   /note="UTP--glucose-1-phosphate uridylyltransferase"
FT                   /id="PRO_0000201357"
SQ   SEQUENCE   295 AA;  32518 MW;  025974C0752115CC CRC64;
     MKVIIPVAGL GTRMLPATKA IPKEMLTIAD KPLIQYIVNE CVAAGIKEIV FVTHSSKNAI
     ENHFDTSFEL ETMLEKRVKR QLLDEVRSIV PNDVTLMHVR QGQAKGLGHA VLCGKAVVGK
     EPFAVVLPDV ILADFTANPK TENLAAMIKR FSETQCSQIM VAPVPQEDVS NYGIVDCATD
     NIRAGETAKI AKMVEKPSIE NAPSNLAIVG RYVFSATIWD LLERTPVGVG DEIQLTDAID
     MLIEKETVEA FHMTGRAFDC GDKLGYMEAF VEYSLRHEKC GQQFQKIIKE LAKSL