ID Q9KUW4_VIBCH Unreviewed; 291 AA.
AC Q9KUW4;
DT 01-OCT-2000, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2000, sequence version 1.
DT 24-JAN-2024, entry version 95.
DE RecName: Full=UTP--glucose-1-phosphate uridylyltransferase {ECO:0000256|ARBA:ARBA00019048, ECO:0000256|RuleBase:RU361259};
DE EC=2.7.7.9 {ECO:0000256|ARBA:ARBA00012415, ECO:0000256|RuleBase:RU361259};
DE AltName: Full=UDP-glucose pyrophosphorylase {ECO:0000256|RuleBase:RU361259};
GN OrderedLocusNames=VC_0395 {ECO:0000313|EMBL:AAF93568.1};
OS Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=243277 {ECO:0000313|EMBL:AAF93568.1, ECO:0000313|Proteomes:UP000000584};
RN [1] {ECO:0000313|EMBL:AAF93568.1, ECO:0000313|Proteomes:UP000000584}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39315 / El Tor Inaba N16961
RC {ECO:0000313|Proteomes:UP000000584};
RX PubMed=10952301; DOI=10.1038/35020000;
RA Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA Nelson K.E., Read T.D., Tettelin H., Richardson D., Ermolaeva M.D.,
RA Vamathevan J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.,
RA Utterback T., Fleishmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT cholerae.";
RL Nature 406:477-483(2000).
CC -!- FUNCTION: May play a role in stationary phase survival.
CC {ECO:0000256|ARBA:ARBA00037294}.
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 ECO:0000256|RuleBase:RU361259};
CC -!- SIMILARITY: Belongs to the UDPGP type 2 family.
CC {ECO:0000256|ARBA:ARBA00006890, ECO:0000256|RuleBase:RU361259}.
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DR EMBL; AE003852; AAF93568.1; -; Genomic_DNA.
DR PIR; H82325; H82325.
DR RefSeq; NP_230049.1; NC_002505.1.
DR AlphaFoldDB; Q9KUW4; -.
DR STRING; 243277.VC_0395; -.
DR DNASU; 2614992; -.
DR EnsemblBacteria; AAF93568; AAF93568; VC_0395.
DR KEGG; vch:VC_0395; -.
DR PATRIC; fig|243277.26.peg.370; -.
DR eggNOG; COG1210; Bacteria.
DR HOGENOM; CLU_029499_1_2_6; -.
DR OMA; MHYVRQG; -.
DR Proteomes; UP000000584; Chromosome 1.
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 Nucleotidyltransferase {ECO:0000256|RuleBase:RU361259,
KW ECO:0000313|EMBL:AAF93568.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000584};
KW Transferase {ECO:0000256|RuleBase:RU361259}.
FT DOMAIN 10..268
FT /note="Nucleotidyl transferase"
FT /evidence="ECO:0000259|Pfam:PF00483"
SQ SEQUENCE 291 AA; 32466 MW; 9535AB752138ACE0 CRC64;
MMIKKCLFPA AGYGTRFLPA TKSMPKEMMP VVNKPLIEYG VDEAIQAGIT GMCIVTGRGK
HSIMDHFDMN YELEHQIRGT NKEELLGDIR KIIESANFTF IRQREMKGLG HAILTGKELV
GDEPFAVVLA DDLCVNEEQG VLAQMVALYK QFRCSIVAVQ EVPENETHKY GVIAGEMIKD
DLFRVDNMVE KPEPGTAPSN LAIIGRYILT PDIFDLIEQT EPGKGGEIQI TDALLKQAKA
GCVLAYKFKG KRFDCGSVEG YIEATNFCYE NMYKKNDQKV ELAKKSTHKG Q
//