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Database: UniProt
Entry: B2TQA1_CLOBB
LinkDB: B2TQA1_CLOBB
Original site: B2TQA1_CLOBB 
ID   B2TQA1_CLOBB            Unreviewed;       290 AA.
AC   B2TQA1; U4PCB6;
DT   01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT   01-JUL-2008, sequence version 1.
DT   24-JAN-2024, entry version 78.
DE   RecName: Full=UTP--glucose-1-phosphate uridylyltransferase {ECO:0000256|ARBA:ARBA00012415, 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   Name=galU {ECO:0000313|EMBL:ACD25126.1};
GN   OrderedLocusNames=CLL_A3172 {ECO:0000313|EMBL:ACD25126.1};
OS   Clostridium botulinum (strain Eklund 17B / Type B).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=935198 {ECO:0000313|EMBL:ACD25126.1, ECO:0000313|Proteomes:UP000001195};
RN   [1] {ECO:0000313|Proteomes:UP000001195}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Eklund 17B / Type B {ECO:0000313|Proteomes:UP000001195};
RA   Brinkac L.M., Brown J.L., Bruce D., Detter C., Munk C., Smith L.A.,
RA   Smith T.J., Sutton G., Brettin T.S.;
RT   "Complete sequence of Clostridium botulinum strain Eklund.";
RL   Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
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; CP001056; ACD25126.1; -; Genomic_DNA.
DR   AlphaFoldDB; B2TQA1; -.
DR   KEGG; cbk:CLL_A3172; -.
DR   PATRIC; fig|935198.13.peg.3137; -.
DR   HOGENOM; CLU_029499_1_2_9; -.
DR   OMA; KRYDVGN; -.
DR   Proteomes; UP000001195; 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   Nucleotidyltransferase {ECO:0000256|RuleBase:RU361259,
KW   ECO:0000313|EMBL:ACD25126.1};
KW   Transferase {ECO:0000256|RuleBase:RU361259, ECO:0000313|EMBL:ACD25126.1}.
FT   DOMAIN          5..265
FT                   /note="Nucleotidyl transferase"
FT                   /evidence="ECO:0000259|Pfam:PF00483"
SQ   SEQUENCE   290 AA;  32669 MW;  C629CE4D68A9831D CRC64;
     MKVKKAIIPA AGLGTRFLPA TKAQPKEMLP IVDKPTIQYI IEEAVASGIE EILIITGRNK
     KCIEDHFDKS IELEFELEKS GKEELLELVR NISDMVDIHY IRQKEPKGLG HAIHCAKTFV
     GNEPFAVLLG DDVVDSEKPC LKQLIDCFSE YNTTILGVQT VAQENVSKYG IVDGLHIEDR
     VYKVKDLVEK PSVEEAPSNV AILGRYIITP EIFNILENTK PGKGGEIQLT DALKTLISKE
     AMYAYNFEGR RYDVGDKLGF LQATVEFALK REELREPFIE YLKGNPWDEK
//
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