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Database: UniProt
Entry: B7IM50_BACC2
LinkDB: B7IM50_BACC2
Original site: B7IM50_BACC2 
ID   B7IM50_BACC2            Unreviewed;       245 AA.
AC   B7IM50;
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=glucose-1-phosphate thymidylyltransferase {ECO:0000256|ARBA:ARBA00012461};
DE            EC=2.7.7.24 {ECO:0000256|ARBA:ARBA00012461};
GN   OrderedLocusNames=BCG9842_B4074 {ECO:0000313|EMBL:ACK95068.1};
OS   Bacillus cereus (strain G9842).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=405531 {ECO:0000313|EMBL:ACK95068.1, ECO:0000313|Proteomes:UP000006744};
RN   [1] {ECO:0000313|EMBL:ACK95068.1, ECO:0000313|Proteomes:UP000006744}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=G9842 {ECO:0000313|EMBL:ACK95068.1,
RC   ECO:0000313|Proteomes:UP000006744};
RA   Dodson R.J., Durkin A.S., Rosovitz M.J., Rasko D.A., Hoffmaster A.,
RA   Ravel J., Sutton G.;
RT   "Genome sequence of Bacillus cereus G9842.";
RL   Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=alpha-D-glucose 1-phosphate + dTTP + H(+) = diphosphate +
CC         dTDP-alpha-D-glucose; Xref=Rhea:RHEA:15225, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:37568, ChEBI:CHEBI:57477,
CC         ChEBI:CHEBI:58601; EC=2.7.7.24;
CC         Evidence={ECO:0000256|ARBA:ARBA00001095};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- SIMILARITY: Belongs to the glucose-1-phosphate thymidylyltransferase
CC       family. {ECO:0000256|ARBA:ARBA00010480}.
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DR   EMBL; CP001186; ACK95068.1; -; Genomic_DNA.
DR   RefSeq; WP_000676159.1; NC_011772.1.
DR   AlphaFoldDB; B7IM50; -.
DR   KEGG; bcg:BCG9842_B4074; -.
DR   HOGENOM; CLU_029499_9_0_9; -.
DR   Proteomes; UP000006744; Chromosome.
DR   GO; GO:0008879; F:glucose-1-phosphate thymidylyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0045226; P:extracellular polysaccharide biosynthetic process; IEA:InterPro.
DR   InterPro; IPR005907; G1P_thy_trans_s.
DR   InterPro; IPR005835; NTP_transferase_dom.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   PANTHER; PTHR43532; GLUCOSE-1-PHOSPHATE THYMIDYLYLTRANSFERASE; 1.
DR   PANTHER; PTHR43532:SF1; GLUCOSE-1-PHOSPHATE THYMIDYLYLTRANSFERASE 1; 1.
DR   Pfam; PF00483; NTP_transferase; 1.
DR   SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
PE   3: Inferred from homology;
KW   Transferase {ECO:0000313|EMBL:ACK95068.1}.
FT   DOMAIN          2..231
FT                   /note="Nucleotidyl transferase"
FT                   /evidence="ECO:0000259|Pfam:PF00483"
SQ   SEQUENCE   245 AA;  27435 MW;  7DA68FFABA6E0F0D CRC64;
     MKGIILAGGT GSRLYPITKV TNKHLLPVGR YPMIYHAVYK LKQCDITDIM IITGKEHMGD
     VVSFLGSGHE FGVSFTYRVQ DKAGGIAQAL GLCEDFVGND RMVVILGDNI FSDDILPYVE
     EFANQKEGAK VLLQSVEDPE RFGVAHIQNR KIVEIEEKPK EPKSSYAVTG IYLYDSKVFS
     YIKELKPSAR GELEITDINN WYLKRGVLTY NEMSGWWTDA GTHASLQKAN TLARDIDFGK
     QFNGE
//
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