ID D7J2H2_9BACE Unreviewed; 295 AA.
AC D7J2H2;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE RecName: Full=Glucose-1-phosphate thymidylyltransferase {ECO:0000256|ARBA:ARBA00012461, ECO:0000256|RuleBase:RU003706};
DE EC=2.7.7.24 {ECO:0000256|ARBA:ARBA00012461, ECO:0000256|RuleBase:RU003706};
GN ORFNames=HMPREF0106_01627 {ECO:0000313|EMBL:EFI14326.1};
OS Bacteroides sp. D22.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=585544 {ECO:0000313|EMBL:EFI14326.1, ECO:0000313|Proteomes:UP000003817};
RN [1] {ECO:0000313|EMBL:EFI14326.1, ECO:0000313|Proteomes:UP000003817}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D22 {ECO:0000313|EMBL:EFI14326.1,
RC ECO:0000313|Proteomes:UP000003817};
RG The Broad Institute Genome Sequencing Platform;
RA Ward D., Earl A., Feldgarden M., Gevers D., Young S.K., Zeng Q.,
RA Koehrsen M., Alvarado L., Berlin A., Bochicchio J., Borenstein D.,
RA Chapman S.B., Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J.,
RA Griggs A., Gujja S., Heilman E., Heiman D., Hepburn T., Howarth C., Jen D.,
RA Larson L., Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T.,
RA Shenoy N., Sisk P., Stolte C., Sykes S., Thomson T., Walk T., White J.,
RA Yandava C., Strauss J., Sibley C., White A., Ambrose C.E., Allen-Vercoe E.,
RA Haas B., Nusbaum C., Birren B.;
RT "The Genome Sequence of Bacteroides sp. strain D22.";
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the formation of dTDP-glucose, from dTTP and
CC glucose 1-phosphate, as well as its pyrophosphorolysis.
CC {ECO:0000256|RuleBase:RU003706}.
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 ECO:0000256|RuleBase:RU003706};
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, ECO:0000256|RuleBase:RU003706}.
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DR EMBL; GG774801; EFI14326.1; -; Genomic_DNA.
DR RefSeq; WP_009039542.1; NZ_GG774801.1.
DR AlphaFoldDB; D7J2H2; -.
DR HOGENOM; CLU_029499_9_0_10; -.
DR Proteomes; UP000003817; Unassembled WGS sequence.
DR GO; GO:0008879; F:glucose-1-phosphate thymidylyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0045226; P:extracellular polysaccharide biosynthetic process; IEA:InterPro.
DR CDD; cd02538; G1P_TT_short; 1.
DR InterPro; IPR005907; G1P_thy_trans_s.
DR InterPro; IPR005835; NTP_transferase_dom.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR NCBIfam; TIGR01207; rmlA; 1.
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 Magnesium {ECO:0000256|RuleBase:RU003706};
KW Metal-binding {ECO:0000256|RuleBase:RU003706};
KW Nucleotidyltransferase {ECO:0000256|RuleBase:RU003706};
KW Transferase {ECO:0000256|RuleBase:RU003706, ECO:0000313|EMBL:EFI14326.1}.
FT DOMAIN 2..241
FT /note="Nucleotidyl transferase"
FT /evidence="ECO:0000259|Pfam:PF00483"
SQ SEQUENCE 295 AA; 32884 MW; 9994E03AB6DAC770 CRC64;
MKGIVLAGGS GTRLYPITKG VSKQLLPIFD KPMIYYPISV LMLAGIREVL IISTPYDLPG
FKRLLGDGSD YGVRFEYAEQ PSPDGLAQAF IIGEDFIGND SVCLVLGDNI FYGQSFTHML
QEAVRTVEEE QKATVFGYWV ADPERYGVAD FDKDGNVLSI EEKPANPKSN YAVVGLYFYP
NKVVDVAKHI QPSPRGELEI TTVNQEFLND HQLKVQLLGR GFAWLDTGTH DSLSEASTFI
EVIEKRQGLK VACLEGIALR HGWITADKMR ELAKPMLKNQ YGQYLLKVIN ELGLE
//
