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Database: UniProt
Entry: D7JCU0_9BACT
LinkDB: D7JCU0_9BACT
Original site: D7JCU0_9BACT 
ID   D7JCU0_9BACT            Unreviewed;       287 AA.
AC   D7JCU0;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   24-JAN-2024, entry version 42.
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=HMPREF0156_00555 {ECO:0000313|EMBL:EFI16967.1};
OS   Bacteroidetes oral taxon 274 str. F0058.
OC   Bacteria; Bacteroidota.
OX   NCBI_TaxID=575590 {ECO:0000313|EMBL:EFI16967.1, ECO:0000313|Proteomes:UP000004685};
RN   [1] {ECO:0000313|Proteomes:UP000004685}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F0058 {ECO:0000313|Proteomes:UP000004685};
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., Izard J., Baranova O.V., Blanton J.M., Tanner A.C.,
RA   Dewhirst F.E., Haas B., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Bacteroidetes bacterium Oral taxon 274 strain
RT   F0058.";
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; GG774889; EFI16967.1; -; Genomic_DNA.
DR   AlphaFoldDB; D7JCU0; -.
DR   STRING; 575590.HMPREF0156_00555; -.
DR   eggNOG; COG1209; Bacteria.
DR   HOGENOM; CLU_029499_9_0_10; -.
DR   OrthoDB; 9803871at2; -.
DR   Proteomes; UP000004685; 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   Reference proteome {ECO:0000313|Proteomes:UP000004685};
KW   Transferase {ECO:0000256|RuleBase:RU003706, ECO:0000313|EMBL:EFI16967.1}.
FT   DOMAIN          2..238
FT                   /note="Nucleotidyl transferase"
FT                   /evidence="ECO:0000259|Pfam:PF00483"
SQ   SEQUENCE   287 AA;  31735 MW;  C417874E6A8A5220 CRC64;
     MKGIILAGGS ATRLFPLSKA ISKQIMPVYD KPMIYYPLST LMLAGICEVL IISTPRDLPM
     FEELLGSGQE LGMKFEYIVQ EVPNGLAQAF VLGADFLNGE GGCLILGDNL FYGQNFSAML
     RRASAIGQGA CIFGYFVKDP RAYGVVEFAP DGKVLSLEEK PAKPKSNFAV PGLYFYDNTV
     VQKAKSLKPS ARGEYEITDL NRLYLEEGSL QVETFGRGFT WLDTGNCDSL LDASNFVATI
     QNRQGFYIAC IEEIAWRNGW ISDSDLNALG RKLDKTEYGR YILELSK
//
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