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Database: UniProt
Entry: S1RL02_9ENTE
LinkDB: S1RL02_9ENTE
Original site: S1RL02_9ENTE 
ID   S1RL02_9ENTE            Unreviewed;       289 AA.
AC   S1RL02;
DT   18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2013, sequence version 1.
DT   24-JAN-2024, entry version 35.
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=I567_02442 {ECO:0000313|EMBL:EOX17177.1}, OMO_00806
GN   {ECO:0000313|EMBL:ESK61837.1};
OS   Enterococcus cecorum DSM 20682 = ATCC 43198.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC   Enterococcus.
OX   NCBI_TaxID=1121864 {ECO:0000313|EMBL:ESK61837.1, ECO:0000313|Proteomes:UP000017415};
RN   [1] {ECO:0000313|EMBL:EOX17177.1, ECO:0000313|Proteomes:UP000014156}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43198 {ECO:0000313|EMBL:EOX17177.1,
RC   ECO:0000313|Proteomes:UP000014156};
RG   The Broad Institute Genomics Platform;
RG   The Broad Institute Genome Sequencing Center for Infectious Disease;
RA   Earl A., Russ C., Gilmore M., Surin D., Walker B., Young S., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA   Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA   Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA   Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Enterococcus cecorum ATCC_43198 (PacBio/Illumina
RT   hybrid assembly).";
RL   Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ESK61837.1, ECO:0000313|Proteomes:UP000017415}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43198 {ECO:0000313|EMBL:ESK61837.1,
RC   ECO:0000313|Proteomes:UP000017415};
RG   The Broad Institute Genomics Platform;
RG   The Broad Institute Genome Sequencing Center for Infectious Disease;
RA   Earl A., Russ C., Gilmore M., Surin D., Walker B., Young S., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA   Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA   Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA   Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Enterococcus cecorum DSM 20682 (= ATCC 43198)
RT   (Illumina assembly).";
RL   Submitted (OCT-2013) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:ESK61837.1}.
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DR   EMBL; ASWI01000006; EOX17177.1; -; Genomic_DNA.
DR   EMBL; AHYS01000004; ESK61837.1; -; Genomic_DNA.
DR   RefSeq; WP_016252488.1; NZ_KI535313.1.
DR   AlphaFoldDB; S1RL02; -.
DR   STRING; 44008.GCA_001318175_02300; -.
DR   GeneID; 60871961; -.
DR   PATRIC; fig|1121864.4.peg.2366; -.
DR   eggNOG; COG1209; Bacteria.
DR   HOGENOM; CLU_029499_9_0_9; -.
DR   OrthoDB; 9803871at2; -.
DR   Proteomes; UP000014156; Unassembled WGS sequence.
DR   Proteomes; UP000017415; 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:UP000017415};
KW   Transferase {ECO:0000256|RuleBase:RU003706, ECO:0000313|EMBL:ESK61837.1}.
FT   DOMAIN          2..238
FT                   /note="Nucleotidyl transferase"
FT                   /evidence="ECO:0000259|Pfam:PF00483"
SQ   SEQUENCE   289 AA;  32220 MW;  876B2D165BA681F5 CRC64;
     MKGIILAGGS GTRLYPLTRA TSKQLMPIYD KPMIYYPMST LMLAGIKEIL IISTPQDTPR
     FEELFGDGHE LGIHIEYAVQ PSPDGLAQAF IIGEEFIGDD SVCLVLGDNI YYGGGLSKML
     QRAASKTEGA TVFGYHVNDP ERFGVVEFDE NMTAISIEEK PEHPKSNYAV TGLYFYDNDV
     VEIAKNIKPS ARGELEITDV NKVYLERGKL SVEVMGRGFA WLDTGTHESL LEASTFIETI
     EKRQNLKVAC LEEIAYRMGY IGKEQLVELA QPLKKNQYGQ YLLRLAAQN
//
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