ID D8ADX4_ECOMS Unreviewed; 293 AA.
AC D8ADX4;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 24-JAN-2024, entry version 38.
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 Name=rfbA {ECO:0000313|EMBL:EFK18661.1};
GN ORFNames=HMPREF9530_04775 {ECO:0000313|EMBL:EFK18661.1};
OS Escherichia coli (strain MS 21-1).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=749527 {ECO:0000313|EMBL:EFK18661.1, ECO:0000313|Proteomes:UP000005688};
RN [1] {ECO:0000313|EMBL:EFK18661.1, ECO:0000313|Proteomes:UP000005688}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MS 21-1 {ECO:0000313|EMBL:EFK18661.1,
RC ECO:0000313|Proteomes:UP000005688};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA Chinwalla A., Mardis E.R., Wilson R.K.;
RL Submitted (JUN-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|ARBA:ARBA00037065, 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:EFK18661.1}.
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DR EMBL; ADTR01000424; EFK18661.1; -; Genomic_DNA.
DR RefSeq; WP_000676059.1; NZ_GG772760.1.
DR AlphaFoldDB; D8ADX4; -.
DR HOGENOM; CLU_029499_9_0_6; -.
DR Proteomes; UP000005688; 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:SF4; GLUCOSE-1-PHOSPHATE THYMIDYLYLTRANSFERASE 2; 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 ECO:0000313|EMBL:EFK18661.1};
KW Transferase {ECO:0000256|RuleBase:RU003706, ECO:0000313|EMBL:EFK18661.1}.
FT DOMAIN 2..238
FT /note="Nucleotidyl transferase"
FT /evidence="ECO:0000259|Pfam:PF00483"
SQ SEQUENCE 293 AA; 32707 MW; 9C6F57FCE52D1B08 CRC64;
MKGIILAGGS GTRLHPITRG VSKQLLPIYD KPMIYYPLSV LMLAGIREIL IITTPEDKGY
FQRLLGDGSE FGIQLEYAEQ PSPDGLAQAF IIGETFLNGE PSCLVLGDNI FFGQGFSPKL
RHVAARTEGA TVFGYQVMDP ERFGVVEFDD NFRAISLEEK PKQPKSNWAV TGLYFYDSKV
VEYAKQVTPS ERGELEITSI NQMYLEAGNL TVELLGRGFA WLDTGTHDSL IEASTFVQTV
EKRQGFKIAC LEEIAWRNGW LDDEGVKRAA SSLAKTGYGQ YLLELLRARP RQY
//
