ID B3FN75_AERHY Unreviewed; 287 AA.
AC B3FN75;
DT 22-JUL-2008, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2008, sequence version 1.
DT 24-JAN-2024, entry version 32.
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=rmlA {ECO:0000313|EMBL:ABX39497.1};
OS Aeromonas hydrophila.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Aeromonadales;
OC Aeromonadaceae; Aeromonas.
OX NCBI_TaxID=644 {ECO:0000313|EMBL:ABX39497.1};
RN [1] {ECO:0000313|EMBL:ABX39497.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=AH-3 {ECO:0000313|EMBL:ABX39497.1};
RX PubMed=18408022; DOI=10.1128/JB.00153-08;
RA Jimenez N., Canals R., Salo M.T., Vilches S., Merino S., Tomas J.M.;
RT "The Aeromonas hydrophila wb*O34 gene cluster: genetics and temperature
RT regulation.";
RL J. Bacteriol. 190:4198-4209(2008).
RN [2] {ECO:0000313|EMBL:ABX39497.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=AH-3 {ECO:0000313|EMBL:ABX39497.1};
RA Jimenez N., Canals R., Salo M.T., Vilches S., Merino S., Tomas J.M.;
RL Submitted (OCT-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}.
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DR EMBL; EU274663; ABX39497.1; -; Genomic_DNA.
DR AlphaFoldDB; B3FN75; -.
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 Transferase {ECO:0000256|RuleBase:RU003706}.
FT DOMAIN 2..238
FT /note="Nucleotidyl transferase"
FT /evidence="ECO:0000259|Pfam:PF00483"
SQ SEQUENCE 287 AA; 32078 MW; EA9BDCCA92F83F39 CRC64;
MKGIILAGGS GSRLHPITRG ISKQLLPIYD KPMIYYPLSV LMLAGIKDIL IITTQEDSES
FQRLLGNGEQ FGINLQYTVQ PSPDGLAQAF ILGEEFIGED NVCLVLGDNI FFGQAFGKQL
QKAIDNQEGA TVFGYKVMDP ERFGVVEFDE KFRAKSIEEK PEKPKSNWAV TGLYFYDNSV
IEIAKSIKPS DRGELEITSV NQAYLERGQL KVEQLGRGFA WLDTGTHDSL IEASQFVQTV
EKRQGFKIAC LEEIAFNNGW LNREQIKTIG NSMVKTGYGQ YLLSLIK
//
