ID G3LYK6_BURPE Unreviewed; 297 AA.
AC G3LYK6;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 13-SEP-2023, entry version 44.
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:AEO78425.1};
GN ORFNames=BURPS002025_LPSb23 {ECO:0000313|EMBL:AEO78425.1};
OS Burkholderia pseudomallei (Pseudomonas pseudomallei).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; pseudomallei group.
OX NCBI_TaxID=28450 {ECO:0000313|EMBL:AEO78425.1};
RN [1] {ECO:0000313|EMBL:AEO78425.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Smith002025 {ECO:0000313|EMBL:AEO78425.1};
RX PubMed=23126230; DOI=10.1186/1471-2180-12-250;
RA Stone J.K., Mayo M., Grasso S.A., Ginther J.L., Warrington S.D.,
RA Allender C.J., Doyle A., Georgia S., Kaestli M., Broomall S.M.,
RA Karavis M.A., Insalaco J.M., Hubbard K.S., McNew L.A., Gibbons H.S.,
RA Currie B.J., Keim P., Tuanyok A.;
RT "Detection of Burkholderia pseudomallei O-antigen serotypes in near-
RT neighbor species.";
RL BMC Microbiol. 12:250-250(2012).
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; JN581996; AEO78425.1; -; Genomic_DNA.
DR RefSeq; WP_004544180.1; NZ_UVEZ01000006.1.
DR AlphaFoldDB; G3LYK6; -.
DR PATRIC; fig|28450.142.peg.6032; -.
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|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003706}.
FT DOMAIN 4..240
FT /note="Nucleotidyl transferase"
FT /evidence="ECO:0000259|Pfam:PF00483"
SQ SEQUENCE 297 AA; 32899 MW; BAF20B55169EB81F CRC64;
MARKGIILAG GSGTRLYPIT HAVSKQLLPV YDKPMIYYPL STLMVADIRD VLIISTPQDT
PRFEAMLGDG SQWGMNIRYA VQPSPDGLAQ AFVIGREFVG RDPSTLILGD NIFYGHDLAK
QLDRASARQA GATVFAYHVH DPERYGVVEF DGEFRALSIE EKPAKPRSNY AVTGLYFYDN
QVCDIAADIK PSARGELEIT DVNSRYLAAG ALNVEIMGRG YAWLDTGTHD SLIDAATFIA
TLQKRQGLVV ACPEEIAYRR QWIDAEQVLK LAQPLAKNGY GQYLKHILTD QVAWPSK
//
