ID A1WFS1_VEREI Unreviewed; 294 AA.
AC A1WFS1;
DT 06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2007, sequence version 1.
DT 27-MAR-2024, entry version 84.
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 OrderedLocusNames=Veis_0696 {ECO:0000313|EMBL:ABM56478.1};
OS Verminephrobacter eiseniae (strain EF01-2).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Verminephrobacter.
OX NCBI_TaxID=391735 {ECO:0000313|EMBL:ABM56478.1, ECO:0000313|Proteomes:UP000000374};
RN [1] {ECO:0000313|Proteomes:UP000000374}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EF01-2 {ECO:0000313|Proteomes:UP000000374};
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T.,
RA Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Kim E., Stahl D., Richardson P.;
RT "Complete sequence of chromosome 1 of Verminephrobacter eiseniae EF01-2.";
RL Submitted (DEC-2006) 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; CP000542; ABM56478.1; -; Genomic_DNA.
DR RefSeq; WP_011808492.1; NC_008786.1.
DR AlphaFoldDB; A1WFS1; -.
DR SMR; A1WFS1; -.
DR STRING; 391735.Veis_0696; -.
DR GeneID; 76459392; -.
DR KEGG; vei:Veis_0696; -.
DR eggNOG; COG1209; Bacteria.
DR HOGENOM; CLU_029499_9_0_4; -.
DR OrthoDB; 9803871at2; -.
DR Proteomes; UP000000374; Chromosome.
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 ECO:0000313|EMBL:ABM56478.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000374};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003706}.
FT DOMAIN 5..241
FT /note="Nucleotidyl transferase"
FT /evidence="ECO:0000259|Pfam:PF00483"
SQ SEQUENCE 294 AA; 32748 MW; B1A9DC31ED947686 CRC64;
MTTRKGIILA GGSGTRLHPA TLAISKQLLP VYDKPMIYYP LSTLMLAGMR EILIISTPQD
TPRFEQLLGT GQQWGIALHY AVQPHPDGLA QAFLIGETFL GDAPSALVLG DNIFYGHDFH
ERLGRAMART EGASVFAYHV QDPERYGVVG FDAQGKAVSL QEKPSAPPSS YAVTGLYFYD
NQVVELARGL KPSQRGEYEI TDLNRRYLEQ AQLHVEIMGR GYAWLDTGTH ESLLQAGQFI
ATLEHRQGLK IACPEEIAWR QRWIDGAQLE RLAQPLCKSG YGQYLLRVLA DKIY
//