ID   A4JIV2_BURVG            Unreviewed;       294 AA.
AC   A4JIV2;
DT   01-MAY-2007, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2007, sequence version 1.
DT   27-MAR-2024, entry version 99.
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=Bcep1808_3215 {ECO:0000313|EMBL:ABO56205.1};
OS   Burkholderia vietnamiensis (strain G4 / LMG 22486) (Burkholderia cepacia
OS   (strain R1808)).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX   NCBI_TaxID=269482 {ECO:0000313|EMBL:ABO56205.1, ECO:0000313|Proteomes:UP000002287};
RN   [1] {ECO:0000313|Proteomes:UP000002287}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=G4 / LMG 22486 {ECO:0000313|Proteomes:UP000002287};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Tiedje J., Richardson P.;
RT   "Complete sequence of chromosome 1 of Burkholderia vietnamiensis G4.";
RL   Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0007829|PDB:5IDT}
RP   X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS).
RA   Dranow D.M., Hornayi P.S., Lorimer D.D., Edwards T.E.;
RT   "Crystal Structure of a Glucose-1-phosphate Thymidylyltransferase from
RT   Burkholderia vietnamiensis with bound Thymidine.";
RL   Submitted (FEB-2016) to the PDB data bank.
RN   [3] {ECO:0007829|PDB:5IDS}
RP   X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS).
RA   Dranow D.M., Hornayi P.S., Lorimer D.D., Edwards T.E.;
RT   "Crystal Structure of a Glucose-1-phosphate Thymidylyltransferase from
RT   Burkholderia vietnamiensis.";
RL   Submitted (FEB-2016) to the PDB data bank.
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; CP000614; ABO56205.1; -; Genomic_DNA.
DR   PDB; 5IDS; X-ray; 2.30 A; A/B/C/D=1-294.
DR   PDB; 5IDT; X-ray; 2.35 A; A/B/C/D=1-294.
DR   PDBsum; 5IDS; -.
DR   PDBsum; 5IDT; -.
DR   AlphaFoldDB; A4JIV2; -.
DR   SMR; A4JIV2; -.
DR   KEGG; bvi:Bcep1808_3215; -.
DR   eggNOG; COG1209; Bacteria.
DR   HOGENOM; CLU_029499_9_0_4; -.
DR   Proteomes; UP000002287; Chromosome 1.
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   1: Evidence at protein level;
KW   3D-structure {ECO:0007829|PDB:5IDS, ECO:0007829|PDB:5IDT};
KW   Magnesium {ECO:0000256|RuleBase:RU003706};
KW   Metal-binding {ECO:0000256|RuleBase:RU003706};
KW   Nucleotidyltransferase {ECO:0000256|RuleBase:RU003706,
KW   ECO:0000313|EMBL:ABO56205.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002287};
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;  32262 MW;  F889ED40F442F9AE CRC64;
     MTQRKGIILA GGSGTRLHPA TLAISKQLLP VYDKPMIYYP LSTLMLAGMR DVLVISTPQD
     TPRFQQLLGD GSQWGMNLQY AVQPSPDGLA QAFIIGEQFI GNAPSALVLG DNIYYGHDFQ
     PLLKAADAQS SGATVFAYHV HDPERYGVVQ FNAQGQAVSI EEKPKAPKSN YAVTGLYFYD
     QQVVDIAKAV KPSARGELEI TSVNQAYMQQ GQLNVQTMGR GYAWLDTGTH DSLLDASQFI
     ATLENRQGLK VACPEEIAWR SGWINASQLE ALVQPLTKNG YGQYLMQILK ETVF
//