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Database: UniProt
Entry: A0A2J6MUU9_9BURK
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ID   A0A2J6MUU9_9BURK        Unreviewed;       301 AA.
AC   A0A2J6MUU9;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   24-JAN-2024, entry version 15.
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:PLZ03215.1};
GN   ORFNames=CY652_05190 {ECO:0000313|EMBL:PLZ03215.1};
OS   Burkholderia sp. WAC0059.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia.
OX   NCBI_TaxID=2066022 {ECO:0000313|EMBL:PLZ03215.1, ECO:0000313|Proteomes:UP000243676};
RN   [1] {ECO:0000313|EMBL:PLZ03215.1, ECO:0000313|Proteomes:UP000243676}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WAC0059 {ECO:0000313|EMBL:PLZ03215.1,
RC   ECO:0000313|Proteomes:UP000243676};
RA   Cho S.-T., Yang Y., Chen C.-L., Wang T.-F., Kuo C.-H.;
RT   "Genome Sequence of Burkholderia sp. WAC0059.";
RL   Submitted (DEC-2017) 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}.
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:PLZ03215.1}.
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DR   EMBL; PNEO01000004; PLZ03215.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2J6MUU9; -.
DR   OrthoDB; 9803871at2; -.
DR   Proteomes; UP000243676; 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: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   Reference proteome {ECO:0000313|Proteomes:UP000243676};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003706}.
FT   DOMAIN          8..244
FT                   /note="Nucleotidyl transferase"
FT                   /evidence="ECO:0000259|Pfam:PF00483"
SQ   SEQUENCE   301 AA;  33817 MW;  814AF2E7B20F7183 CRC64;
     MASKTTRKGI ILAGGSGTRL YPITHAISKQ LLPVYDKPMI YYPLSTLMLA GIRDVLIIST
     PSDTPRFEAM LGDGSQWGMN LQYAVQPSPD GLAQAFLIGR EFIGADSCAL ILGDNIFYGH
     DLALKLRQAD ERTDCATVFA YHVQDPERYG VVEFDNQLRV LSIEEKPQRP RSNYAVTGLY
     FYDNDVCDIA ADIRPSARGE LEITDINLHY LALRRLHVEV MGRGYAWLDT GTHDSLIDAA
     TFIATLQKRQ GLVVACPEEV AYRYRWIDAE QLSRLAVPLS KNSYGRYLMN LLTDEIVWQS
     Q
//
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