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Database: UniProt
Entry: E3BJ55_9VIBR
LinkDB: E3BJ55_9VIBR
Original site: E3BJ55_9VIBR 
ID   E3BJ55_9VIBR            Unreviewed;       288 AA.
AC   E3BJ55;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   24-JAN-2024, entry version 38.
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   ORFNames=VIBC2010_20225 {ECO:0000313|EMBL:EFP96981.1};
OS   Vibrio caribbeanicus ATCC BAA-2122.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=796620 {ECO:0000313|EMBL:EFP96981.1, ECO:0000313|Proteomes:UP000002943};
RN   [1] {ECO:0000313|EMBL:EFP96981.1, ECO:0000313|Proteomes:UP000002943}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-2122 {ECO:0000313|EMBL:EFP96981.1,
RC   ECO:0000313|Proteomes:UP000002943};
RX   PubMed=21930677; DOI=10.1099/ijs.0.032375-0;
RA   Hoffmann M., Monday S.R., Allard M.W., Strain E.A., Whittaker P., Naum M.,
RA   McCarthy P.J., Lopez J.V., Fischer M., Brown E.W.;
RT   "Vibrio caribbeanicus sp. nov., isolated from the marine sponge
RT   Scleritoderma cyanea.";
RL   Int. J. Syst. Evol. Microbiol. 62:1736-1743(2012).
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}.
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:EFP96981.1}.
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DR   EMBL; AEIU01000068; EFP96981.1; -; Genomic_DNA.
DR   RefSeq; WP_009601051.1; NZ_AEIU01000068.1.
DR   AlphaFoldDB; E3BJ55; -.
DR   STRING; 796620.VIBC2010_20225; -.
DR   eggNOG; COG1209; Bacteria.
DR   OrthoDB; 9803871at2; -.
DR   Proteomes; UP000002943; 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: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   Reference proteome {ECO:0000313|Proteomes:UP000002943};
KW   Transferase {ECO:0000256|RuleBase:RU003706, ECO:0000313|EMBL:EFP96981.1}.
FT   DOMAIN          2..238
FT                   /note="Nucleotidyl transferase"
FT                   /evidence="ECO:0000259|Pfam:PF00483"
SQ   SEQUENCE   288 AA;  32008 MW;  B21B4E5FFEBC5A53 CRC64;
     MKGIVLAGGS GTRLYPITRG VSKQLLPVYD KPMIYYPLST LMLAGIRDVL IITTPEDNES
     FKRLLGDGSD FGINLEYAVQ PSPDGLAQAF IIGEDFIGDD SVCLVLGDNI FYGQSFSSTL
     VNAANRGTGA TVFGYQVKDP ERFGVVEFDE NMKAISLEEK PKAPKSNYAV TGLYFYDNRV
     IEFAKQVKPS DRGELEITSL NEMYLNDGTL NVELLGRGFA WLDTGTHQSL HEASSFVQTI
     ENVQGLKVAC LEEIAWRNHW LSDKELMTLA TPMLKNEYGK YLMDLIEK
//
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