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Database: UniProt
Entry: A0A0N0M1F4_9GAMM
LinkDB: A0A0N0M1F4_9GAMM
Original site: A0A0N0M1F4_9GAMM 
ID   A0A0N0M1F4_9GAMM        Unreviewed;       299 AA.
AC   A0A0N0M1F4;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   24-JAN-2024, entry version 22.
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=ADS77_02430 {ECO:0000313|EMBL:KPH65148.1};
OS   Pseudoalteromonas porphyrae.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=187330 {ECO:0000313|EMBL:KPH65148.1, ECO:0000313|Proteomes:UP000037848};
RN   [1] {ECO:0000313|EMBL:KPH65148.1, ECO:0000313|Proteomes:UP000037848}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCD-SED14 {ECO:0000313|EMBL:KPH65148.1,
RC   ECO:0000313|Proteomes:UP000037848};
RA   Coil D.A., Jospin G., Lee R.D., Eisen J.A.;
RT   "Draft Genome Sequence of Pseudoalteromonas porphyrae UCD-SED14.";
RL   Submitted (AUG-2015) 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|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:KPH65148.1}.
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DR   EMBL; LHPH01000002; KPH65148.1; -; Genomic_DNA.
DR   RefSeq; WP_054452787.1; NZ_LHPH01000002.1.
DR   AlphaFoldDB; A0A0N0M1F4; -.
DR   PATRIC; fig|187330.3.peg.523; -.
DR   OrthoDB; 9803871at2; -.
DR   Proteomes; UP000037848; 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   Transferase {ECO:0000256|RuleBase:RU003706, ECO:0000313|EMBL:KPH65148.1}.
FT   DOMAIN          2..241
FT                   /note="Nucleotidyl transferase"
FT                   /evidence="ECO:0000259|Pfam:PF00483"
SQ   SEQUENCE   299 AA;  33339 MW;  F6D48B3AD5699E44 CRC64;
     MKGIILAGGS GTRLYPITMG VSKQLLPIYD KPMVYYPLSV LMLAGIREVL IITTPEDIDS
     FKRLLGDGSQ FGIELSYTVQ PSPDGLAQAF ILGEEFIGKD DVCLVLGDNI FYGQGFTTKL
     KHAVNNAKNG NGSTVFGYQV KDPERFGVVE FNKDKKAISI EEKPTNPKSH FAVTGLYFYD
     NSVVELAKKV EPSHRGELEI TCLNEMYLKQ NKLNVEILGR GFTWLDTGTH ESLLEAAQFV
     ETIERCQGYK IACLEEVAFN NSWLSPEQVK ELATPLLKNG YGQYLLHLIK DEKTLEIPN
//
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