ID   F4PFK7_BATDJ            Unreviewed;       300 AA.
AC   F4PFK7;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   RecName: Full=glucose-1-phosphate thymidylyltransferase {ECO:0000256|ARBA:ARBA00012461};
DE            EC=2.7.7.24 {ECO:0000256|ARBA:ARBA00012461};
GN   ORFNames=BATDEDRAFT_15109 {ECO:0000313|EMBL:EGF75991.1};
OS   Batrachochytrium dendrobatidis (strain JAM81 / FGSC 10211) (Frog chytrid
OS   fungus).
OC   Eukaryota; Fungi; Fungi incertae sedis; Chytridiomycota;
OC   Chytridiomycota incertae sedis; Chytridiomycetes; Rhizophydiales;
OC   Rhizophydiales incertae sedis; Batrachochytrium.
OX   NCBI_TaxID=684364 {ECO:0000313|EMBL:EGF75991.1, ECO:0000313|Proteomes:UP000007241};
RN   [1] {ECO:0000313|EMBL:EGF75991.1, ECO:0000313|Proteomes:UP000007241}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JAM81 / FGSC 10211 {ECO:0000313|Proteomes:UP000007241};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Kuo A., Salamov A., Schmutz J., Lucas S., Pitluck S., Rosenblum E.,
RA   Stajich J., Eisen M., Grigoriev I.V.;
RT   "The draft genome of Batrachochytrium dendrobatidis.";
RL   Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases.
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   -!- 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}.
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DR   EMBL; GL882938; EGF75991.1; -; Genomic_DNA.
DR   RefSeq; XP_006683390.1; XM_006683327.1.
DR   AlphaFoldDB; F4PFK7; -.
DR   STRING; 684364.F4PFK7; -.
DR   GeneID; 18237020; -.
DR   HOGENOM; CLU_029499_9_0_1; -.
DR   InParanoid; F4PFK7; -.
DR   OMA; PHDAEQF; -.
DR   OrthoDB; 5473612at2759; -.
DR   Proteomes; UP000007241; Unassembled WGS sequence.
DR   GO; GO:0008879; F:glucose-1-phosphate thymidylyltransferase activity; IEA:UniProtKB-EC.
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   Reference proteome {ECO:0000313|Proteomes:UP000007241}.
FT   DOMAIN          2..238
FT                   /note="Nucleotidyl transferase"
FT                   /evidence="ECO:0000259|Pfam:PF00483"
SQ   SEQUENCE   300 AA;  33788 MW;  02F33C1981F8A231 CRC64;
     MKGIILAGGS GTRLYPLTRS ISKQLLPVYD KPMIYYPLSV LMLAGIKEIL IISTPIDVPR
     FEQLLGDGSE LGIHLSYAIQ EEPNGLAEAF IIGEGFIGND EVALILGDNI FYGHEFISHL
     ERVRRQLKGA TIFGYNVNDP ERFGVVEFDE NRKVLSIEEK PKTPKSNFAI TGLYFFDNQV
     IDIAKSVNPS IRGELEITDI LKEYVVRDQL KVELLGRGFA WLDTGTHESL LEASQFIEII
     EKRTLLKVAC LEEIAYNKGY ISETKLLELA EPLKKSEYGR YILKIADMNK SREAEAVLIE
//