ID   F9YVV3_CAPCC            Unreviewed;       290 AA.
AC   F9YVV3;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   27-MAR-2024, entry version 52.
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=Ccan_23410 {ECO:0000313|EMBL:AEK24456.1};
OS   Capnocytophaga canimorsus (strain 5).
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Capnocytophaga.
OX   NCBI_TaxID=860228 {ECO:0000313|EMBL:AEK24456.1, ECO:0000313|Proteomes:UP000008895};
RN   [1] {ECO:0000313|EMBL:AEK24456.1, ECO:0000313|Proteomes:UP000008895}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=5 {ECO:0000313|Proteomes:UP000008895};
RX   PubMed=21914877; DOI=10.1128/JB.05853-11;
RA   Manfredi P., Pagni M., Cornelis G.R.;
RT   "Complete genome sequence of the dog commensal and human pathogen
RT   Capnocytophaga canimorsus strain 5.";
RL   J. Bacteriol. 193:5558-5559(2011).
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; CP002113; AEK24456.1; -; Genomic_DNA.
DR   RefSeq; WP_013998433.1; NC_015846.1.
DR   AlphaFoldDB; F9YVV3; -.
DR   STRING; 860228.Ccan_23410; -.
DR   KEGG; ccm:Ccan_23410; -.
DR   eggNOG; COG1209; Bacteria.
DR   HOGENOM; CLU_029499_9_0_10; -.
DR   OrthoDB; 9803871at2; -.
DR   Proteomes; UP000008895; Chromosome.
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   ECO:0000313|EMBL:AEK24456.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008895};
KW   Transferase {ECO:0000256|RuleBase:RU003706, ECO:0000313|EMBL:AEK24456.1}.
FT   DOMAIN          2..241
FT                   /note="Nucleotidyl transferase"
FT                   /evidence="ECO:0000259|Pfam:PF00483"
SQ   SEQUENCE   290 AA;  32392 MW;  C52D7F7F29AC38D1 CRC64;
     MKGIILAGGS GTRLYPITKG ISKQLLPIYD KPMIYYPLSV LMLAGIREVL VISTPQDLPG
     FQRLLGDGSD YGISISYAEQ PSPDGLAQAF IIGEQFIGND DVCLVLGDNI FYGQSFTKML
     LQSVETAEKE RKATVFGYYV KDPERYGVAE FDAEGNVLSI EEKPEKPKSH YAVVGLYFYP
     NKVVNVAKNI KPSARGELEI TTVNQEFLKD NELKVQLLGR GFAWLDTGTH DSLSEASNFV
     ETIEKRQGLK ISCLEEIAYQ RGWISAEKIR ELAQPMLKNQ YGQYLINLLK
//