ID A0A133Y9V3_9BACT Unreviewed; 298 AA.
AC A0A133Y9V3;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, 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=HMPREF1870_01818 {ECO:0000313|EMBL:KXB39993.1};
OS Bacteroidales bacterium KA00344.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales.
OX NCBI_TaxID=1497954 {ECO:0000313|EMBL:KXB39993.1, ECO:0000313|Proteomes:UP000070254};
RN [1] {ECO:0000313|Proteomes:UP000070254}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KA00344 {ECO:0000313|Proteomes:UP000070254};
RA Mitreva M., Pepin K.H., Mihindukulasuriya K.A., Fulton R., Fronick C.,
RA O'Laughlin M., Miner T., Herter B., Rosa B.A., Cordes M., Tomlinson C.,
RA Wollam A., Palsikar V.B., Mardis E.R., Wilson R.K.;
RL Submitted (JAN-2016) 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:KXB39993.1}.
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DR EMBL; LSCT01000158; KXB39993.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A133Y9V3; -.
DR STRING; 1497954.HMPREF1870_01818; -.
DR PATRIC; fig|1497954.3.peg.1846; -.
DR OrthoDB; 9803871at2; -.
DR Proteomes; UP000070254; 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:UP000070254};
KW Transferase {ECO:0000256|RuleBase:RU003706, ECO:0000313|EMBL:KXB39993.1}.
FT DOMAIN 2..241
FT /note="Nucleotidyl transferase"
FT /evidence="ECO:0000259|Pfam:PF00483"
SQ SEQUENCE 298 AA; 33136 MW; D1630FE1C20DE7B2 CRC64;
MKGIVLAGGS GTRLYPITKG ISKQLIPIFD KPMIYYPVSV LMLAGIRDIL IISTPHDLPG
FKRLLGDGHE LGVRFEYAEQ PSPDGLAQAF IIGEKFIGND SVCLVLGDNI FHGAGFTRLL
QESVDTAVYE DGATVFGYYV NDPERYGVAE FDSDGNCLSI EEKPEKPKSN YAVVGLYFYP
NSVVDIAKHI KPSDRGELEI TTVNQEYLAR EALKVQTLPR GFAWLDTGTH DSLSEASTFI
EVIEKRQGLK IACLEEIAYT QGWISREQLI EDATPMAKNE YGKYLLRLAE EEKIDNNI
//
