ID A0A1F4ZEI2_9BACT Unreviewed; 243 AA.
AC A0A1F4ZEI2;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 22-FEB-2023, entry version 14.
DE RecName: Full=glucose-1-phosphate thymidylyltransferase {ECO:0000256|ARBA:ARBA00012461};
DE EC=2.7.7.24 {ECO:0000256|ARBA:ARBA00012461};
GN ORFNames=A2989_01455 {ECO:0000313|EMBL:OGD04047.1};
OS Candidatus Amesbacteria bacterium RIFCSPLOWO2_01_FULL_48_25.
OC Bacteria; Candidatus Amesbacteria.
OX NCBI_TaxID=1797259 {ECO:0000313|EMBL:OGD04047.1, ECO:0000313|Proteomes:UP000177080};
RN [1] {ECO:0000313|EMBL:OGD04047.1, ECO:0000313|Proteomes:UP000177080}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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}.
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:OGD04047.1}.
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DR EMBL; MEXN01000003; OGD04047.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F4ZEI2; -.
DR STRING; 1797259.A2989_01455; -.
DR Proteomes; UP000177080; 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 InterPro; IPR005907; G1P_thy_trans_s.
DR InterPro; IPR005835; NTP_transferase_dom.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
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 Capsid protein {ECO:0000313|EMBL:OGD04047.1};
KW Virion {ECO:0000313|EMBL:OGD04047.1}.
FT DOMAIN 2..234
FT /note="Nucleotidyl transferase"
FT /evidence="ECO:0000259|Pfam:PF00483"
SQ SEQUENCE 243 AA; 27094 MW; 71D0BBEB21C49BBC CRC64;
MKGVILAGGL GTRLYPLTYA TNKHLLPIYD EPMIYYPIRT LVRAGIREAM IVVSGPHSGQ
FISILKNGKE LGLNHLEYGY QDNPTGGLAD GLKVAEDFAE GKPITFILGD NVTDADISKS
VTSFTTGSVM FLKKVPDPER FGVPVFDKNH PKKLVGIVEK PVHPPSQYAS VGLYLFDHRC
FSVARKLKLS KRGQLEITDV QNYYIRDGSM KWEELKGYWH DVGTFDSLLA ANVYWAKEKG
LKV
//
