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Database: UniProt
Entry: A0A1G1M3N7_9BACT
LinkDB: A0A1G1M3N7_9BACT
Original site: A0A1G1M3N7_9BACT 
ID   A0A1G1M3N7_9BACT        Unreviewed;       242 AA.
AC   A0A1G1M3N7;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   13-SEP-2023, entry version 15.
DE   RecName: Full=glucose-1-phosphate thymidylyltransferase {ECO:0000256|ARBA:ARBA00012461};
DE            EC=2.7.7.24 {ECO:0000256|ARBA:ARBA00012461};
GN   ORFNames=A2Y42_01830 {ECO:0000313|EMBL:OGX12025.1};
OS   Omnitrophica WOR_2 bacterium GWB2_45_9.
OC   Bacteria; Candidatus Omnitrophota.
OX   NCBI_TaxID=1801843 {ECO:0000313|EMBL:OGX12025.1, ECO:0000313|Proteomes:UP000180191};
RN   [1] {ECO:0000313|EMBL:OGX12025.1, ECO:0000313|Proteomes:UP000180191}
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:OGX12025.1}.
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DR   EMBL; MHGB01000002; OGX12025.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G1M3N7; -.
DR   Proteomes; UP000180191; 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:OGX12025.1};
KW   Virion {ECO:0000313|EMBL:OGX12025.1}.
FT   DOMAIN          5..232
FT                   /note="Nucleotidyl transferase"
FT                   /evidence="ECO:0000259|Pfam:PF00483"
SQ   SEQUENCE   242 AA;  27226 MW;  B3E3E7864F1C78A6 CRC64;
     MSGLKGVILA GGLGKRLEPL TRITNKHLLP IYNKPMVYYP LETLVEAGIK DIMIVTGGNN
     AGDFLRLIGN GQEFGLRHIN YTYQRGEGGI AEALRLAEHF VDGSKVVVIL GDNLIGCSIK
     KYVEKFLKQE KGARVLLKEV KDPERFGVAE IKDGKILSIE EKPKSKYAVT GIYMYDYRVF
     DIAKTLKPSE RGELEITDVN NFYLKRGELY YDTLSGWWTD CGLPETLYRA ATLARRKALN
     DK
//
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