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Database: UniProt
Entry: A0A398CFW7_9BACL
LinkDB: A0A398CFW7_9BACL
Original site: A0A398CFW7_9BACL 
ID   A0A398CFW7_9BACL        Unreviewed;       247 AA.
AC   A0A398CFW7;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   24-JAN-2024, 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=D3H35_15100 {ECO:0000313|EMBL:RIE02086.1};
OS   Cohnella faecalis.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Cohnella.
OX   NCBI_TaxID=2315694 {ECO:0000313|EMBL:RIE02086.1, ECO:0000313|Proteomes:UP000266340};
RN   [1] {ECO:0000313|EMBL:RIE02086.1, ECO:0000313|Proteomes:UP000266340}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K2E09-144 {ECO:0000313|EMBL:RIE02086.1,
RC   ECO:0000313|Proteomes:UP000266340};
RA   Zhu H.;
RT   "Cohnella cavernae sp. nov., isolated from a karst cave.";
RL   Submitted (SEP-2018) 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}.
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:RIE02086.1}.
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DR   EMBL; QXJM01000039; RIE02086.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A398CFW7; -.
DR   OrthoDB; 9803871at2; -.
DR   Proteomes; UP000266340; 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:RIE02086.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000266340};
KW   Virion {ECO:0000313|EMBL:RIE02086.1}.
FT   DOMAIN          2..233
FT                   /note="Nucleotidyl transferase"
FT                   /evidence="ECO:0000259|Pfam:PF00483"
SQ   SEQUENCE   247 AA;  26963 MW;  31D19E229331DB27 CRC64;
     MKGIILAGGT GSRLFPLTKV TNKHLLPVGK YPMIFHAVFK LKQAGIQDIL IVTGKEHMGD
     VVNLLGSGKE MGVSFTYKVQ DEAGGIAEAL GLAEQFVGAE PMVVVLGDNV FSDDISGYLT
     NFKKQRSGAK ILIQEVADPQ RYGVPELHGD RIVSIEEKPA IPKSNFAVTG IYMYDNSVFE
     IIKNLRPSGR GELEITDVNN AYIASNQLSY DILVGWWTDA GTHASWAKAN ELAQDIVYGE
     EFGKIKE
//
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