ID A0A0E4HE54_9BACL Unreviewed; 313 AA.
AC A0A0E4HE54;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 24-JAN-2024, entry version 28.
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 Name=rmlA3 {ECO:0000313|EMBL:CQR58552.1};
GN ORFNames=PRIO_6205 {ECO:0000313|EMBL:CQR58552.1};
OS Paenibacillus riograndensis SBR5.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus;
OC Paenibacillus sonchi group.
OX NCBI_TaxID=1073571 {ECO:0000313|EMBL:CQR58552.1, ECO:0000313|Proteomes:UP000033163};
RN [1] {ECO:0000313|Proteomes:UP000033163}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Wibberg D.;
RL Submitted (MAR-2015) 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}.
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DR EMBL; LN831776; CQR58552.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0E4HE54; -.
DR KEGG; pri:PRIO_6205; -.
DR PATRIC; fig|1073571.4.peg.6628; -.
DR HOGENOM; CLU_029499_9_0_9; -.
DR Proteomes; UP000033163; Chromosome I.
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:CQR58552.1};
KW Transferase {ECO:0000256|RuleBase:RU003706, ECO:0000313|EMBL:CQR58552.1}.
FT DOMAIN 23..259
FT /note="Nucleotidyl transferase"
FT /evidence="ECO:0000259|Pfam:PF00483"
SQ SEQUENCE 313 AA; 34759 MW; 8D84BAD4B24361AE CRC64;
MNTQEITLFK IHMEQGELKT VMKGIILAGG SGTRLYPLTM VTSKQLLPVY DKPMIYYPLS
TLMLAGIKEI LIISTAEDTP RFKNLLGDGS QFGISLQYIV QPNPDGLAQA FILGESFIGE
DSVAMILGDN IYYGNGMTKI LKEAARKKRG ATVFGYHVPD PERFGVIEFD GEGKVLSVEE
KPEHPKSNYA VTGLYFYDNR VVSLAKEVKP SRRGELEITS INEAYLKLGE LDVALLGRGF
TWLDTGTHQS LVDATNFVRT IEDHQGIKIS APEEIAYING WITKEHLLEC GHKLSKTGYG
QYLIKVATGK IQF
//
