ID A0A1M4YJL9_9BACE Unreviewed; 289 AA.
AC A0A1M4YJL9;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 18.
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=SAMN05444349_110122 {ECO:0000313|EMBL:SHF05586.1};
OS Bacteroides faecichinchillae.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=871325 {ECO:0000313|EMBL:SHF05586.1, ECO:0000313|Proteomes:UP000184436};
RN [1] {ECO:0000313|EMBL:SHF05586.1, ECO:0000313|Proteomes:UP000184436}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 26883 {ECO:0000313|EMBL:SHF05586.1,
RC ECO:0000313|Proteomes:UP000184436};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-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}.
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DR EMBL; FQVD01000010; SHF05586.1; -; Genomic_DNA.
DR RefSeq; WP_025074552.1; NZ_SSTN01000014.1.
DR AlphaFoldDB; A0A1M4YJL9; -.
DR STRING; 871325.SAMN05444349_110122; -.
DR OrthoDB; 9803871at2; -.
DR Proteomes; UP000184436; 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:UP000184436};
KW Transferase {ECO:0000256|RuleBase:RU003706, ECO:0000313|EMBL:SHF05586.1}.
FT DOMAIN 2..238
FT /note="Nucleotidyl transferase"
FT /evidence="ECO:0000259|Pfam:PF00483"
SQ SEQUENCE 289 AA; 32156 MW; 55B41A29967F4DF0 CRC64;
MKGIILAGGS ATRLYPLSKA ISKQIMPVYD KPMIYYPLST LMLAGIREVL IISTPRDLPM
FRDLLGTGEE LGMSFSYKIQ EKPNGLAQAF VLGADFLNGE PGCLILGDNM FYGQGFSAML
RRAASITKGA CIFGYYVKDP RAYGVVEFDE QGKVMSLEEK PVHPKSNYAV PGLYFYDATV
TAKAAALRPS ARGEYEITDL NRLYLEEGTL KVELFGRGFA WLDTGNCDSL LEASNFVATI
QNRQGFYVSC IEEIAWRQGW ISSEQLFVLG QQLEKTEYGK YLIELAKQS
//
