ID E8RMN2_ASTEC Unreviewed; 290 AA.
AC E8RMN2;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 27-MAR-2024, entry version 53.
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 OrderedLocusNames=Astex_2258 {ECO:0000313|EMBL:ADU13913.1};
OS Asticcacaulis excentricus (strain ATCC 15261 / DSM 4724 / KCTC 12464 /
OS NCIMB 9791 / VKM B-1370 / CB 48).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Asticcacaulis.
OX NCBI_TaxID=573065 {ECO:0000313|EMBL:ADU13913.1, ECO:0000313|Proteomes:UP000001492};
RN [1] {ECO:0000313|Proteomes:UP000001492}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15261 / DSM 4724 / KCTC 12464 / NCIMB 9791 / VKM B-1370 /
RC CB 48 {ECO:0000313|Proteomes:UP000001492};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Teshima H., Davenport K., Detter J.C., Han C., Tapia R.,
RA Land M., Hauser L., Jeffries C., Kyrpides N., Ivanova N., Ovchinnikova G.,
RA Brun Y.V., Woyke T.;
RT "Complete sequence of chromosome 1 of Asticcacaulis excentricus CB 48.";
RL Submitted (DEC-2010) 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; CP002395; ADU13913.1; -; Genomic_DNA.
DR RefSeq; WP_013479741.1; NC_014816.1.
DR AlphaFoldDB; E8RMN2; -.
DR STRING; 573065.Astex_2258; -.
DR KEGG; aex:Astex_2258; -.
DR eggNOG; COG1209; Bacteria.
DR HOGENOM; CLU_029499_9_0_5; -.
DR OrthoDB; 9803871at2; -.
DR Proteomes; UP000001492; Chromosome 1.
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:UP000001492};
KW Transferase {ECO:0000256|RuleBase:RU003706, ECO:0000313|EMBL:ADU13913.1}.
FT DOMAIN 2..237
FT /note="Nucleotidyl transferase"
FT /evidence="ECO:0000259|Pfam:PF00483"
SQ SEQUENCE 290 AA; 32006 MW; 2BE3AC3D7D17CBC6 CRC64;
MKGIILAGGS GTRLHPMTIG VSKQMMPVYD KPMIYYPLST LMMAGIREIL IISTPHDLPL
FKKLLGDGQK WGIELSYAEQ PSPDGLAQAY MIGADFVGRA PSCLILGDNI YYGSNLSETL
EGSSKLTSGA SVFAYQVSDP ERYGVVEFDD KFKALSVEEK PLQPKSNWAI TGLYFYDDQV
VDIAANLAPS ARGEYEITDV NRVYLERGQL SVQPIGRGYA WLDTGTPDSL LDAAEFVRVL
EKRQGMKICC PEEIAWRRGY ISDTELEGLA KNLGKSEYGK YLARCLNGGR
//
