ID Q8KFM1_CHLTE Unreviewed; 293 AA.
AC Q8KFM1;
DT 01-OCT-2002, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2002, sequence version 1.
DT 27-MAR-2024, entry version 112.
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=rfbA {ECO:0000313|EMBL:AAM71551.1};
GN OrderedLocusNames=CT0305 {ECO:0000313|EMBL:AAM71551.1};
OS Chlorobaculum tepidum (strain ATCC 49652 / DSM 12025 / NBRC 103806 / TLS)
OS (Chlorobium tepidum).
OC Bacteria; Chlorobiota; Chlorobiia; Chlorobiales; Chlorobiaceae;
OC Chlorobaculum.
OX NCBI_TaxID=194439 {ECO:0000313|EMBL:AAM71551.1, ECO:0000313|Proteomes:UP000001007};
RN [1] {ECO:0000313|EMBL:AAM71551.1, ECO:0000313|Proteomes:UP000001007}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49652 / DSM 12025 / NBRC 103806 / TLS
RC {ECO:0000313|Proteomes:UP000001007};
RX PubMed=12093901; DOI=10.1073/pnas.132181499;
RA Eisen J.A., Nelson K.E., Paulsen I.T., Heidelberg J.F., Wu M., Dodson R.J.,
RA Deboy R., Gwinn M.L., Nelson W.C., Haft D.H., Hickey E.K., Peterson J.D.,
RA Durkin A.S., Kolonay J.L., Yang F., Holt I., Umayam L.A., Mason T.,
RA Brenner M., Shea T.P., Parksey D., Nierman W.C., Feldblyum T.V.,
RA Hansen C.L., Craven M.B., Radune D., Vamathevan J., Khouri H., White O.,
RA Gruber T.M., Ketchum K.A., Venter J.C., Tettelin H., Bryant D.A.,
RA Fraser C.M.;
RT "The complete genome sequence of Chlorobium tepidum TLS, a photosynthetic,
RT anaerobic, green-sulfur bacterium.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:9509-9514(2002).
CC -!- FUNCTION: Catalyzes the formation of dTDP-glucose, from dTTP and
CC glucose 1-phosphate, as well as its pyrophosphorolysis.
CC {ECO:0000256|ARBA:ARBA00037065, 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; AE006470; AAM71551.1; -; Genomic_DNA.
DR RefSeq; NP_661209.1; NC_002932.3.
DR RefSeq; WP_010931997.1; NC_002932.3.
DR AlphaFoldDB; Q8KFM1; -.
DR STRING; 194439.CT0305; -.
DR EnsemblBacteria; AAM71551; AAM71551; CT0305.
DR KEGG; cte:CT0305; -.
DR PATRIC; fig|194439.7.peg.295; -.
DR eggNOG; COG1209; Bacteria.
DR HOGENOM; CLU_029499_9_0_10; -.
DR OrthoDB; 9803871at2; -.
DR Proteomes; UP000001007; Chromosome.
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:SF4; GLUCOSE-1-PHOSPHATE THYMIDYLYLTRANSFERASE 2; 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:AAM71551.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001007};
KW Transferase {ECO:0000256|RuleBase:RU003706, ECO:0000313|EMBL:AAM71551.1}.
FT DOMAIN 2..241
FT /note="Nucleotidyl transferase"
FT /evidence="ECO:0000259|Pfam:PF00483"
SQ SEQUENCE 293 AA; 32521 MW; 1EE9DA3A2133242B CRC64;
MKGIILAGGS GTRLYPVTKG VSKQLLPVYD KPMIYYPLTT LMLAGIRDIL VITTPDDQSS
FVKLLGDGSD WGINLSYTVQ PSPDGLAQAF ILGRDFIGDD DVCLVLGDNI FFGYGFSGML
EEAVHVVERR RKAVVFGYYV SDPERYGVVE FDSDGQVFSI VEKPEKPKSN YAVVGLYFYP
NDVIDIAASV NPSSRGELEI TSVNQTYLDR GDLVCSIMGR GFAWLDTGTH ESFQEAGNFI
ETVEKRQGLK VACPEEIAWR NGWIGDADIE RLASPLLKNQ YGQYLLNLLE RRI
//
