ID D1BX04_XYLCX Unreviewed; 287 AA.
AC D1BX04;
DT 19-JAN-2010, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2010, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE RecName: Full=Glucose-1-phosphate thymidylyltransferase {ECO:0000256|ARBA:ARBA00017654, ECO:0000256|RuleBase:RU003706};
DE EC=2.7.7.24 {ECO:0000256|ARBA:ARBA00012461, ECO:0000256|RuleBase:RU003706};
GN OrderedLocusNames=Xcel_2557 {ECO:0000313|EMBL:ACZ31572.1};
OS Xylanimonas cellulosilytica (strain DSM 15894 / CECT 5975 / LMG 20990 /
OS XIL07).
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales;
OC Promicromonosporaceae; Xylanimonas.
OX NCBI_TaxID=446471 {ECO:0000313|EMBL:ACZ31572.1, ECO:0000313|Proteomes:UP000002255};
RN [1] {ECO:0000313|Proteomes:UP000002255}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15894 / CECT 5975 / LMG 20990 / XIL07
RC {ECO:0000313|Proteomes:UP000002255};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Ivanova N.,
RA Mikhailova N., Foster B., Clum A., Brettin T., Detter J.C., Han C.,
RA Larimer F., Land M., Hauser L., Markowitz V., Cheng J.F., Hugenholtz P.,
RA Woyke T., Wu D., Gehrich-Schroeter G., Schneider S., Pukall S.R.,
RA Klenk H.P., Eisen J.A.;
RT "The complete chromosome of Xylanimonas cellulosilytica DSM 15894.";
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ACZ31572.1, ECO:0000313|Proteomes:UP000002255}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15894 / CECT 5975 / LMG 20990 / XIL07
RC {ECO:0000313|Proteomes:UP000002255};
RX PubMed=21304672; DOI=10.4056/sigs.571102;
RA Foster B., Pukall R., Abt B., Nolan M., Glavina Del Rio T., Chen F.,
RA Lucas S., Tice H., Pitluck S., Cheng J.-F., Chertkov O., Brettin T.,
RA Han C., Detter J.C., Bruce D., Goodwin L., Ivanova N., Mavromatis K.,
RA Pati A., Mikhailova N., Chen A., Palaniappan K., Land M., Hauser L.,
RA Chang Y.-J., Jeffries C.D., Chain P., Rohde M., Goeker M., Bristow J.,
RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.-P.,
RA Lapidus A.;
RT "Complete genome sequence of Xylanimonas cellulosilytica type strain
RT (XIL07).";
RL Stand. Genomic Sci. 2:1-8(2010).
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; CP001821; ACZ31572.1; -; Genomic_DNA.
DR RefSeq; WP_012879314.1; NC_013530.1.
DR AlphaFoldDB; D1BX04; -.
DR STRING; 446471.Xcel_2557; -.
DR KEGG; xce:Xcel_2557; -.
DR eggNOG; COG1209; Bacteria.
DR HOGENOM; CLU_029499_9_0_11; -.
DR OrthoDB; 9803871at2; -.
DR Proteomes; UP000002255; 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: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:UP000002255};
KW Transferase {ECO:0000256|RuleBase:RU003706}.
FT DOMAIN 3..234
FT /note="Nucleotidyl transferase"
FT /evidence="ECO:0000259|Pfam:PF00483"
SQ SEQUENCE 287 AA; 31460 MW; 3F83DBEBDFA6B11D CRC64;
MRGIILAGGS GTRLHPITLG VSKQLVPVYD KPMIYYPLST LILAGIKDIL IITTPHDAEQ
FRRLLGDGSQ FGVSISYTVQ AEPNGLAQAF VLGADFVGSE GAALVLGDNI FYGPGLGSKL
TRFENIDGGA VFAYRVANPT EYGVVEFDES FRALSLEEKP AEPKSNYAVP GLYFYDNDVV
EIAKNLTPSA RGEYEITDVN RHYLEAGKLQ VEVLPRGTAW LDTGTFDSLL EAGDYVRTIE
NRQGLKIGAP EEVAWRRGFL SDDELRERAE KLTKSGYGTY LLSLLDH
//
