ID B1KUV6_CLOBM Unreviewed; 353 AA.
AC B1KUV6;
DT 29-APR-2008, integrated into UniProtKB/TrEMBL.
DT 29-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 73.
DE SubName: Full=Glucose-1-phosphate thymidylyltransferase {ECO:0000313|EMBL:ACA56885.1};
DE EC=2.7.7.24 {ECO:0000313|EMBL:ACA56885.1};
GN OrderedLocusNames=CLK_1511 {ECO:0000313|EMBL:ACA56885.1};
OS Clostridium botulinum (strain Loch Maree / Type A3).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=498214 {ECO:0000313|EMBL:ACA56885.1, ECO:0000313|Proteomes:UP000000722};
RN [1] {ECO:0000313|EMBL:ACA56885.1, ECO:0000313|Proteomes:UP000000722}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Loch Maree / Type A3 {ECO:0000313|Proteomes:UP000000722};
RX PubMed=18060065; DOI=10.1371/journal.pone.0001271;
RA Smith T.J., Hill K.K., Foley B.T., Detter J.C., Munk A.C., Bruce D.C.,
RA Doggett N.A., Smith L.A., Marks J.D., Xie G., Brettin T.S.;
RT "Analysis of the neurotoxin complex genes in Clostridium botulinum A1-A4
RT and B1 strains: BoNT/A3, /Ba4 and /B1 clusters are located within
RT plasmids.";
RL PLoS ONE 2:E1271-E1271(2007).
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DR EMBL; CP000962; ACA56885.1; -; Genomic_DNA.
DR RefSeq; WP_012344694.1; NC_010520.1.
DR AlphaFoldDB; B1KUV6; -.
DR KEGG; cbl:CLK_1511; -.
DR HOGENOM; CLU_029499_0_1_9; -.
DR Proteomes; UP000000722; Chromosome.
DR GO; GO:0008879; F:glucose-1-phosphate thymidylyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR CDD; cd04189; G1P_TT_long; 1.
DR Gene3D; 2.160.10.10; Hexapeptide repeat proteins; 1.
DR InterPro; IPR005908; G1P_thy_trans_l.
DR InterPro; IPR005835; NTP_transferase_dom.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR NCBIfam; TIGR01208; rmlA_long; 1.
DR PANTHER; PTHR42883; GLUCOSE-1-PHOSPHATE THYMIDYLTRANSFERASE; 1.
DR PANTHER; PTHR42883:SF2; ZGC:136439; 1.
DR Pfam; PF00483; NTP_transferase; 1.
DR SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
PE 4: Predicted;
KW Nucleotidyltransferase {ECO:0000313|EMBL:ACA56885.1};
KW Transferase {ECO:0000313|EMBL:ACA56885.1}.
FT DOMAIN 2..234
FT /note="Nucleotidyl transferase"
FT /evidence="ECO:0000259|Pfam:PF00483"
SQ SEQUENCE 353 AA; 39395 MW; 1AC823E80BF6D373 CRC64;
MKALILSGGT GTRLRPLTYT NAKQLLPLAN KPILFYIIEK IVKAGIYDIG IIVGDTREEV
KKMVGNGDRW GVKISYLYQP MPLGLAHAVK TASEFLMEDD FLMVLGDNVF NMELNKLIDS
FYSNNANSAL LLHKVENPSQ YGVAVVEDTL IIKLVEKPKE FVSDLIITGV YIFDKSIFMA
IDNIKPSQRG ELEITDAIQK QLKTGGRVTY ELIQGWWKDT GQLQDILEAN RLMLDEIDCE
FKTLPQCNSV FMGKIQIGRN VIIENSTIIG PVAIADDTTI TNSCIGPYTS IDKAVTVNDC
EIDNCIILEN AKIDGIHKRI SGSLIGRKVQ IKELHKRPFS HTFLLGDDSK INL
//
