(data stored in ACNUC7421 zone)

SWISSPROT: C5BBC0_EDWI9

ID   C5BBC0_EDWI9            Unreviewed;       293 AA.
AC   C5BBC0;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   07-JUN-2017, entry version 54.
DE   RecName: Full=Glucose-1-phosphate thymidylyltransferase {ECO:0000256|RuleBase:RU003706};
DE            EC=2.7.7.24 {ECO:0000256|RuleBase:RU003706};
GN   OrderedLocusNames=NT01EI_0095 {ECO:0000313|EMBL:ACR67355.1};
OS   Edwardsiella ictaluri (strain 93-146).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Hafniaceae; Edwardsiella.
OX   NCBI_TaxID=634503 {ECO:0000313|EMBL:ACR67355.1, ECO:0000313|Proteomes:UP000001485};
RN   [1] {ECO:0000313|Proteomes:UP000001485}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=93-146 {ECO:0000313|Proteomes:UP000001485};
RA   Williams M.L., Gillaspy A.F., Dyer D.W., Thune R.L., Waldbieser G.C.,
RA   Schuster S.C., Gipson J., Zaitshik J., Landry C., Lawrence M.L.;
RT   "Complete genome sequence of Edwardsiella ictaluri 93-146.";
RL   Submitted (MAR-2009) 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: dTTP + alpha-D-glucose 1-phosphate =
CC       diphosphate + dTDP-alpha-D-glucose.
CC       {ECO:0000256|RuleBase:RU003706}.
CC   -!- SIMILARITY: Belongs to the glucose-1-phosphate
CC       thymidylyltransferase family. {ECO:0000256|RuleBase:RU003706}.
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DR   EMBL; CP001600; ACR67355.1; -; Genomic_DNA.
DR   RefSeq; WP_015869574.1; NC_012779.2.
DR   ProteinModelPortal; C5BBC0; -.
DR   STRING; 634503.NT01EI_0095; -.
DR   EnsemblBacteria; ACR67355; ACR67355; NT01EI_0095.
DR   GeneID; 7959814; -.
DR   KEGG; eic:NT01EI_0095; -.
DR   PATRIC; fig|634503.3.peg.89; -.
DR   eggNOG; ENOG4107QPT; Bacteria.
DR   eggNOG; COG1209; LUCA.
DR   HOGENOM; HOG000283473; -.
DR   KO; K00973; -.
DR   OMA; FIGPYSS; -.
DR   OrthoDB; POG091H050O; -.
DR   Proteomes; UP000001485; 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   Gene3D; 3.90.550.10; -; 1.
DR   InterPro; IPR005907; G1P_thy_trans_s.
DR   InterPro; IPR005835; NTP_transferase_dom.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   PANTHER; PTHR43532; PTHR43532; 1.
DR   Pfam; PF00483; NTP_transferase; 1.
DR   SUPFAM; SSF53448; SSF53448; 1.
DR   TIGRFAMs; TIGR01207; rmlA; 1.
PE   3: Inferred from homology;
DR   PRODOM; C5BBC0.
DR   SWISS-2DPAGE; C5BBC0.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001485};
KW   Magnesium {ECO:0000256|RuleBase:RU003706};
KW   Metal-binding {ECO:0000256|RuleBase:RU003706};
KW   Nucleotidyltransferase {ECO:0000256|RuleBase:RU003706,
KW   ECO:0000313|EMBL:ACR67355.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001485};
KW   Transferase {ECO:0000256|RuleBase:RU003706,
KW   ECO:0000313|EMBL:ACR67355.1}.
FT   DOMAIN        2    238       NTP_transferase. {ECO:0000259|Pfam:
FT                                PF00483}.
SQ   SEQUENCE   293 AA;  32673 MW;  A17AB17734F67270 CRC64;
     MKGIILAGGS GTRLYPITRG VSKQLLPIYD KPMIYYPLSV LMLAGIRDIL LISTPQDLPA
     FQRLLGDGGD IGVRLQYAEQ PRPEGLAQAF LIGESFLDGD SCCLVLGDNI FFGQGFSPKL
     RQVAQRGGGA TVFGYQVMDP ERFGVVEFDD DFRALSIEEK PQRPRSNWAV TGLYFYDAQV
     VDFARRVTPS VRGELEITSI NQMYLQRGEL NVELLGRGFA WLDTGTHDSL LEASAFVQTV
     EKRQGFKIAC LEEIAWRNGW LDDHGVARAA ASLDKTAYGA YLRELLHVRP RQY
//

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