(data stored in SCRATCH zone)

SWISSPROT: B1VRP8_STRGG

ID   B1VRP8_STRGG            Unreviewed;       289 AA.
AC   B1VRP8;
DT   20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT   20-MAY-2008, sequence version 1.
DT   07-JUN-2017, entry version 57.
DE   RecName: Full=Glucose-1-phosphate thymidylyltransferase {ECO:0000256|RuleBase:RU003706};
DE            EC=2.7.7.24 {ECO:0000256|RuleBase:RU003706};
GN   OrderedLocusNames=SGR_637 {ECO:0000313|EMBL:BAG17466.1};
OS   Streptomyces griseus subsp. griseus (strain JCM 4626 / NBRC 13350).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=455632 {ECO:0000313|EMBL:BAG17466.1, ECO:0000313|Proteomes:UP000001685};
RN   [1] {ECO:0000313|EMBL:BAG17466.1, ECO:0000313|Proteomes:UP000001685}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 4626 / NBRC 13350 {ECO:0000313|Proteomes:UP000001685};
RX   PubMed=18375553; DOI=10.1128/JB.00204-08;
RA   Ohnishi Y., Ishikawa J., Hara H., Suzuki H., Ikenoya M., Ikeda H.,
RA   Yamashita A., Hattori M., Horinouchi S.;
RT   "Genome sequence of the streptomycin-producing microorganism
RT   Streptomyces griseus IFO 13350.";
RL   J. Bacteriol. 190:4050-4060(2008).
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; AP009493; BAG17466.1; -; Genomic_DNA.
DR   RefSeq; WP_003964529.1; NC_010572.1.
DR   ProteinModelPortal; B1VRP8; -.
DR   SMR; B1VRP8; -.
DR   STRING; 455632.SGR_637; -.
DR   EnsemblBacteria; BAG17466; BAG17466; SGR_637.
DR   GeneID; 6209622; -.
DR   KEGG; sgr:SGR_637; -.
DR   PATRIC; fig|455632.4.peg.622; -.
DR   eggNOG; ENOG4108I19; Bacteria.
DR   eggNOG; COG1209; LUCA.
DR   HOGENOM; HOG000283473; -.
DR   KO; K00973; -.
DR   OMA; GPYPMIY; -.
DR   Proteomes; UP000001685; 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; B1VRP8.
DR   SWISS-2DPAGE; B1VRP8.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001685};
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:UP000001685};
KW   Transferase {ECO:0000256|RuleBase:RU003706,
KW   ECO:0000313|EMBL:BAG17466.1}.
FT   DOMAIN        2    235       NTP_transferase. {ECO:0000259|Pfam:
FT                                PF00483}.
SQ   SEQUENCE   289 AA;  31594 MW;  96F674352C3A2C26 CRC64;
     MKGIILAGGH GTRLQPITFG VSKQLLPVYD KPMIYYPLSV LMLAGITDIQ IVAAPDGLQG
     FRRLLGDGSD LGLDLSYAEQ DKPRGLADAF LVSEDHIGDD AVALVLGDNL FHGPGFSDIL
     RRVALDLDGA VLFGYPVRDP ERYGVGEVDG AGNLTALEEK PARPRSNLAI TGLYFYDNDV
     VEIARSLRPS ERGELEITDV NRRYLERGKA ALVQLGRGFV WLDTGTHDAL IDAGQYVQLL
     EHRQGVRIAC VEEIAWRMGY IDREACHRLG AQLARSPYGQ YVMDIAAAG
//

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