(data stored in SCRATCH zone)

SWISSPROT: A0A0H2Y3B2_YERPA

ID   A0A0H2Y3B2_YERPA        Unreviewed;       310 AA.
AC   A0A0H2Y3B2;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   08-MAY-2019, entry version 16.
DE   RecName: Full=Glucose-1-phosphate thymidylyltransferase {ECO:0000256|RuleBase:RU003706};
DE            EC=2.7.7.24 {ECO:0000256|RuleBase:RU003706};
GN   OrderedLocusNames=YPA_0157 {ECO:0000313|EMBL:ABG12126.1};
OS   Yersinia pestis bv. Antiqua (strain Antiqua).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=360102 {ECO:0000313|EMBL:ABG12126.1, ECO:0000313|Proteomes:UP000001971};
RN   [1] {ECO:0000313|EMBL:ABG12126.1, ECO:0000313|Proteomes:UP000001971}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Antiqua {ECO:0000313|EMBL:ABG12126.1,
RC   ECO:0000313|Proteomes:UP000001971};
RX   PubMed=16740952; DOI=10.1128/JB.00124-06;
RA   Chain P.S., Hu P., Malfatti S.A., Radnedge L., Larimer F.,
RA   Vergez L.M., Worsham P., Chu M.C., Andersen G.L.;
RT   "Complete genome sequence of Yersinia pestis strains Antiqua and
RT   Nepal516: evidence of gene reduction in an emerging pathogen.";
RL   J. Bacteriol. 188:4453-4463(2006).
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|RuleBase:RU003706};
CC   -!- SIMILARITY: Belongs to the glucose-1-phosphate
CC       thymidylyltransferase family. {ECO:0000256|RuleBase:RU003706}.
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DR   EMBL; CP000308; ABG12126.1; -; Genomic_DNA.
DR   EnsemblBacteria; ABG12126; ABG12126; YPA_0157.
DR   KEGG; ypa:YPA_0157; -.
DR   KO; K00973; -.
DR   OMA; KPSWRNE; -.
DR   BioCyc; YPES360102:GHZU-172-MONOMER; -.
DR   Proteomes; UP000001971; 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; A0A0H2Y3B2.
DR   SWISS-2DPAGE; A0A0H2Y3B2.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001971};
KW   Magnesium {ECO:0000256|RuleBase:RU003706};
KW   Metal-binding {ECO:0000256|RuleBase:RU003706};
KW   Nucleotidyltransferase {ECO:0000256|RuleBase:RU003706,
KW   ECO:0000313|EMBL:ABG12126.1};
KW   Transferase {ECO:0000256|RuleBase:RU003706,
KW   ECO:0000313|EMBL:ABG12126.1}.
FT   DOMAIN       19    255       NTP_transferase. {ECO:0000259|Pfam:
FT                                PF00483}.
SQ   SEQUENCE   310 AA;  34539 MW;  3EBBB92257BB9397 CRC64;
     MYQEIVCIRR LHVSGERMKG IILAGGSGSR LHPITRGVSK QLLPIYDKPM IYYPLSVLML
     AGIRDVLIIS TPEDLPSFQR LLGNGDEFGI NLSYAAQPSP DGLAQAFIIG EAFIDNEPCC
     LVLGDNIYFG QGFSPKLKAV AARQQGATVF GYQVMDPERF GVVEFDDNFR ALSIEEKPSQ
     PKSNWAVTGL YFYDNQVVDF AKQVKPSARG ELEITSINQM YLDRGELTVE LLGRGFAWLD
     TGTHDSLIEA STFVQTVEKR QGFKIACLEE IAWRNGWLDD DGVKRAATAL AKTGYGKYLL
     DLLHARPRQY
//

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