(data stored in ACNUC7421 zone)

SWISSPROT: Q144P2_PARXL

ID   Q144P2_PARXL            Unreviewed;       292 AA.
AC   Q144P2;
DT   22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT   22-AUG-2006, sequence version 1.
DT   08-MAY-2019, entry version 85.
DE   RecName: Full=Glucose-1-phosphate thymidylyltransferase {ECO:0000256|RuleBase:RU003706};
DE            EC=2.7.7.24 {ECO:0000256|RuleBase:RU003706};
GN   ORFNames=Bxe_A3801 {ECO:0000313|EMBL:ABE29197.1};
OS   Paraburkholderia xenovorans (strain LB400).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=266265 {ECO:0000313|EMBL:ABE29197.1, ECO:0000313|Proteomes:UP000001817};
RN   [1] {ECO:0000313|EMBL:ABE29197.1, ECO:0000313|Proteomes:UP000001817}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LB400 {ECO:0000313|EMBL:ABE29197.1,
RC   ECO:0000313|Proteomes:UP000001817};
RX   PubMed=17030797; DOI=10.1073/pnas.0606924103;
RA   Chain P.S., Denef V.J., Konstantinidis K.T., Vergez L.M., Agullo L.,
RA   Reyes V.L., Hauser L., Cordova M., Gomez L., Gonzalez M., Land M.,
RA   Lao V., Larimer F., LiPuma J.J., Mahenthiralingam E., Malfatti S.A.,
RA   Marx C.J., Parnell J.J., Ramette A., Richardson P., Seeger M.,
RA   Smith D., Spilker T., Sul W.J., Tsoi T.V., Ulrich L.E., Zhulin I.B.,
RA   Tiedje J.M.;
RT   "Burkholderia xenovorans LB400 harbors a multi-replicon, 9.73-Mbp
RT   genome shaped for versatility.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15280-15287(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; CP000270; ABE29197.1; -; Genomic_DNA.
DR   RefSeq; WP_011486993.1; NZ_CP008760.1.
DR   STRING; 266265.Bxe_A3801; -.
DR   EnsemblBacteria; ABE29197; ABE29197; Bxe_A3801.
DR   GeneID; 4002585; -.
DR   KEGG; bxb:DR64_1478; -.
DR   KEGG; bxe:Bxe_A3801; -.
DR   PATRIC; fig|266265.5.peg.688; -.
DR   eggNOG; ENOG4108I19; Bacteria.
DR   eggNOG; COG1209; LUCA.
DR   HOGENOM; HOG000283473; -.
DR   KO; K00973; -.
DR   OMA; GPYPMIY; -.
DR   OrthoDB; 1004719at2; -.
DR   BioCyc; BXEN266265:BXE_RS03255-MONOMER; -.
DR   Proteomes; UP000001817; Chromosome 1.
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; Q144P2.
DR   SWISS-2DPAGE; Q144P2.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001817};
KW   Magnesium {ECO:0000256|RuleBase:RU003706};
KW   Metal-binding {ECO:0000256|RuleBase:RU003706};
KW   Nucleotidyltransferase {ECO:0000256|RuleBase:RU003706,
KW   ECO:0000313|EMBL:ABE29197.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001817};
KW   Transferase {ECO:0000256|RuleBase:RU003706,
KW   ECO:0000313|EMBL:ABE29197.1}.
FT   DOMAIN        3    239       NTP_transferase. {ECO:0000259|Pfam:
FT                                PF00483}.
SQ   SEQUENCE   292 AA;  32445 MW;  78BDA97A8BC7C4A7 CRC64;
     MRKGIILAGG SGTRLYPITR SVSKQLLPVY DKPMIYYPLS TLMLAGIRDI LVISTAEDTP
     RFAEMLGDGS AWGIDLQYAV QPSPDGLAQA FIIGREFIGS DPCTLILGDN IFHGHDLVRQ
     LTRAGQSEQG ATVFAYHVHD PERYGVVEFD ENFHALSLEE KPLKPRSNYA VTGLYFYDNQ
     VCDIAADVKP SARGELEITD VNKRYLEIAQ LDVEIMGRGY AWLDTGTHDS LLEAASFIAT
     LQSRQGLMVA CPEEIAYRSH WISAEQVERL AGPLAKNRYG QYLKQIISEA VK
//

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