Identification |
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Name: | Deoxyguanosinetriphosphate triphosphohydrolase |
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Synonyms: | - dGTP triphosphohydrolase
- dGTPase
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Gene Name: | dgt |
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Enzyme Class: | |
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Biological Properties |
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General Function: | Involved in magnesium ion binding |
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Specific Function: | dGTPase preferentially hydrolyzes dGTP over the other canonical NTPs |
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Cellular Location: | Cytoplasmic |
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SMPDB Pathways: | Not Available |
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KEGG Pathways: | |
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KEGG Reactions: | |
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EcoCyc Reactions: | |
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Complex Reactions: | |
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Metabolites: | |
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GO Classification: | Function |
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binding | catalytic activity | cation binding | dGTPase activity | hydrolase activity | hydrolase activity, acting on ester bonds | ion binding | magnesium ion binding | metal ion binding | phosphoric ester hydrolase activity | triphosphoric monoester hydrolase activity | Process |
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cellular nitrogen compound metabolic process | GTP metabolic process | metabolic process | nitrogen compound metabolic process | nucleobase, nucleoside and nucleotide metabolic process | nucleobase, nucleoside, nucleotide and nucleic acid metabolic process | nucleoside phosphate metabolic process | nucleotide metabolic process | purine nucleoside triphosphate metabolic process | purine nucleotide metabolic process | purine ribonucleoside triphosphate metabolic process |
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Gene Properties |
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Blattner: | b0160 |
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Gene Orientation | Clockwise |
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Centisome Percentage: | 3.86 |
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Left Sequence End | 179237 |
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Right Sequence End | 180754 |
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Gene Sequence: | >1518 bp
ATGGCACAGATTGATTTCCGAAAAAAAATAAACTGGCATCGTCGTTACCGTTCACCGCAG
GGCGTTAAAACCGAACATGAGATCCTGCGGATCTTCGAGAGCGATCGCGGGCGTATCATC
AACTCTCCGGCAATTCGTCGTCTGCAACAAAAGACCCAGGTTTTTCCACTGGAGCGCAAT
GCCGCCGTGCGCACGCGTCTTACCCACTCGATGGAAGTCCAGCAGGTGGGGCGCTACATC
GCCAAAGAAATTTTAAGCCGTCTGAAAGAGCTTAAATTACTGGAAGCATACGGCCTGGAT
GAACTGACCGGTCCCTTTGAAAGCATTGTTGAGATGTCATGCCTGATGCACGATATCGGC
AATCCGCCGTTTGGTCATTTTGGCGAAGCGGCGATAAATGACTGGTTTCGCCAACGTTTG
CACCCGGAAGATGCCGAAAGCCAGCCTCTGACTGACGATCGCTGCAGCGTGGCGGCACTA
CGTTTACGGGACGGGGAAGAACCGCTTAACGAGCTGCGGCGCAAGATTCGTCAGGACTTA
TGTCATTTTGAGGGGAATGCACAAGGCATTCGCCTGGTGCATACATTGATGCGGATGAAT
CTCACCTGGGCACAGGTTGGCGGTATTTTAAAATATACCCGTCCGGCGTGGTGGCGTGGC
GAAACGCCTGAGACACATCACTATTTAATGAAAAAGCCGGGTTATTATCTTTCTGAAGAA
GCCTATATTGCCCGGTTGCGTAAAGAACTTAATTTGGCGCTTTACAGTCGTTTTCCATTA
ACGTGGATTATGGAAGCTGCCGACGACATCTCCTATTGTGTGGCAGACCTTGAAGATGCG
GTAGAGAAAAGAATATTTACCGTTGAGCAGCTTTATCATCATTTGCACGAAGCGTGGGGC
CAGCATGAGAAAGGTTCGCTCTTTTCGCTGGTGGTTGAAAATGCCTGGGAAAAATCACGC
TCAAATAGTTTAAGCCGCAGTACGGAAGATCAGTTTTTTATGTATTTACGGGTAAACACC
CTAAATAAACTGGTACCCTACGCGGCACAACGATTTATTGATAATCTGCCTGCGATTTTC
GCCGGAACGTTTAATCATGCATTATTGGAAGATGCCAGCGAATGCAGCGATCTTCTTAAG
CTATATAAAAATGTCGCTGTAAAACATGTGTTTAGCCATCCAGATGTCGAGCGGCTTGAA
TTGCAGGGCTATCGGGTCATTAGCGGATTATTAGAGATTTATCGTCCTTTATTAAGCCTG
TCGTTATCAGACTTTACTGAACTGGTAGAAAAAGAACGGGTGAAACGTTTCCCTATTGAA
TCGCGCTTATTCCACAAACTCTCGACGCGCCATCGGCTGGCCTATGTCGAGGCTGTCAGT
AAATTACCGTCAGATTCTCCTGAGTTTCCGCTATGGGAATATTATTACCGTTGCCGCCTG
CTGCAGGATTATATCAGCGGTATGACCGACCTCTATGCGTGGGATGAATACCGACGTCTG
ATGGCCGTAGAACAATAA |
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Protein Properties |
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Pfam Domain Function: | |
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Protein Residues: | 505 |
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Protein Molecular Weight: | 59382 |
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Protein Theoretical pI: | 8 |
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Signaling Regions: | |
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Transmembrane Regions: | |
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Protein Sequence: | >Deoxyguanosinetriphosphate triphosphohydrolase
MAQIDFRKKINWHRRYRSPQGVKTEHEILRIFESDRGRIINSPAIRRLQQKTQVFPLERN
AAVRTRLTHSMEVQQVGRYIAKEILSRLKELKLLEAYGLDELTGPFESIVEMSCLMHDIG
NPPFGHFGEAAINDWFRQRLHPEDAESQPLTDDRCSVAALRLRDGEEPLNELRRKIRQDL
CHFEGNAQGIRLVHTLMRMNLTWAQVGGILKYTRPAWWRGETPETHHYLMKKPGYYLSEE
AYIARLRKELNLALYSRFPLTWIMEAADDISYCVADLEDAVEKRIFTVEQLYHHLHEAWG
QHEKGSLFSLVVENAWEKSRSNSLSRSTEDQFFMYLRVNTLNKLVPYAAQRFIDNLPAIF
AGTFNHALLEDASECSDLLKLYKNVAVKHVFSHPDVERLELQGYRVISGLLEIYRPLLSL
SLSDFTELVEKERVKRFPIESRLFHKLSTRHRLAYVEAVSKLPSDSPEFPLWEYYYRCRL
LQDYISGMTDLYAWDEYRRLMAVEQ |
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References |
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External Links: | |
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General Reference: | - Blattner, F. R., Plunkett, G. 3rd, Bloch, C. A., Perna, N. T., Burland, V., Riley, M., Collado-Vides, J., Glasner, J. D., Rode, C. K., Mayhew, G. F., Gregor, J., Davis, N. W., Kirkpatrick, H. A., Goeden, M. A., Rose, D. J., Mau, B., Shao, Y. (1997). "The complete genome sequence of Escherichia coli K-12." Science 277:1453-1462. Pubmed: 9278503
- Fujita, N., Mori, H., Yura, T., Ishihama, A. (1994). "Systematic sequencing of the Escherichia coli genome: analysis of the 2.4-4.1 min (110,917-193,643 bp) region." Nucleic Acids Res 22:1637-1639. Pubmed: 8202364
- Hayashi, K., Morooka, N., Yamamoto, Y., Fujita, K., Isono, K., Choi, S., Ohtsubo, E., Baba, T., Wanner, B. L., Mori, H., Horiuchi, T. (2006). "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Mol Syst Biol 2:2006.0007. Pubmed: 16738553
- Quirk, S., Bhatnagar, S. K., Bessman, M. J. (1990). "Primary structure of the deoxyguanosine triphosphate triphosphohydrolase-encoding gene (dgt) of Escherichia coli." Gene 89:13-18. Pubmed: 2165018
- Seto, D., Bhatnagar, S. K., Bessman, M. J. (1988). "The purification and properties of deoxyguanosine triphosphate triphosphohydrolase from Escherichia coli." J Biol Chem 263:1494-1499. Pubmed: 2826481
- Wurgler, S. M., Richardson, C. C. (1990). "Structure and regulation of the gene for dGTP triphosphohydrolase from Escherichia coli." Proc Natl Acad Sci U S A 87:2740-2744. Pubmed: 2157212
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