DNA beta-glucosyltransferase
Details
- Name
- DNA beta-glucosyltransferase
- Synonyms
- 2.4.1.27
- BGT
- Gene Name
- bgt
- Organism
- Enterobacteria phage T4
- Amino acid sequence
>lcl|BSEQ0011393|DNA beta-glucosyltransferase MKIAIINMGNNVINFKTVPSSETIYLFKVISEMGLNVDIISLKNGVYTKSFDEVDVNDYD RLIVVNSSINFFGGKPNLAILSAQKFMAKYKSKIYYLFTDIRLPFSQSWPNVKNRPWAYL YTEEELLIKSPIKVISQGINLDIAKAAHKKVDNVIEFEYFPIEQYKIHMNDFQLSKPTKK TLDVIYGGSFRSGQRESKMVEFLFDTGLNIEFFGNAREKQFKNPKYPWTKAPVFTGKIPM NMVSEKNSQAIAALIIGDKNYNDNFITLRVWETMASDAVMLIDEEFDTKHRIINDARFYV NNRAELIDRVNELKHSDVLRKEMLSIQHDILNKTRAKKAEWQDAFKKAIDL
- Number of residues
- 351
- Molecular Weight
- 40665.6
- Theoretical pI
- 9.56
- GO Classification
- FunctionsDNA beta-glucosyltransferase activityProcessesDNA modification / viral process
- General Function
- Dna beta-glucosyltransferase activity
- Specific Function
- Catalyzes the transfer of glucose (Glc) from uridine diphosphoglucose (UDP-Glc) to 5-hydroxymethylcytosine (5-HMC) in double-stranded DNA. Is involved in a DNA modification process to protect the phage genome against its own nucleases and the host restriction endonuclease system.
- Pfam Domain Function
- T4-Gluco-transf (PF09198)
- Transmembrane Regions
- Not Available
- Cellular Location
- Not Available
- Gene sequence
>lcl|BSEQ0011394|DNA beta-glucosyltransferase (bgt) ATGAAAATTGCTATAATTAATATGGGTAATAATGTTATTAATTTTAAAACTGTTCCATCT TCTGAAACTATTTATCTTTTTAAAGTTATTTCTGAAATGGGTCTTAATGTCGACATTATT TCTCTTAAAAATGGTGTTTACACTAAATCTTTTGATGAAGTAGATGTTAATGATTATGAC CGTTTGATAGTTGTTAATTCTTCTATTAACTTTTTTGGCGGTAAACCTAATTTAGCAATT TTATCTGCGCAAAAATTTATGGCAAAATACAAAAGTAAAATTTATTATTTATTTACAGAT ATACGTTTGCCGTTTTCGCAGTCTTGGCCAAATGTTAAAAATAGACCATGGGCATATTTG TACACTGAAGAAGAGCTATTAATTAAATCACCAATTAAAGTGATTTCCCAAGGTATAAAT TTAGACATTGCTAAGGCTGCGCATAAGAAAGTTGATAATGTTATTGAATTTGAATATTTT CCTATTGAACAATATAAAATTCATATGAACGATTTTCAATTATCTAAGCCTACCAAGAAA ACTTTGGATGTTATTTATGGCGGTTCATTTCGGTCCGGTCAACGCGAATCCAAGATGGTA GAATTCTTATTTGACACCGGTTTAAATATTGAGTTTTTTGGCAATGCACGAGAAAAACAG TTTAAAAATCCTAAATATCCTTGGACCAAAGCTCCGGTGTTCACTGGAAAAATTCCTATG AACATGGTATCTGAAAAGAATAGTCAAGCTATTGCTGCATTAATTATTGGTGACAAGAAT TATAATGACAACTTTATTACCTTACGCGTCTGGGAAACAATGGCATCTGATGCAGTGATG CTAATTGACGAAGAATTTGATACCAAACATCGAATTATTAATGATGCTCGTTTTTATGTA AATAATCGTGCTGAACTCATTGATAGAGTCAATGAGTTAAAACACAGTGATGTTTTGCGT AAAGAGATGCTTTCTATTCAACATGATATTTTAAATAAAACCCGTGCAAAGAAAGCCGAA TGGCAAGATGCGTTCAAAAAAGCTATTGATTTATAA
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID P04547 UniProtKB Entry Name GSTB_BPT4 GenBank Protein ID 15252 GenBank Gene ID X03139 - General References
- Tomaschewski J, Gram H, Crabb JW, Ruger W: T4-induced alpha- and beta-glucosyltransferase: cloning of the genes and a comparison of their products based on sequencing data. Nucleic Acids Res. 1985 Nov 11;13(21):7551-68. [Article]
- Miller ES, Kutter E, Mosig G, Arisaka F, Kunisawa T, Ruger W: Bacteriophage T4 genome. Microbiol Mol Biol Rev. 2003 Mar;67(1):86-156, table of contents. [Article]
- Thylen C: Expression and DNA sequence of the cloned bacteriophage T4 dCMP hydroxymethylase gene. J Bacteriol. 1988 Apr;170(4):1994-8. [Article]
- Lamm N, Tomaschewski J, Ruger W: Nucleotide sequence of the deoxycytidylate hydroxymethylase gene of bacteriophage T4 (g42) and the homology of its gene product with thymidylate synthase of E. coli. Nucleic Acids Res. 1987 May 11;15(9):3920. [Article]
- Sharma M, Ellis RL, Hinton DM: Identification of a family of bacteriophage T4 genes encoding proteins similar to those present in group I introns of fungi and phage. Proc Natl Acad Sci U S A. 1992 Jul 15;89(14):6658-62. [Article]
- Terragni J, Bitinaite J, Zheng Y, Pradhan S: Biochemical characterization of recombinant beta-glucosyltransferase and analysis of global 5-hydroxymethylcytosine in unique genomes. Biochemistry. 2012 Feb 7;51(5):1009-19. doi: 10.1021/bi2014739. Epub 2012 Jan 27. [Article]
- Vrielink A, Ruger W, Driessen HP, Freemont PS: Crystal structure of the DNA modifying enzyme beta-glucosyltransferase in the presence and absence of the substrate uridine diphosphoglucose. EMBO J. 1994 Aug 1;13(15):3413-22. [Article]
- Morera S, Imberty A, Aschke-Sonnenborn U, Ruger W, Freemont PS: T4 phage beta-glucosyltransferase: substrate binding and proposed catalytic mechanism. J Mol Biol. 1999 Sep 24;292(3):717-30. [Article]