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24  structures 8  species 0  interactions 9  sequences 2  architectures

Family: T4-Gluco-transf (PF09198)

Summary: Bacteriophage T4 beta-glucosyltransferase

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This is the Wikipedia entry entitled "DNA beta-glucosyltransferase". More...

DNA beta-glucosyltransferase Edit Wikipedia article

DNA beta-glucosyltransferase
EC number2.4.1.27
CAS number9030-14-2
IntEnzIntEnz view
ExPASyNiceZyme view
MetaCycmetabolic pathway
PDB structuresRCSB PDB PDBe PDBsum

In enzymology, a DNA beta-glucosyltransferase (EC is an enzyme that catalyzes the chemical reaction in which a beta-D-glucosyl residue is transferred from UDP-glucose to an hydroxymethylcytosine residue in DNA. It is analogous to the enzyme DNA alpha-glucosyltransferase.

This enzyme belongs to the family of glycosyltransferases, specifically the hexosyltransferases. The systematic name of this enzyme class is UDP-glucose:DNA beta-D-glucosyltransferase. Other names in common use include T4-HMC-beta-glucosyl transferase, T4-beta-glucosyl transferase, T4 phage beta-glucosyltransferase, UDP glucose-DNA beta-glucosyltransferase, and uridine diphosphoglucose-deoxyribonucleate beta-glucosyltransferase.

Structural studies

As of late 2007, 20 structures have been solved for this class of enzymes, with PDB accession codes 1BGT, 1BGU, 1C3J, 1IXY, 1J39, 1JEJ, 1JG6, 1JG7, 1JIU, 1JIV, 1JIX, 1M5R, 1NVK, 1NZD, 1NZF, 1QKJ, 1SXP, 1SXQ, 2BGT, and 2BGU.

Bacteriophage T4 beta-glucosyltransferase

PDB 1m5r EBI.jpg
ternary complex of t4 phage bgt with udp and a 13 mer dna duplex

In molecular biology,Bacteriophage T4 beta-glucosyltransferase refers to a protein domain found in a virus of Escherichia coli named bacteriophage T4. Members of this family are enzymes encoded by bacteriophage T4, which modify DNA by transferring glucose from uridine diphosphoglucose to 5-hydroxymethyl cytosine bases of phage T4 DNA.[1]


Beta-glucosyltransferase is an enzyme, or more specifically an inverting glycosyltransferase(GT). In other words, it transfers glucose from uridine diphospho-glucose (UDPglucose)to an acceptor, modified DNA through beta-Glycosidic bond. The role of the enzyme is to protect the infecting viral DNA from the bacteria's restriction enzymes. Glucosylation prevents the virus DNA from being cut up. Furthermore, glucosylation may aid gene expression of the bacteriophage by influencing transcription.[2][3][4]


This structure has both alpha helices and beta strands.[2]


  1. ^ Moréra S, Larivière L, Kurzeck J, Aschke-Sonnenborn U, Freemont PS, Janin J, Rüger W (August 2001). "High resolution crystal structures of T4 phage beta-glucosyltransferase: induced fit and effect of substrate and metal binding". J. Mol. Biol. 311 (3): 569–77. doi:10.1006/jmbi.2001.4905. PMID 11493010.
  2. ^ a b Larivière L, Gueguen-Chaignon V, Moréra S (2003). "Crystal structures of the T4 phage beta-glucosyltransferase and the D100A mutant in complex with UDP-glucose: glucose binding and identification of the catalytic base for a direct displacement mechanism". J Mol Biol. 330 (5): 1077–86. doi:10.1016/s0022-2836(03)00635-1. PMID 12860129.
  3. ^ Moréra S, Imberty A, Aschke-Sonnenborn U, Rüger W, Freemont PS (1999). "T4 phage beta-glucosyltransferase: substrate binding and proposed catalytic mechanism". J Mol Biol. 292 (3): 717–30. doi:10.1006/jmbi.1999.3094. PMID 10497034.
  4. ^ Moréra S, Larivière L, Kurzeck J, Aschke-Sonnenborn U, Freemont PS, Janin J, et al. (2001). "High resolution crystal structures of T4 phage beta-glucosyltransferase: induced fit and effect of substrate and metal binding". J Mol Biol. 311 (3): 569–77. doi:10.1006/jmbi.2001.4905. PMID 11493010.
This article incorporates text from the public domain Pfam and InterPro: IPR015281
  • Kornberg SR, Zimmerman SB & Kornberg A (1961). "Glucosylation of deoxyribonucleic acid by enzymes from bacteriophage-infected Escherichia coli". J. Biol. Chem. 236: 1487–1493.

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This tab holds the annotation information that is stored in the Pfam database. As we move to using Wikipedia as our main source of annotation, the contents of this tab will be gradually replaced by the Wikipedia tab.

Bacteriophage T4 beta-glucosyltransferase Provide feedback

Members of this family are DNA-modifying enzymes encoded by bacteriophage T4 that transfer glucose from uridine diphosphoglucose to 5-hydroxymethyl cytosine bases of phage T4 DNA [1].

Literature references

  1. Morera S, Lariviere L, Kurzeck J, Aschke-Sonnenborn U, Freemont PS, Janin J, Ruger W; , J Mol Biol. 2001;311:569-577.: High resolution crystal structures of T4 phage beta-glucosyltransferase: induced fit and effect of substrate and metal binding. PUBMED:11493010 EPMC:11493010

External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR015281

Members of this family include DNA-modifying enzymes encoded by bacteriophage T4 that catalyses the transfer of glucose (Glc) from uridine diphosphoglucose (UDP-Glc) to 5-hydroxymethylcytosine (5-HMC) in double-stranded DNA [ PUBMED:11493010 ]. It is involved in a DNA modification process to protect the phage genome against its own nucleases and the host restriction endonuclease system [ PUBMED:22229759 ].

Gene Ontology

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Domain organisation

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Seed source: pdb_1jix
Previous IDs: none
Type: Domain
Sequence Ontology: SO:0000417
Author: Sammut SJ
Number in seed: 1
Number in full: 9
Average length of the domain: 38.00 aa
Average identity of full alignment: 67 %
Average coverage of the sequence by the domain: 10.71 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 57096847 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 25.0 25.0
Trusted cut-off 25.0 25.1
Noise cut-off 21.1 19.3
Model length: 38
Family (HMM) version: 12
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Archea Archea Eukaryota Eukaryota
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Viruses Viruses Unclassified Unclassified
Viroids Viroids Unclassified sequence Unclassified sequence


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For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the T4-Gluco-transf domain has been found. There are 24 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein sequence.

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