Gene Ontology annotation based on UniProtKB/Swiss-Prot UniPathway vocabulary mapping
Gene Ontology annotation based on UniProtKB/Swiss-Prot keyword mapping
Combined Automated Annotation using Multiple IEA Sources.
On the specificity of bacteriophage-induced hydroxymethylcytosine glucosyltransferases. II. Specificities of hydroxymethylcytosine alphaand beta-glucosyltransferases induced by bacteriophage T4.
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Characterized the sequence and substrate specificities of T4-induced hydroxymethylcytosine alpha- and beta-glucosyltransferases on T4 DNA.
"On the specificity of bacteriophage-induced hydroxymethylcytosine glucosyltransferases. II. Specificities of hydroxymethylcytosine alphaand beta-glucosyltransferases induced by bacteriophage T4."
Deep research summary for Bacteriophage T4 bgt
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BGT transfers glucose from UDP-glucose onto 5hmC residues in double-stranded DNA to form beta-glucosyl-5hmC.
"**BGT (bgt; UniProt P04547)** is a **DNA-modifying glycosyltransferase** that transfers glucose from **UDP-glucose** onto **5hmC residues in double-stranded DNA**, producing **β-glucosyl-5hmC** in the phage genome."
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Glucosylation of 5hmC by AGT and BGT protects T4 DNA from host restriction endonucleases.
"Glucosylation of 5hmC is described as part of a **phage DNA protection system**, helping prevent cleavage by host nucleases and restriction endonucleases"
UniProtKB entry P04547 (BGT_BPT4)
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BGT catalyzes the transfer of glucose from UDP-glucose to 5hmC in T4 DNA (EC 2.4.1.27).
"Catalyzes the transfer of glucose from uridine diphosphoglucose to 5-hydroxymethyl cytosine of T4 DNA to yield glucosyl 5-hydroxymethyl cytosine (glc-HMC) (PubMed:22229759)."
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Enzymatic reaction and EC number of BGT.
"Reaction=Transfers a beta-D-glucosyl residue from UDP-alpha-D-glucose to a hydroxymethylcytosine residue in DNA.; EC=2.4.1.27;"
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The glc-HMC modification protects the phage genome against host restriction endonucleases and CRISPR-Cas9 defense.
"The glc-HMC modification protects the phage genome against its own nucleases and the host restriction endonuclease system (PubMed:22229759)."