1C3J

T4 PHAGE BETA-GLUCOSYLTRANSFERASE: SUBSTRATE BINDING AND PROPOSED CATALYTIC MECHANISM

External Resource: Annotation

Domain Annotation: SCOP/SCOPe Classification
Domain Annotation: SCOP2 Classification
Domain Annotation: ECOD Classification
Domain Annotation: CATH
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification
Structure Motif: Primary M-CSA Annotation

Domain Annotation: SCOP/SCOPe Classification SCOP-e Database Homepage

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d1c3ja_	Alpha and beta proteins (a/b)	UDP-Glycosyltransferase/glycogen phosphorylase	UDP-Glycosyltransferase/glycogen phosphorylase	beta-Glucosyltransferase (DNA-modifying)	beta-Glucosyltransferase (DNA-modifying)	(Tequatrovirus T4 ) [TaxId: 10665 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	Type B glycosyltransferase-like	8034427	3001586	SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	Glyco_trans_1_2_like	e1c3jA2	A: a/b three-layered sandwiches	X: UDP-Glycosyltransferase/glycogen phosphorylase (From Topology)	H: UDP-Glycosyltransferase/glycogen phosphorylase (From Topology)	T: UDP-Glycosyltransferase/glycogen phosphorylase	F: Glyco_trans_1_2_like	ECOD (1.6)
A	T4-Gluco-transf	e1c3jA1	A: a/b three-layered sandwiches	X: UDP-Glycosyltransferase/glycogen phosphorylase (From Topology)	H: UDP-Glycosyltransferase/glycogen phosphorylase (From Topology)	T: UDP-Glycosyltransferase/glycogen phosphorylase	F: T4-Gluco-transf	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.40.50.2000	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Glycogen Phosphorylase B	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF09198	Bacteriophage T4 beta-glucosyltransferase (T4-Gluco-transf)	Bacteriophage T4 beta-glucosyltransferase	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]. It is involved in a DNA modification process to protect the phage ...	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]. It is involved in a DNA modification process to protect the phage genome against its own nucleases and the host restriction endonuclease system [2].	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	BETA-GLUCOSYLTRANSFERASE	DNA beta-glucosyltransferase activity glycosyltransferase activity catalytic activity, acting on DNA catalytic activity, acting on a nucleic acid transferase activity glucosyltransferase activity hexosyltransferase activity catalytic activity	symbiont-mediated perturbation of host defense response response to host defenses biological process involved in interspecies interaction between organisms response to stimulus response to other organism symbiont-mediated perturbation of host immune response symbiont-mediated evasion of recognition by host innate immune effector response to defenses of other organism symbiont-mediated evasion of host innate immune response response to external stimulus symbiont-mediated evasion of host restriction-modification system response to biotic stimulus biological process involved in interaction with host biological process involved in symbiotic interaction evasion of host immune response symbiont-mediated perturbation of host defense response response to host defenses biological process involved in interspecies interaction between organisms response to stimulus response to other organism symbiont-mediated perturbation of host immune response symbiont-mediated evasion of recognition by host innate immune effector response to defenses of other organism symbiont-mediated evasion of host innate immune response response to external stimulus symbiont-mediated evasion of host restriction-modification system response to biotic stimulus biological process involved in interaction with host biological process involved in symbiotic interaction evasion of host immune response modulation by symbiont of host process response to host immune response response to host response to external biotic stimulus modulation of process of another organism nucleobase-containing compound metabolic process organic cyclic compound metabolic process DNA modification organic substance metabolic process macromolecule modification metabolic process primary metabolic process DNA metabolic process macromolecule metabolic process nucleic acid metabolic process	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR015281	DNA beta-glucosyltransferase, bacteriophage	Family

Structure Motif Annotation: Mechanism and Catalytic Site Atlas M-CSA Database Homepage

Chains	Enzyme Name	Description	Catalytic Residues
A	DNA beta-glucosyltransferase M-CSA #339	DNA beta-glucosyltransferase (BGT) is an enzyme encoded by a number of bacteriophage belonging to the T-even group. It catalyses the transfer of glucose from uridine diphosphoglucose (UDP-glucose) to 5-hydroxymethylcytosine (5-HMC) bases in double stranded DNA. Such glucosylation protects the infecting viral DNA from host restrictive enzymes. It may, in addition, be involved in phage specific gene expression by influencing transcription. Glucosylation also occurs in Trypanosoma bruceii where it is thought to be involved in regulating the expression of variant surface glycoproteins used by the parasite for protection against immune recognition. BGT is one of two enzymes involved in the glucosylation. In contrast to its counterpart which catalyses the formation of alpha-, it forms beta-glycosidic linkages While a divalent cation is required for optimal catalytic activity, crystallographic data suggests that the metal and substrate do not occupy the active site at the same time, and therefore, casts doubt on whether the metal is necessary for a non-reaction function, such as product displacement.	Defined by 4 residues: GLU:A-22PHE:A-72ASP:A-100ARG:A-191 Some residues are not modelled and lack atomic coordinates. Visualization is not available. Some residues are not modelled and lack atomic coordinates. Structure Motif searching is not available. EC: 2.4.1.27 (PDB Primary Data)

RCSB PDB Core Operations are funded by the National Science Foundation (DBI-1832184), the US Department of Energy (DE-SC0019749), and the National Cancer Institute, National Institute of Allergy and Infectious Diseases, and National Institute of General Medical Sciences of the National Institutes of Health under grant R01GM133198.