1B5D

DCMP Hydroxymethylase from T4 (Intact)

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	d1b5da_	Alpha and beta proteins (a+b)	Thymidylate synthase/dCMP hydroxymethylase	Thymidylate synthase/dCMP hydroxymethylase	Thymidylate synthase/dCMP hydroxymethylase	dCMP hydroxymethylase	(Tequatrovirus T4 ) [TaxId: 10665 ],	SCOPe (2.08)
B	d1b5db_	Alpha and beta proteins (a+b)	Thymidylate synthase/dCMP hydroxymethylase	Thymidylate synthase/dCMP hydroxymethylase	Thymidylate synthase/dCMP hydroxymethylase	dCMP hydroxymethylase	(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	Thymidylate synthase/dCMP hydroxymethylase	8036160	3000544	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Thymidylate synthase/dCMP hydroxymethylase	8036160	3000544	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	PF00303	e1b5dA1	A: a+b two layers	X: Thymidylate synthase/dCMP hydroxymethylase (From Topology)	H: Thymidylate synthase/dCMP hydroxymethylase (From Topology)	T: Thymidylate synthase/dCMP hydroxymethylase	F: PF00303	ECOD (1.6)
B	PF00303	e1b5dB1	A: a+b two layers	X: Thymidylate synthase/dCMP hydroxymethylase (From Topology)	H: Thymidylate synthase/dCMP hydroxymethylase (From Topology)	T: Thymidylate synthase/dCMP hydroxymethylase	F: PF00303	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.30.572.10	Alpha Beta	2-Layer Sandwich	Thymidylate Synthase	Chain A	CATH (4.3.0)
B	3.30.572.10	Alpha Beta	2-Layer Sandwich	Thymidylate Synthase	Chain A	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF00303	Thymidylate synthase (Thymidylat_synt)	Thymidylate synthase	This is a family of proteins that are flavin-dependent thymidylate synthases.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	PROTEIN (DEOXYCYTIDYLATE HYDROXYMETHYLASE)	transferase activity, transferring one-carbon groups deoxycytidylate 5-hydroxymethyltransferase activity transferase activity hydroxymethyl-, formyl- and related transferase activity catalytic activity	-	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR014619	Deoxycytidylate hydroxymethylase	Family
A, B	IPR036926	Thymidylate synthase/dCMP hydroxymethylase superfamily	Homologous Superfamily
A, B	IPR023451	Thymidylate synthase/dCMP hydroxymethylase domain	Domain

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

Chains	Enzyme Name	Description	Catalytic Residues
A	deoxycytidylate 5-hydroxymethyltransferase M-CSA #700	Deoxycytidylate (dCMP) 5-hydroxymethylase (CH) of bacteriophage T4 catalyses the addition of a protective hydroxymethyl group to cytosine monophosphate as a method of avoiding digestion by the host restriction systems. It requires the presence of methylenetetrahydrofolate (CH2THF).	Defined by 3 residues: GLU:A-60CYS:A-148ASP:A-179 \| Explore in 3D: M-CSA Motif Definition Search M-CSA Motif EC: 2.1.2.8 (PDB Primary Data) Search M-CSA Motif + EC 2.1.2.8

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.