Bacterial virus anti-defence systems · sequence & structure resource

Encyclopaedia of Bacterial Virus Anti-Defence Systems


Protein: Deoxycytidylate hydroxymethylase

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Overview

Mode of Action (MoA) converts 2′-deoxycytidylate (or 2′-deoxycytidine-5′-monophosphate, dCMP) into 5-hydroxymethyl-dCMP (a step in DNA hypermodification).
Evidence Crystal structure of T4 deoxycytidylate hydroxymethylase with dCMP shows the direct binding (ECO_0001034). Substitution of Asp179 to Asn drastically reduced activity on dCMP (~15,000-fold decrease in k_cat/K_M), but increased activity on dUMP, suggesting Asp179 is crucial for dCMP specificity and catalysis.
MoA Category modifies phage molecules to avoid recognition
Subtype(s) of the defence system(s) inhibited by the protein Defence Subtype Escherichia coli RM
Relevant publication(s) DOI 10.1093/emboj/18.5.1104
Other components of the anti-defence system Multicomponent System dnmp; bgt
Known structure in PDB PDB ID 1B5E_A
Genome(s) encoding the protein Protein Source Enterobacteria phage T4
Defence system(s) inhibited by the protein Defences RM
View homologs from eukaryotic dsDNA viruses

3D structure

PDB entry model.

A similar PDB structure exists: 1B5E_A

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Feature viewer - predicted secondary structure

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Pfam annotations

Pfam Name Pfam Acc Pfam Length Colour HMM Start HMM End Ali Start Ali End Env Start Env End Evalue
Thymidylat_synt PF00303 266 53 219 55 226 18 238 3.7e-18

Sequence Viewer

Amino acid position: -

MISDSMTVEEIRLHLGLALKEKDFVVDKTGVKTIEIIGASFVADEPFIFGALNDEYIQRELEWYKSKSLFVKDIPGETPKIWQQVASSKGEINSNYGWAIWSEDNYAQYDMCLAELGQNPDSRRGIMIYTRPSMQFDYNKDGMSDFMCTNTVQYLIRDKKINAVVNMRSNDVVFGFRNDYAWQKYVLDKLVSDLNAGDSTRQYKAGSIIWNVGSLHVYSRHFYLVDHWWKTGETHISKKDYVGKYA