Protein Domain : Deoxycytidylate hydroxymethylase IPR014619

Type  Family
Description  In bacteriophage T4, a specific DNA modification system has evolved in order to protect its own DNA from degradation by host nucleases [ ]. Firstly, the cytosine base in dCMP is hydroxymethylated by the T4 enzyme deoxycytidylate hydroxymethylase to produce hydroxymethyl-dCMP (Hm-dCMP). This product is subsequently converted to Hm-dCTP by the combined action of T4 deoxynucleoside monophosphate kinase and host nucleoside diphosphate kinase. Hm-dCTP is then incorporated into T4 DNA by the phage DNA polymerase enzyme. Glucosylation of the Hm-dCTP residues within the phage DNA by glucosyltransferases completes the modification. Degradation of host dCTP by a T4 dCTPase ensures that no unmodified cytosine residues are incorporated in the phage genome.This entry represents the deoxycytidylate hydroxymethylase enzyme catalysing the first step in T4 the cytosine modification system. This enzyme is a dimer which, despite a low sequence identity, forms a similar fold to that of thymidylate synthases [ ]. Each monomer consists of several alpha helices surrounding a six-stranded β-sheet which forms the dimerisation interface. The active site is formed in a deep pocket, with the sugar and phosphate-binding residues in a similar configuration to that of thymidylate synthase, while the residues presumed to bind cytosine and the folate cofactor are more divergent. The enzyme has been shown to interact with proteins in the T4 deoxyribonucleoside triphosphate synthetase complex [, ].
Short Name  Deoxycytidylate_hydroxyMease

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