Top Level Name

  ⌊ Superfamily (core) Haloacid Dehalogenase

    ⌊ Subgroup C1.8: polynucleotide 5'-hydroxyl-kinase c-terminal phosphatase like

     ⌊ Family polynucleotide 5'-hydroxyl-kinase c-terminal phosphatase


1LTQ (polynucleotide 5'-hydroxyl-kinase)
Total 100% <100%
Functional domains 1 0 1
UniProtKB 1 0 1
GI 4 0 4
Structures 5
Reactions 1
Functional domains of this family were last updated on Nov. 22, 2017

Enzymes in the polynucleotide 5'-hydroxyl-kinase c-terminal phosphatase family contain two distinct structural domains, each with a seperate active site. Only the C-terminal domain is part of the haloacid dehalogenase superfamily. This domain has 3'-phosphatase activity, and can hydrolyze 2'3'-cyclic phosphodiesters. However, the biologically relevant phosphatase reaction has not yet been identified. Mg2+ is required as a cofactor. The N-terminal domain has kinase activity, but is not a part of the haloacid dehalogenase superfamily.

Galburt, E.A., et al.

Structure of a tRNA repair enzyme and molecular biology workhorse: T4 polynucleotide kinase

▸ Abstract

Structure (Camb) 2002;10(9):1249-1260 | PubMed ID: 12220496

No notes.

Total number of functional domains in this group.
Number of Functional Domains that have been manually or automatically been assigned to a family.
Number of Functional Domains that have not been assigned to a family.
Number of structures available from the PDB for members of this group.
Number of Functional Domains with 100% of Conserved Residues
Number of Functional Domains with less than 100% Conserved Residues

Active Site

Catalyzed Reaction(s)

polynucleotide 5'-hydroxyl-kinase

+ +
5'-dephospho-DNA
16678		 ATP
15422		 5'-phospho-DNA
16149		 ADP
16761

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