CATH Classification

Domain Context

CATH Clusters

Superfamily Crystal structure of tRNA isopentenylpyrophosphate transferase (bh2366) domain
Functional Family Adenylate isopentenyltransferase

Enzyme Information

2.5.1.27
Adenylate dimethylallyltransferase (AMP-dependent).
based on mapping to UniProt Q5GHF7
Dimethylallyl diphosphate + AMP = diphosphate + N(6)- (dimethylallyl)adenosine 5'-phosphate.
-!- Involved in the biosynthesis of cytokinins in plants. -!- Some isoforms from the plant Arabidopsis thaliana are specific for AMP while others also have the activity of EC 2.5.1.112.
2.5.1.112
Adenylate dimethylallyltransferase (ADP/ATP-dependent).
based on mapping to UniProt Q5GHF7
(1) Dimethylallyl diphosphate + ADP = diphosphate + N6-(dimethylallyl)adenosine diphosphate. (2) Dimethylallyl diphosphate + ATP = diphosphate + N6-(dimethylallyl)adenosine triphosphate.
-!- Involved in the biosynthesis of cytokinins in plants. -!- The IPT4 isoform from the plant Arabidopsis thaliana is specific for ADP and ATP. -!- Other isoforms, such as IPT1 from Arabidopsis thaliana and the enzyme from the common hop, Humulus lupulus, also have a lower activity with AMP (cf. EC 2.5.1.27). -!- Formerly EC 2.5.1.n4.

UniProtKB Entries (1)

Q5GHF7
IPT_HUMLU
Humulus lupulus
Adenylate isopentenyltransferase

PDB Structure

PDB 3A8T
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
Crystal structure and substrate specificity of plant adenylate isopentenyltransferase from Humulus lupulus: distinctive binding affinity for purine and pyrimidine nucleotides
Chu, H.-M., Ko, T.-P., Wang, A.H.-J.
Nucleic Acids Res.
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