CATH Classification

Domain Context

CATH Clusters

Superfamily ATP-grasp fold, B domain
Functional Family Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase

Enzyme Information

2.7.4.24
Diphosphoinositol-pentakisphosphate kinase.
based on mapping to UniProt O43314
(1) ATP + 1D-myo-inositol 5-diphosphate 1,2,3,4,6-pentakisphosphate = ADP + 1D-myo-inositol 1,5-bis(diphosphate) 2,3,4,6-tetrakisphosphate. (2) ATP + 1D-myo-inositol hexakisphosphate = ADP + 1D-myo-inositol 1-diphosphate 2,3,4,5,6-pentakisphosphate.
-!- This enzyme is activated by osmotic shock. -!- Ins(1,3,4,5,6)P(5), 1D-myo-inositol diphosphate tetrakisphosphate and 1D-myo-inositol bisdiphosphate triphosphate are not substrates. -!- Formerly EC 2.7.1.155.
2.7.4.21
Inositol-hexakisphosphate kinase.
based on mapping to UniProt O43314
(1) ATP + 1D-myo-inositol hexakisphosphate = ADP + 1D-myo-inositol 5-diphosphate 1,2,3,4,6-pentakisphosphate. (2) ATP + 1D-myo-inositol 1-diphosphate 2,3,4,5,6-pentakisphosphate = ADP + 1D-myo-inositol 1,5-bis(diphosphate) 2,3,4,6-tetrakisphosphate.
-!- Three mammalian isoforms are known to exist. -!- Formerly EC 2.7.1.152.

UniProtKB Entries (1)

O43314
VIP2_HUMAN
Homo sapiens
Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase 2

PDB Structure

PDB 5DGI
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
Cellular Cations Control Conformational Switching of Inositol Pyrophosphate Analogues.
Hager, A., Wu, M., Wang, H., Brown, N.W., Shears, S.B., Veiga, N., Fiedler, D.
Chemistry