InterPro : IPR023210

Name  NADP-dependent oxidoreductase domain Short Name  NADP_OxRdtase_dom
Type  Domain Description  The aldo-keto reductase family includes a number of related monomeric NADPH-dependent oxidoreductases, such as aldehyde reductase, aldose reductase, prostaglandin F synthase, xylose reductase, rho crystallin, and many others []. All possess a similar structure, with a beta-alpha-beta fold characteristic of nucleotide binding proteins []. The fold comprises a parallel beta-8/alpha-8-barrel, which contains a novel NADP-binding motif. The binding site is located in a large,deep, elliptical pocket in the C-terminal end of the beta sheet, the substrate being bound in an extended conformation. The hydrophobicnature of the pocket favours aromatic and apolar substrates over highly polar ones [].Binding of the NADPH coenzyme causes a massive conformational change, reorienting a loop, effectively locking thecoenzyme in place. This binding is more similar to FAD- than to NAD(P)-binding oxidoreductases [].Some proteins of this entry contain a K+ ion channel beta chain regulatory domain; these are reported to have oxidoreductase activity []. This entry represents the NADP-dependent oxidoreductase domain found in these proteins.

Sequence Features

GO Displayer


InterPro protein domain ID --> Contigs



0 Child Features

0 Contains

0 Found In

0 Parent Features

5 Publications

First Author Title Year Journal Volume Pages
Bohren KM The aldo-keto reductase superfamily. cDNAs and deduced amino acid sequences of human aldehyde and aldose reductases. 1989 J Biol Chem 264 9547-51
Schade SZ Sequence analysis of bovine lens aldose reductase. 1990 J Biol Chem 265 3628-35
Borhani DW The crystal structure of the aldose reductase.NADPH binary complex. 1992 J Biol Chem 267 24841-7
Wilson DK An unlikely sugar substrate site in the 1.65 A structure of the human aldose reductase holoenzyme implicated in diabetic complications. 1992 Science 257 81-4
Gulbis JM Structure of the cytoplasmic beta subunit-T1 assembly of voltage-dependent K+ channels. 2000 Science 289 123-7

To cite PlanMine, please refer to the following publication:

Rozanski, A., Moon, H., Brandl, H., Martín-Durán, J. M., Grohme, M., Hüttner, K., Bartscherer, K., Henry, I., & Rink, J. C.
PlanMine 3.0—improvements to a mineable resource of flatworm biology and biodiversity
Nucleic Acids Research, gky1070. doi:10.1093/nar/gky1070 (2018)