Aldo-Keto Reductase (AKR) Superfamily Database

About AKR | AKR Members | Phylogenies | Multiple Sequence Alignment | Submit AKR Sequences

Site under construction

This site contains existing and potential protein sequences of the AKR protein superfamily, as well as tools to visualize aligned sequences and their conservation across species. In addition, scientists are encouraged to submit newly identified AKRs.

AKRs share similar three-dimensional structures involving a parallel β-8/α-8-barrel fold, and they function as enzymes that catalyze the reduced nicotinamide adenine dinucleotide (phosphate) (NAD(P)H)-dependent oxido-reduction of carbonyl groups. Over 190 members have been identified in species ranging from prokaryotes to plants, fungi, and animals. These proteins, which are grouped into 16 families named AKR1-AKR16, have unique structural features that influence their substrates and kinetics.

Contributors

Previous versions of this website coding and design by Jaehyun Joo, Blanca Himes, Anisha Tehim, Nisha Narayanan, and Trevor Penning.

Current version by Kim Lorenz, Benjamin F Voight, and Trevor Penning. Full code for this site is available on GitHub

References

Mindnich RD, Penning TM. Aldo-keto reductase (AKR) superfamily: genomics and annotation. Hum Genomics. 2009 Jul;3(4):362-70. doi: 10.1186/1479-7364-3-4-362. PMID: 19706366; PMCID: PMC3206293.

Penning TM. The aldo-keto reductases (AKRs): Overview. Chem Biol Interact. 2015 Jun 5;234:236-46. doi: 10.1016/j.cbi.2014.09.024. Epub 2014 Oct 7. PMID: 25304492; PMCID: PMC4388799.

Huacachino AA, Joo J, Narayanan N, Tehim A, Himes BE, Penning TM. Aldo-Keto Reductase (AKR) Superfamily Website and Database: an Update Chem Biol Interact. 2024 Aug 1:398:111111. doi: 10.1016/j.cbi.2024.111111. Epub 2024 Jun 13. PMID: 38878851; PMCID: PMC11232437.

Funding

This work was supported by the University of Pennsylvania Center of Excellence in Environmental Toxicology (P30 ES013508).