| Family: | ALDO/KETO REDUCTASE (PTHR11732) | ||
| Subfamilies: | 16 | ||
| PANTHER Links: |
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| Abstract: |
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 [PMID:2498333]. All possess a similar structure, with a beta-alpha-beta fold characteristic of nucleotide binding proteins [PMID:2105951]. 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 hydrophobic nature of the pocket favours aromatic and apolar substrates over highly polar ones [PMID:1621098]. Binding of the NADPH coenzyme causes a massive conformational change, reorienting a loop, effectively locking the coenzyme in place. This binding is more similar to FAD- than to NAD(P)-binding oxidoreductases [PMID:1447221]. Some proteins of this entry contain a K+ ion channel beta chain regulatory domain; these are reported to have oxidoreductase activity [PMID:10884227]. |
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| InterPro Accession: | IPR001395 | ||
| PANTHER Molecular Function: |
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| PANTHER Biological Process: |
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| Pathway Categories: | No pathway information available | ||
| Training Sequences: |
403
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| HMM Length | 456 | ||
| Downloads: | HMM (HMMER format) |
| Total | Celera | FlyBase | NCBI | |
| H. sapiens | 49 | 30 | 0 | 19 |
| M. musculus | 53 | 33 | 0 | 20 |
| R. norvegicus | 43 | 20 | 0 | 23 |
| D. melanogaster | 13 | 0 | 13 | 0 |




