SMART: Pfam domain Aldo_ket

The domain within your query sequence starts at position 18 and ends at position 301; the E-value for the Aldo_ket_red domain shown below is 9.9e-67.

ALGFGTYKPEEVNENKPLEAIHLALEAGFRHIDTAYVYQTENHVGQAIRSKIAAGLVKRE
DIFLTTKLWCTFHRPELVRSNLEKSLKNLQLDYADLYLIHYPVQMKPGEDLFPEDEHGKT
LFDTVDICATWEAMEKCKDAGLVKSIGVSNFNSRQLEKILNKPGLKYKPVCNQVECHLYL
NQRKLLNYCKSKDIVLVAYCALGSQRPKRWVDPSSPVLLNDPILCDMAKKHKRSPAQIAL
RYHLQRGIVVLAQSYKENEIKENIQVFEFELPSEDMKILDSLDR

Aldo_ket_red

PFAM accession number:	PF00248
Interpro abstract (IPR023210):	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 [ (PUBMED:2498333) ]. All possess a similar structure, with a beta-alpha-beta fold characteristic of nucleotide binding proteins [ (PUBMED: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 [ (PUBMED: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 [ (PUBMED:1447221) ]. Some proteins of this entry contain a K+ ion channel beta chain regulatory domain; these are reported to have oxidoreductase activity [ (PUBMED:10884227) ]. This entry represents the NADP-dependent oxidoreductase domain found in these proteins.

PFAM accession number:

PF00248

Interpro abstract (IPR023210):

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 [ (PUBMED:2498333) ]. All possess a similar structure, with a beta-alpha-beta fold characteristic of nucleotide binding proteins [ (PUBMED: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 [ (PUBMED: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 [ (PUBMED:1447221) ].

Some proteins of this entry contain a K+ ion channel beta chain regulatory domain; these are reported to have oxidoreductase activity [ (PUBMED:10884227) ].

This entry represents the NADP-dependent oxidoreductase domain found in these proteins.

This is a PFAM domain. For full annotation and more information, please see the PFAM entry Aldo_ket_red