The domain within your query sequence starts at position 13 and ends at position 294; the E-value for the Aldo_ket_red domain shown below is 4.1e-56.

MPTLGLGTWKSPPGQVTEAVKVAIDLGYRHIDCAQVYQNEKEVGVALQEKLKEQVVKRQD
LFIVSKLWCTFHDKSMVKGAFQKTLSDLQLDYLDLYLIHWPTGFKPGPDYFPLDASGNVI
PSDTDFVDTWTAMEQLVDEGLVKTIGVSNFNPLQIERILNKPGLKYKPAVNQIECHPYLT
QEKLIEYCHSKGIVVTAYSPLGSPDRPWAKPEDPSLLEDPRIKAIAAKYNKTTAQVLIRF
PIQRNLVVIPKSVTPVRIAENLKVFDFEVSSEDMATLLSYNR

Aldo_ket_red

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.

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