Summary: Aldo/keto reductase family
Pfam includes annotations and additional family information from a range of different sources. These sources can be accessed via the tabs below.
This is the Wikipedia entry entitled "Aldo-keto reductase". More...
Aldo-keto reductase Edit Wikipedia article
The aldo-keto reductase family is a family of proteins that are subdivided into 16 categories; these include a number of related monomeric NADPH-dependent oxidoreductases, such as aldehyde reductase, aldose reductase, prostaglandin F synthase, xylose reductase, rho crystallin, and many others.[1]
Contents
Structure
All possess a similar structure, with a beta-alpha-beta fold characteristic of nucleotide binding proteins.[2] 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.[3]
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.[4]
Examples
Some proteins of this family contain a potassium channel beta chain regulatory domain; these are reported to have oxidoreductase activity.[5]
See also
References
- ^ Bohren KM, Bullock B, Wermuth B, Gabbay KH (June 1989). "The aldo-keto reductase superfamily. cDNAs and deduced amino acid sequences of human aldehyde and aldose reductases". J. Biol. Chem. 264 (16): 9547–51. PMID 2498333.
- ^ Schade SZ, Early SL, Williams TR, Kézdy FJ, Heinrikson RL, Grimshaw CE, Doughty CC (March 1990). "Sequence analysis of bovine lens aldose reductase". J. Biol. Chem. 265 (7): 3628–35. PMID 2105951.
- ^ Wilson DK, Bohren KM, Gabbay KH, Quiocho FA (July 1992). "An unlikely sugar substrate site in the 1.65 A structure of the human aldose reductase holoenzyme implicated in diabetic complications". Science. 257 (5066): 81–4. doi:10.1126/science.1621098. PMID 1621098.
- ^ Borhani DW, Harter TM, Petrash JM (December 1992). "The crystal structure of the aldose reductase.NADPH binary complex". J. Biol. Chem. 267 (34): 24841–7. PMID 1447221.
- ^ Gulbis JM, Zhou M, Mann S, MacKinnon R (July 2000). "Structure of the cytoplasmic beta subunit-T1 assembly of voltage-dependent K+ channels". Science. 289 (5476): 123–7. doi:10.1126/science.289.5476.123. PMID 10884227.
This page is based on a Wikipedia article. The text is available under the Creative Commons Attribution/Share-Alike License.
This tab holds the annotation information that is stored in the Pfam database. As we move to using Wikipedia as our main source of annotation, the contents of this tab will be gradually replaced by the Wikipedia tab.
Aldo/keto reductase family Provide feedback
This family includes a number of K+ ion channel beta chain regulatory domains - these are reported to have oxidoreductase activity [2].
Literature references
-
Wilson DK, Tarle I, Petrash JM, Quiocho FA; , Proc Natl Acad Sci U S A 1993;90:9847-9851.: Refined 1.8 A structure of human aldose reductase complexed with the potent inhibitor zopolrestat. PUBMED:8234324 EPMC:8234324
-
Gulbis JM, Zhou M, Mann S, MacKinnon R; , Science 2000;289:123-127.: Structure of the cytoplasmic beta subunit-T1 assembly of voltage-dependent K+ channels. PUBMED:10884227 EPMC:10884227
External database links
HOMSTRAD: | aldosered |
PRINTS: | PR00069 |
PROSITE: | PDOC00061 |
SCOP: | 1ads |
Transporter classification: | 8.A.5 |
This tab holds annotation information from the InterPro database.
InterPro entry 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.
Domain organisation
Below is a listing of the unique domain organisations or architectures in which this domain is found. More...
Loading domain graphics...
Alignments
We store a range of different sequence alignments for families. As well as the seed alignment from which the family is built, we provide the full alignment, generated by searching the sequence database (reference proteomes) using the family HMM. We also generate alignments using four representative proteomes (RP) sets, the UniProtKB sequence database, the NCBI sequence database, and our metagenomics sequence database. More...
View options
We make a range of alignments for each Pfam-A family. You can see a description of each above. You can view these alignments in various ways but please note that some types of alignment are never generated while others may not be available for all families, most commonly because the alignments are too large to handle.
Seed (33) |
Full (79121) |
Representative proteomes | UniProt (267993) |
NCBI (376588) |
Meta (7424) |
||||
---|---|---|---|---|---|---|---|---|---|
RP15 (8380) |
RP35 (33863) |
RP55 (70538) |
RP75 (121389) |
||||||
Jalview | |||||||||
HTML | |||||||||
PP/heatmap | 1 |
1Cannot generate PP/Heatmap alignments for seeds; no PP data available
Key:
available,
not generated,
— not available.
Format an alignment
Download options
We make all of our alignments available in Stockholm format. You can download them here as raw, plain text files or as gzip-compressed files.
Seed (33) |
Full (79121) |
Representative proteomes | UniProt (267993) |
NCBI (376588) |
Meta (7424) |
||||
---|---|---|---|---|---|---|---|---|---|
RP15 (8380) |
RP35 (33863) |
RP55 (70538) |
RP75 (121389) |
||||||
Raw Stockholm | |||||||||
Gzipped |
You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.
HMM logo
HMM logos is one way of visualising profile HMMs. Logos provide a quick overview of the properties of an HMM in a graphical form. You can see a more detailed description of HMM logos and find out how you can interpret them here. More...
Trees
This page displays the phylogenetic tree for this family's seed alignment. We use FastTree to calculate neighbour join trees with a local bootstrap based on 100 resamples (shown next to the tree nodes). FastTree calculates approximately-maximum-likelihood phylogenetic trees from our seed alignment.
Note: You can also download the data file for the tree.
Curation and family details
This section shows the detailed information about the Pfam family. You can see the definitions of many of the terms in this section in the glossary and a fuller explanation of the scoring system that we use in the scores section of the help pages.
Curation
Seed source: | Prosite |
Previous IDs: | aldo_ket_red; |
Type: | Domain |
Sequence Ontology: | SO:0000417 |
Author: |
Finn RD |
Number in seed: | 33 |
Number in full: | 79121 |
Average length of the domain: | 264.40 aa |
Average identity of full alignment: | 24 % |
Average coverage of the sequence by the domain: | 84.79 % |
HMM information
HMM build commands: |
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 47079205 -E 1000 --cpu 4 HMM pfamseq
|
||||||||||||
Model details: |
|
||||||||||||
Model length: | 291 | ||||||||||||
Family (HMM) version: | 22 | ||||||||||||
Download: | download the raw HMM for this family |
Species distribution
Sunburst controls
HideWeight segments by...
Change the size of the sunburst
Colour assignments
![]() |
![]() |
![]() |
![]() |
![]() |
![]() |
![]() |
![]() |
Selections
Align selected sequences to HMM
Generate a FASTA-format file
Clear selection
This visualisation provides a simple graphical representation of the distribution of this family across species. You can find the original interactive tree in the adjacent tab. More...
Tree controls
HideThe tree shows the occurrence of this domain across different species. More...
Loading...
Please note: for large trees this can take some time. While the tree is loading, you can safely switch away from this tab but if you browse away from the family page entirely, the tree will not be loaded.
Interactions
Structures
For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the Aldo_ket_red domain has been found. There are 623 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein sequence.
Loading structure mapping...