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| PROSITE documentation PDOC00061 |
Aldo/keto reductase family signatures
Description
The aldo-keto reductase family [1,2] groups together a number of structurally
and functionally related NADPH-dependent oxidoreductases as well as some other
proteins. The proteins known to belong to this family are:
- Aldehyde reductase (EC 1.1.1.2).
- Aldose reductase (EC 1.1.1.21).
- 3-α-hydroxysteroid dehydrogenase (EC 1.1.1.50), which terminates
androgen action by converting 5-α-dihydrotestosterone to 3-α-
androstanediol.
- Prostaglandin F synthase (EC 1.1.1.188) which catalyzes the reduction of
prostaglandins H2 and D2 to F2-α.
- D-sorbitol-6-phosphate dehydrogenase (EC 1.1.1.200) from apple.
- Morphine 6-dehydrogenase (EC 1.1.1.218) from Pseudomonas putida plasmid
pMDH7.2 (gene morA).
- Chlordecone reductase (EC 1.1.1.225) which reduces the pesticide
chlordecone (kepone) to the corresponding alcohol.
- 2,5-diketo-D-gluconic acid reductase (EC 1.1.1.274) which catalyzes the
reduction of 2,5-diketogluconic acid to 2-keto-L-gulonic acid, a key
intermediate in the production of ascorbic acid.
- NAD(P)H-dependent xylose reductase (EC 1.1.1.-) from the yeast Pichia
stipitis. This enzyme reduces xylose into xylit.
- Trans-1,2-dihydrobenzene-1,2-diol dehydrogenase (EC 1.3.1.20).
- 3-oxo-5-β-steroid 4-dehydrogenase (EC 1.3.99.6) which catalyzes the
reduction of delta(4)-3-oxosteroids.
- A soybean reductase, which co-acts with chalcone synthase in the formation
of 4,2',4'-trihydroxychalcone.
- Frog eye lens rho crystallin.
- Yeast GCY protein, whose function is not known.
- Leishmania major P110/11E protein. P110/11E is a developmentally regulated
protein whose abundance is markedly elevated in promastigotes compared with
amastigotes. Its exact function is not yet known.
- Escherichia coli hypothetical protein yafB.
- Escherichia coli hypothetical protein yghE.
- Yeast hypothetical protein YBR149w.
- Yeast hypothetical protein YHR104w.
- Yeast hypothetical protein YJR096w.
These proteins have all about 300 amino acid residues. We derived 3 consensus
patterns specific to this family of proteins. The first one is located in the
N-terminal section of these proteins. The second pattern is located in the
central section. The third pattern, located in the C-terminal, is centered on
a lysine residue whose chemical modification, in aldose and aldehyde
reductases, affect the catalytic efficiency.
April 2006 / Patterns revised.
Technical section
PROSITE methods (with tools and information) covered by this documentation:
| ALDOKETO_REDUCTASE_1, PS00798; Aldo/keto reductase family signature 1 (PATTERN) |
| Consensus pattern: |
G-[FY]-R-[HSAL]-[LIVMF]-D-[STAGCL]-[AS]-x(5)-[EQ]-x(2)-[LIVMCA]-[GS]
|
| Sequences known to belong to this class detected by the pattern: |
ALL |
| Other sequence(s) detected in Swiss-Prot: |
NONE. |
|
|
|
| Matching PDB structures:
1A80 1ABN 1ADS 1AE4 ... [ALL] |
| ALDOKETO_REDUCTASE_2, PS00062; Aldo/keto reductase family signature 2 (PATTERN) |
| Consensus pattern: |
[LIVMFY]-x(8)-{L}-[KREQ]-{K}-[LIVM]-G-[LIVM]-[SC]-N-[FY]
|
| Sequences known to belong to this class detected by the pattern: |
ALL, except for morA |
| Other sequence(s) detected in Swiss-Prot: |
5. |
|
|
|
| Matching PDB structures:
1ABN 1ADS 1AE4 1AFS ... [ALL] |
| ALDOKETO_REDUCTASE_3, PS00063; Aldo/keto reductase family putative active site signature (PATTERN) |
| Consensus pattern: |
[LIVM]-[PAIV]-[KR]-[ST]-{EPQG}-{RFI}-x(2)-R-{SVAF}-x-[GSTAEQK]-[NSL]-x-{LVRI}-[LIVMFA]
K may be the active site residue |
| Sequences known to belong to this class detected by the pattern: |
ALL, except for yafB |
| Other sequence(s) detected in Swiss-Prot: |
41. |
|
|
|
| Matching PDB structures:
1ABN 1ADS 1AE4 1AFS ... [ALL] |
References
| 1 |
Authors |
Bohren K.M., Bullock B., Wermuth B., Gabbay K.H. |
| Title |
The aldo-keto reductase superfamily. cDNAs and deduced amino acid sequences of human aldehyde and aldose reductases. |
| Source |
J. Biol. Chem. 264:9547-9551(1989). |
| PubMed ID |
2498333 |
| 2 |
Authors |
Bruce N.C., Willey D.L., Coulson A.F.M., Jeffery J. |
| Title |
Bacterial morphine dehydrogenase further defines a distinct superfamily of oxidoreductases with diverse functional activities. |
| Source |
Biochem. J. 299:805-811(1994). |
| PubMed ID |
8192670 |
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