| Analysis | rpsblast_cdd | Start | 15 |
| End | 278 | Strand | + |
| Length | 264 | Note | Gaps:71 |
| Hit Coverage | 66.98 | Hit Length | 318 |
| Hit Pident | 32.39 | E Val | 5e-13 |
| Hit Description | cd05228 AR_FR_like_1_SDR_e uncharacterized subgroup of aldehyde reductase and flavonoid reductase related proteins extended (e) SDRs. This subgroup contains proteins of unknown function related to aldehyde reductase and flavonoid reductase of the extended SDR-type. Aldehyde reductase I (aka carbonyl reductase) is an NADP-binding SDR it has an NADP-binding motif consensus that is slightly different from the canonical SDR form and lacks the Asn of the extended SDR active site tetrad. Aldehyde reductase I catalyzes the NADP-dependent reduction of ethyl 4-chloro-3-oxobutanoate to ethyl (R)-4-chloro-3-hydroxybutanoate. The related flavonoid reductases act in the NADP-dependent reduction of flavonoids ketone-containing plant secondary metabolites. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins and include isomerases epimerases oxidoreductases and lyases they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold an NAD(P)(H)-binding region and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range they catalyze a wide range of activities including the metabolism of steroids cofactors carbohydrates lipids aromatic compounds and amino acids and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151 human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys there is often an upstream Ser and/or an Asn contributing to the active site while substrate binding is in the C-terminal region which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys a water molecule stabilized by Asn and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. | Hit Pcons | 12.21 |
| Name | Qrob_P0088120.2 |
| Protein Identifier |
Organism . Name |
Score | Score Type | Protein Description | Alias (in v1) | Code Enzyme | Gene Prediction Quality |
|---|---|---|---|---|---|---|---|
| Qrob_P0088120.2 | Quercus robur | 90.2 | egn | (M=3) K07748 - sterol-4alpha-carboxylate 3-dehydrogenase (decarboxylating) [EC:1.1.1.170] | EC:1.1.1.170 | validated |
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