| Analysis | rpsblast_cdd | Start | 12 |
| End | 315 | Strand | + |
| Length | 304 | Note | Gaps:58 |
| Hit Coverage | 77.34 | Hit Length | 331 |
| Hit Pident | 38.28 | E Val | 2e-45 |
| Hit Description | cd05241 3b-HSD-like_SDR_e 3beta-hydroxysteroid dehydrogenases (3b-HSD)-like extended (e) SDRs. Extended SDR family domains belonging to this subgroup have the characteristic active site tetrad and a fairly well-conserved NAD(P)-binding motif. 3b-HSD catalyzes the NAD-dependent conversion of various steroids such as pregnenolone to progesterone or androstenediol to testosterone. This subgroup includes an unusual bifunctional 3b-HSD/C-4 decarboxylase from Arabidopsis thaliana and Saccharomyces cerevisiae ERG26 a 3b-HSD/C-4 decarboxylase involved in the synthesis of ergosterol the major sterol of yeast. It also includes human 3 beta-HSD/HSD3B1 and C(27) 3beta-HSD/ [3beta-hydroxy-delta(5)-C(27)-steroid oxidoreductase HSD3B7]. C(27) 3beta-HSD/HSD3B7 is a membrane-bound enzyme of the endoplasmic reticulum that catalyzes the isomerization and oxidation of 7alpha-hydroxylated sterol intermediates an early step in bile acid biosynthesis. Mutations in the human NSDHL (NAD(P)H steroid dehydrogenase-like protein) cause CHILD syndrome (congenital hemidysplasia with ichthyosiform nevus and limb defects) an X-linked dominant male-lethal trait. Mutations in the human gene encoding C(27) 3beta-HSD underlie a rare autosomal recessive form of neonatal cholestasis. 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 sythase 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 | 19.92 |
| 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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