| Analysis | rpsblast_cdd | Start | 87 |
| End | 399 | Strand | + |
| Length | 313 | Note | Gaps:2 |
| Hit Coverage | 100.00 | Hit Length | 311 |
| Hit Pident | 76.53 | E Val | 1e-157 |
| Hit Description | cd09810 LPOR_like_SDR_c_like light-dependent protochlorophyllide reductase (LPOR)-like classical (c)-like SDRs. Classical SDR-like subgroup containing LPOR and related proteins. Protochlorophyllide (Pchlide) reductases act in chlorophyll biosynthesis. There are distinct enzymes that catalyze Pchlide reduction in light or dark conditions. Light-dependent reduction is via an NADP-dependent SDR LPOR. Proteins in this subfamily share the glycine-rich NAD-binding motif of the classical SDRs have a partial match to the canonical active site tetrad but lack the typical active site Ser. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet) an NAD(P)(H)-binding region and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes 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 (15-PGDH) numbering). In addition to the Tyr and Lys there is often an upstream Ser (Ser-138 15-PGDH numbering) and/or an Asn (Asn-107 15-PGDH numbering) 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. Extended SDRs have additional elements in the C-terminal region and typically have a TGXXGXXG cofactor binding motif. 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. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization decarboxylation epimerization C N bond reduction dehydratase activity dehalogenation Enoyl-CoA reduction and carbonyl-alcohol oxidoreduction. | Hit Pcons | 10.61 |
| Name | Qrob_P0446560.2 |
| Protein Identifier |
Organism . Name |
Score | Score Type | Protein Description | Alias (in v1) | Code Enzyme | Gene Prediction Quality |
|---|---|---|---|---|---|---|---|
| Qrob_P0446560.2 | Quercus robur | 99.0 | egn | (M=1) 1.3.1.33 - Protochlorophyllide reductase. | EC:1.3.1.33 | validated |
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