| Analysis | rpsblast_cdd | Start | 86 |
| End | 167 | Strand | + |
| Length | 82 | Note | Gaps:9 |
| Hit Coverage | 82.08 | Hit Length | 106 |
| Hit Pident | 34.48 | E Val | 2e-10 |
| Hit Description | cd05811 CBM20_glucoamylase Glucoamylase (glucan1 4-alpha-glucosidase) C-terminal CBM20 (carbohydrate-binding module family 20) domain. Glucoamylases are inverting exo-acting starch hydrolases that hydrolyze starch and related polysaccharides by releasing the nonreducing end glucose. They are mainly active on alpha-1 4-glycosidic bonds but also have some activity towards 1 6-glycosidic bonds occurring in natural oligosaccharides. The ability of glucoamylases to cleave 1-6-glycosidic binds is called "debranching activity" and is of importance in industrial applications where complete degradation of starch to glucose is needed. Most glucoamylases are multidomain proteins containing an N-terminal catalytic domain a C-terminal CBM20 domain and a highly O-glycosylated linker region that connects the two. The CBM20 domain is found in a large number of starch degrading enzymes including alpha-amylase beta-amylase glucoamylase and CGTase (cyclodextrin glucanotransferase). CBM20 is also present in proteins that have a regulatory role in starch metabolism in plants (e.g. alpha-amylase) or glycogen metabolism in mammals (e.g. laforin). CBM20 folds as an antiparallel beta-barrel structure with two starch binding sites. These two sites are thought to differ functionally with site 1 acting as the initial starch recognition site and site 2 involved in the specific recognition of appropriate regions of starch.. | Hit Pcons | 16.09 |
| Name | Qrob_P0255590.2 |
| Protein Identifier |
Organism . Name |
Score | Score Type | Protein Description | Alias (in v1) | Code Enzyme | Gene Prediction Quality |
|---|---|---|---|---|---|---|---|
| Qrob_P0255590.2 | Quercus robur | 100.0 | egn | (M=4) 2.7.9.5 - Phosphoglucan, water dikinase. | EC:2.7.9.5 | validated |
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