Species | Blumeria graminis | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Ascomycota; Leotiomycetes; ; Erysiphaceae; Blumeria; Blumeria graminis | |||||||||||
CAZyme ID | VDB93054.1 | |||||||||||
CAZy Family | GT2|GT2 | |||||||||||
CAZyme Description | unspecified product | |||||||||||
CAZyme Property |
|
|||||||||||
Genome Property |
|
|||||||||||
Gene Location |
EC | 3.2.1.3:94 | 1.14.99.55:4 |
---|
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH15 | 98 | 482 | 4.5e-73 | 0.889196675900277 |
CBM20 | 511 | 593 | 1.2e-21 | 0.8777777777777778 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
395586 | Glyco_hydro_15 | 2.44e-118 | 98 | 482 | 36 | 416 | Glycosyl hydrolases family 15. In higher organisms this family is represented by phosphorylase kinase subunits. |
99886 | CBM20_glucoamylase | 1.47e-36 | 509 | 602 | 13 | 106 | 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. |
395557 | CBM_20 | 2.24e-27 | 509 | 598 | 7 | 95 | Starch binding domain. |
119437 | CBM20 | 4.83e-21 | 511 | 602 | 8 | 96 | The family 20 carbohydrate-binding module (CBM20), also known as the starch-binding 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. |
215006 | CBM_2 | 4.98e-21 | 508 | 590 | 7 | 88 | Starch binding domain. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
0.0 | 1 | 605 | 1 | 605 | |
1.11e-213 | 98 | 603 | 113 | 676 | |
4.77e-213 | 98 | 603 | 113 | 678 | |
1.13e-210 | 98 | 602 | 82 | 645 | |
2.82e-210 | 98 | 602 | 109 | 672 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
2.44e-204 | 98 | 603 | 46 | 598 | Chain A, GLUCOAMYLASE [Trichoderma reesei],2VN7_A Chain A, GLUCOAMYLASE [Trichoderma reesei] |
|
1.28e-195 | 98 | 603 | 47 | 616 | Structure of the catalytic domain of Aspergillus niger Glucoamylase [Aspergillus niger] |
|
2.42e-182 | 99 | 592 | 53 | 582 | Crystal structure of Penicillium oxalicum Glucoamylase [Penicillium oxalicum 114-2] |
|
2.39e-174 | 98 | 493 | 47 | 437 | Catalytic domain of glucoamylase from aspergillus niger complexed with tris and glycerol [Aspergillus niger] |
|
2.52e-171 | 98 | 493 | 47 | 436 | Refined structure for the complex of acarbose with glucoamylase from Aspergillus awamori var. x100 to 2.4 angstroms resolution [Aspergillus awamori],1DOG_A REFINED STRUCTURE FOR THE COMPLEX OF 1-DEOXYNOJIRIMYCIN WITH GLUCOAMYLASE FROM (ASPERGILLUS AWAMORI) VAR. X100 TO 2.4 ANGSTROMS RESOLUTION [Aspergillus awamori],1GLM_A REFINED CRYSTAL STRUCTURES OF GLUCOAMYLASE FROM ASPERGILLUS AWAMORI VAR. X100 [Aspergillus awamori],3GLY_A REFINED CRYSTAL STRUCTURES OF GLUCOAMYLASE FROM ASPERGILLUS AWAMORI VAR. X100 [Aspergillus awamori] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
8.03e-196 | 98 | 603 | 81 | 626 | Glucoamylase OS=Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987) OX=367110 GN=gla-1 PE=1 SV=3 |
|
1.46e-194 | 98 | 603 | 71 | 640 | Glucoamylase OS=Aspergillus awamori OX=105351 GN=GLAA PE=1 SV=1 |
|
1.46e-194 | 98 | 603 | 71 | 640 | Glucoamylase OS=Aspergillus niger OX=5061 GN=GLAA PE=1 SV=1 |
|
4.81e-190 | 98 | 603 | 71 | 639 | Glucoamylase OS=Aspergillus usamii OX=186680 GN=glaA PE=3 SV=1 |
|
1.10e-188 | 98 | 603 | 71 | 639 | Glucoamylase I OS=Aspergillus kawachii OX=1069201 GN=gaI PE=1 SV=1 |
Other | SP_Sec_SPI | CS Position |
---|---|---|
1.000062 | 0.000000 |
Copyright 2022 © YIN LAB, UNL. All rights reserved. Designed by Jinfang Zheng and Boyang Hu. Maintained by Yanbin Yin.