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CAZyme Information: ATY62564.1
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Basic Information |
Genomic context |
Full Sequence |
Enzyme annotations |
CAZy signature domains |
CDD domains |
CAZyme hits |
PDB hits |
Swiss-Prot hits |
SignalP and Lipop annotations |
TMHMM annotations
Basic Information help
| Species | Cordyceps militaris | |||||||||||
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| Lineage | Ascomycota; Sordariomycetes; ; Cordycipitaceae; Cordyceps; Cordyceps militaris | |||||||||||
| CAZyme ID | ATY62564.1 | |||||||||||
| CAZy Family | GH18|CBM66 | |||||||||||
| CAZyme Description | glucoamylase I precursor | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | ||||||||||||
Enzyme Prediction help
| EC | 3.2.1.3:94 | 3.2.1.1:13 |
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CAZyme Signature Domains help
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| GH15 | 70 | 481 | 1.7e-79 | 0.9833795013850416 |
| CBM20 | 550 | 641 | 6.7e-29 | 0.9777777777777777 |
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| 395586 | Glyco_hydro_15 | 1.09e-143 | 64 | 482 | 1 | 416 | Glycosyl hydrolases family 15. In higher organisms this family is represented by phosphorylase kinase subunits. |
| 99886 | CBM20_glucoamylase | 2.53e-49 | 544 | 649 | 1 | 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 | 5.81e-38 | 550 | 644 | 1 | 94 | Starch binding domain. |
| 99883 | CBM20_alpha_amylase | 8.33e-30 | 550 | 649 | 1 | 94 | Alpha-amylase, C-terminal CBM20 (carbohydrate-binding module, family 20) domain. This domain is found in several bacterial and fungal alpha-amylases including the maltopentaose-forming amylases (G5-amylases). Most alpha-amylases have, in addition to the C-terminal CBM20 domain, an N-terminal catalytic domain belonging to glycosyl hydrolase family 13, which hydrolyzes internal alpha-1,4-glucosidic bonds in starch and related saccharides, yielding maltotriose and maltose. Two types of soluble substrates are used by alpha-amylases including long substrates (e.g. amylose) and short substrates (e.g. maltodextrins or maltooligosaccharides). 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. |
| 215006 | CBM_2 | 2.45e-27 | 550 | 637 | 1 | 88 | Starch binding domain. |
CAZyme Hits help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| 0.0 | 1 | 650 | 1 | 650 | |
| 2.19e-301 | 5 | 650 | 18 | 674 | |
| 5.88e-301 | 5 | 650 | 9 | 653 | |
| 1.73e-298 | 3 | 650 | 7 | 665 | |
| 1.73e-298 | 3 | 650 | 7 | 665 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 3.10e-283 | 54 | 650 | 1 | 598 | Chain A, GLUCOAMYLASE [Trichoderma reesei],2VN7_A Chain A, GLUCOAMYLASE [Trichoderma reesei] |
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| 2.13e-221 | 55 | 650 | 3 | 616 | Structure of the catalytic domain of Aspergillus niger Glucoamylase [Aspergillus niger] |
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| 5.44e-206 | 54 | 650 | 7 | 593 | Crystal structure of Penicillium oxalicum Glucoamylase [Penicillium oxalicum 114-2] |
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| 1.21e-193 | 55 | 518 | 3 | 462 | Catalytic domain of glucoamylase from aspergillus niger complexed with tris and glycerol [Aspergillus niger] |
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| 2.43e-193 | 55 | 518 | 3 | 461 | 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] |
Swiss-Prot Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 1.56e-272 | 22 | 650 | 1 | 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 |
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| 1.13e-223 | 33 | 650 | 5 | 639 | Glucoamylase OS=Aspergillus usamii OX=186680 GN=glaA PE=3 SV=1 |
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| 3.10e-221 | 33 | 650 | 5 | 640 | Glucoamylase OS=Aspergillus niger OX=5061 GN=GLAA PE=1 SV=1 |
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| 3.10e-221 | 33 | 650 | 5 | 640 | Glucoamylase OS=Aspergillus awamori OX=105351 GN=GLAA PE=1 SV=1 |
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| 1.21e-220 | 33 | 650 | 5 | 639 | Glucoamylase I OS=Aspergillus kawachii OX=1069201 GN=gaI PE=1 SV=1 |
SignalP and Lipop Annotations help
This protein is predicted as OTHER
| Other | SP_Sec_SPI | CS Position |
|---|---|---|
| 0.587776 | 0.412215 |