Species | Fusarium proliferatum | |||||||||||
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Lineage | Ascomycota; Sordariomycetes; ; Nectriaceae; Fusarium; Fusarium proliferatum | |||||||||||
CAZyme ID | FPRN_06057-t42_1-p1 | |||||||||||
CAZy Family | CE5 | |||||||||||
CAZyme Description | probable glucan 1,4-alpha-glucosidase | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location |
EC | 3.2.1.3:94 | 1.14.99.55:4 |
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Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH15 | 79 | 489 | 7.9e-79 | 0.9806094182825484 |
CBM20 | 565 | 655 | 1.2e-27 | 0.9666666666666667 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
395586 | Glyco_hydro_15 | 1.76e-138 | 72 | 489 | 2 | 416 | Glycosyl hydrolases family 15. In higher organisms this family is represented by phosphorylase kinase subunits. |
99886 | CBM20_glucoamylase | 5.87e-51 | 565 | 664 | 7 | 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 | 1.66e-35 | 565 | 656 | 1 | 91 | Starch binding domain. |
99883 | CBM20_alpha_amylase | 2.30e-28 | 565 | 664 | 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 | 1.79e-27 | 565 | 652 | 1 | 88 | Starch binding domain. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
0.0 | 1 | 666 | 1 | 666 | |
0.0 | 1 | 666 | 1 | 666 | |
0.0 | 1 | 666 | 1 | 666 | |
0.0 | 1 | 666 | 1 | 666 | |
0.0 | 1 | 666 | 10 | 675 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
1.31e-281 | 61 | 666 | 1 | 599 | Chain A, GLUCOAMYLASE [Trichoderma reesei],2VN7_A Chain A, GLUCOAMYLASE [Trichoderma reesei] |
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2.18e-225 | 60 | 665 | 1 | 616 | Structure of the catalytic domain of Aspergillus niger Glucoamylase [Aspergillus niger] |
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1.00e-202 | 65 | 665 | 11 | 593 | Crystal structure of Penicillium oxalicum Glucoamylase [Penicillium oxalicum 114-2] |
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2.97e-193 | 60 | 530 | 1 | 468 | Catalytic domain of glucoamylase from aspergillus niger complexed with tris and glycerol [Aspergillus niger] |
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3.40e-192 | 60 | 530 | 1 | 467 | 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 |
---|---|---|---|---|---|---|
1.26e-263 | 26 | 665 | 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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6.37e-225 | 55 | 665 | 20 | 640 | Glucoamylase OS=Aspergillus awamori OX=105351 GN=GLAA PE=1 SV=1 |
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6.37e-225 | 55 | 665 | 20 | 640 | Glucoamylase OS=Aspergillus niger OX=5061 GN=GLAA PE=1 SV=1 |
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4.98e-224 | 55 | 665 | 20 | 639 | Glucoamylase OS=Aspergillus usamii OX=186680 GN=glaA PE=3 SV=1 |
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1.12e-223 | 55 | 665 | 23 | 612 | Glucoamylase OS=Aspergillus oryzae (strain ATCC 42149 / RIB 40) OX=510516 GN=glaA PE=2 SV=2 |
Other | SP_Sec_SPI | CS Position |
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1.000063 | 0.000004 |
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