Species | Coccidioides immitis | |||||||||||
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Lineage | Ascomycota; Eurotiomycetes; ; Onygenaceae; Coccidioides; Coccidioides immitis | |||||||||||
CAZyme ID | TPX25657.1 | |||||||||||
CAZy Family | GT39 | |||||||||||
CAZyme Description | Glucoamylase [Source:UniProtKB/TrEMBL;Acc:A0A6C1M536] | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location |
EC | 3.2.1.3:94 | 3.2.1.3:71 |
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Family | Start | End | Evalue | family coverage |
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GH15 | 48 | 455 | 6.6e-80 | 0.9861495844875346 |
CBM20 | 518 | 607 | 3.9e-27 | 0.9555555555555556 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
395586 | Glyco_hydro_15 | 3.26e-136 | 45 | 455 | 3 | 415 | Glycosyl hydrolases family 15. In higher organisms this family is represented by phosphorylase kinase subunits. |
99886 | CBM20_glucoamylase | 2.22e-47 | 516 | 618 | 5 | 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 | 2.93e-34 | 518 | 611 | 1 | 93 | Starch binding domain. |
99883 | CBM20_alpha_amylase | 7.75e-30 | 518 | 619 | 1 | 95 | 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 | 6.15e-25 | 518 | 605 | 1 | 88 | Starch binding domain. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
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2.42e-273 | 34 | 619 | 43 | 646 | |
1.45e-272 | 22 | 619 | 20 | 618 | |
1.45e-272 | 22 | 619 | 20 | 618 | |
1.45e-272 | 22 | 619 | 20 | 618 | |
1.45e-272 | 22 | 619 | 20 | 618 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
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6.87e-247 | 33 | 619 | 2 | 616 | Structure of the catalytic domain of Aspergillus niger Glucoamylase [Aspergillus niger] |
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1.64e-218 | 33 | 498 | 2 | 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] |
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1.70e-218 | 33 | 498 | 2 | 467 | GLUCOAMYLASE-471 COMPLEXED WITH ACARBOSE [Aspergillus awamori] |
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1.76e-218 | 33 | 498 | 2 | 467 | GLUCOAMYLASE-471 COMPLEXED WITH D-GLUCO-DIHYDROACARBOSE [Aspergillus awamori] |
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2.54e-215 | 33 | 619 | 1 | 598 | Chain A, GLUCOAMYLASE [Trichoderma reesei],2VN7_A Chain A, GLUCOAMYLASE [Trichoderma reesei] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
8.23e-263 | 17 | 619 | 10 | 610 | Glucoamylase ARB_02327-1 OS=Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) OX=663331 GN=ARB_02327-1 PE=1 SV=1 |
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1.57e-258 | 28 | 619 | 24 | 612 | Glucoamylase OS=Aspergillus oryzae (strain ATCC 42149 / RIB 40) OX=510516 GN=glaA PE=2 SV=2 |
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1.58e-250 | 28 | 619 | 21 | 639 | Glucoamylase OS=Aspergillus usamii OX=186680 GN=glaA PE=3 SV=1 |
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5.98e-248 | 28 | 619 | 21 | 639 | Glucoamylase I OS=Aspergillus kawachii OX=1069201 GN=gaI PE=1 SV=1 |
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5.80e-246 | 28 | 619 | 21 | 640 | Glucoamylase OS=Aspergillus awamori OX=105351 GN=GLAA PE=1 SV=1 |
Other | SP_Sec_SPI | CS Position |
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0.007838 | 0.992146 | CS pos: 24-25. Pr: 0.8133 |
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