dbCAN-seq: a database of CAZyme sequence and annotation

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CAZyme Information: EAW16774.1

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Basic Information help

Species

Aspergillus fischeri

Lineage

Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus fischeri

CAZyme ID

EAW16774.1

CAZy Family

CBM24|CBM24

CAZyme Description

glucan 1,4-alpha-glucosidase, putative

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
620	DS027697\|CGC3	67277.34	5.2602

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AfischeriNRRL181	10668	331117	278	10390

Gene Location

Full Sequence Download help

Enzyme Prediction help

EC	3.2.1.3:94	3.2.1.1:13

CAZyme Signature Domains help

Family	Start	End	Evalue	family coverage
GH15	53	464	5.6e-75	0.9695290858725761
CBM20	518	608	1.5e-21	0.9555555555555556

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
395586	Glyco_hydro_15	1.43e-131	47	465	5	415	Glycosyl hydrolases family 15. In higher organisms this family is represented by phosphorylase kinase subunits.
99886	CBM20_glucoamylase	1.36e-44	512	618	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	1.47e-32	518	614	1	95	Starch binding domain.
215006	CBM_2	2.19e-24	518	606	1	88	Starch binding domain.
119437	CBM20	7.19e-23	520	608	2	88	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.

CAZyme Hits help

Hit ID	E-Value	Query Start	Query End	Hit Start
6.78e-278	9	620	8	616
9.03e-220	35	620	70	679
4.85e-219	25	619	22	616
5.19e-219	4	608	2	606
5.19e-219	4	608	2	606

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
1.22e-278	37	619	11	593	Crystal structure of Penicillium oxalicum Glucoamylase [Penicillium oxalicum 114-2]
2.63e-215	35	620	3	599	Chain A, GLUCOAMYLASE [Trichoderma reesei],2VN7_A Chain A, GLUCOAMYLASE [Trichoderma reesei]
1.07e-208	35	608	4	604	Structure of the catalytic domain of Aspergillus niger Glucoamylase [Aspergillus niger]
5.56e-187	35	501	4	461	Catalytic domain of glucoamylase from aspergillus niger complexed with tris and glycerol [Aspergillus niger]
2.08e-184	35	501	4	460	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
1.24e-207	35	608	28	628	Glucoamylase OS=Aspergillus niger OX=5061 GN=GLAA PE=1 SV=1
1.24e-207	35	608	28	628	Glucoamylase OS=Aspergillus awamori OX=105351 GN=GLAA PE=1 SV=1
1.01e-205	35	619	38	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
3.16e-205	35	608	28	627	Glucoamylase OS=Aspergillus usamii OX=186680 GN=glaA PE=3 SV=1
3.61e-204	35	608	28	627	Glucoamylase I OS=Aspergillus kawachii OX=1069201 GN=gaI PE=1 SV=1

SignalP and Lipop Annotations help

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000633	0.999338	CS pos: 29-30. Pr: 0.9357

TMHMM Annotations help

There is no transmembrane helices in EAW16774.1.