CAZyme Information: Afu4g10140-T-p1

Basic Information

• Species: Aspergillus fumigatus
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus fumigatus
• CAZyme ID: Afu4g10140-T-p1
• CAZy Family: GH3
• CAZyme Description: Has domain(s) with predicted catalytic activity, glucan 1,4-alpha-glucosidase activity, hydrolase activity, hydrolyzing O-glycosyl compounds, starch binding activity and role in polysaccharide metabolic process

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
352	Chr4_A_fumigatus_Af293|CGC10	38477.44	4.6331

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AfumigatusAf293	10130	330879	290	9840

• Gene Location: location=Chr4_A_fumigatus_Af293:2642836-2644013(+)

Full Sequence      

MQQEGVSGGSSLSVLECDRSASRFNFPYFPTIIIIIIIIIITVIYSRQSSIRACESCACE
AVSIRLDEMKDETPRMTEMTRKPFLTIAIGVLTTVSALSDPAQIVIPATITPQTTDPLVS
WLAQETSYALDGVLNNVGPNGAKATGASSGIIIASPSQSNPDYYYTWTRDAALTVKYLVG
SFAADHDPAIQRIIEDYVESQAHLQTVSNPSGNLSSGGLGEPKLRVDGSAFHGSWGRPQS
DGPALRATTLISYANLMIDNGYFSTVESSIWPIIQNDLSYLTEFWNSSTFGTFVCFSYGR
TVMLDAGEEFEYKFIRKRVGDGKVIWEEGQNRAFVVPRECGPSNATINAVWR

Enzyme Prediction     

EC	3.2.1.3:94

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH15	134	291	1.9e-29	0.4155124653739612

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
395586	Glyco_hydro_15	6.29e-50	129	291	3	169	Glycosyl hydrolases family 15. In higher organisms this family is represented by phosphorylase kinase subunits.
99886	CBM20_glucoamylase	4.11e-15	301	351	58	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	2.39e-10	301	346	51	95	Starch binding domain.
99883	CBM20_alpha_amylase	7.72e-08	301	352	48	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.
119437	CBM20	1.49e-07	302	351	51	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CAC28076.1|CBM20|GH15|3.2.1.3	1.38e-70	108	290	22	203
ABH92242.1|CBM20|GH15|3.2.1.3	1.38e-70	108	290	22	203
CAY05394.1|CBM20|GH15|3.2.1.3	1.38e-70	108	290	22	203
AAR61400.1|CBM20|GH15|3.2.1.3	1.38e-70	108	290	22	203
ABH92239.1|CBM20|GH15|3.2.1.3	1.65e-69	115	290	2	176

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1AGM_A	3.31e-60	118	288	3	172	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]
1GAH_A	3.38e-60	118	288	3	172	GLUCOAMYLASE-471 COMPLEXED WITH ACARBOSE [Aspergillus awamori]
1GAI_A	3.46e-60	118	288	3	172	GLUCOAMYLASE-471 COMPLEXED WITH D-GLUCO-DIHYDROACARBOSE [Aspergillus awamori]
3EQA_A	6.96e-59	118	288	3	173	Catalytic domain of glucoamylase from aspergillus niger complexed with tris and glycerol [Aspergillus niger]
6FRV_A	1.15e-57	118	288	3	173	Structure of the catalytic domain of Aspergillus niger Glucoamylase [Aspergillus niger]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|P23176|AMYG_ASPKA	1.60e-58	118	288	27	196	Glucoamylase I OS=Aspergillus kawachii OX=1069201 GN=gaI PE=1 SV=1
sp|P36914|AMYG_ASPOR	1.47e-57	118	290	30	201	Glucoamylase OS=Aspergillus oryzae (strain ATCC 42149 / RIB 40) OX=510516 GN=glaA PE=2 SV=2
sp|P22832|AMYG_ASPUS	1.63e-57	118	288	27	196	Glucoamylase OS=Aspergillus usamii OX=186680 GN=glaA PE=3 SV=1
sp|P69327|AMYG_ASPAW	8.66e-57	118	288	27	197	Glucoamylase OS=Aspergillus awamori OX=105351 GN=GLAA PE=1 SV=1
sp|P69328|AMYG_ASPNG	8.66e-57	118	288	27	197	Glucoamylase OS=Aspergillus niger OX=5061 GN=GLAA PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000055	0.000009

TMHMM  Annotations     

Start	End
24	46
84	106