CAZyme Information: ODM22587.1

Basic Information

• Species: Aspergillus cristatus
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus cristatus
• CAZyme ID: ODM22587.1
• CAZy Family: GT22
• CAZyme Description: Glucoamylase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
632	JXNT01000001|CGC31	67410.30	4.5430

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AcristatusGZAAS20.1005	10344	N/A	0	10344

• Gene Location: location=JXNT01000001:460042-462149(-)

Full Sequence      

MAPRFWTALYALALGHAVVAAPQLAARATTSLDTWLASETTVAREGILNNIGSSGAYAAS
AKPGIVIASPSTSNPNYYYTWTRDSALTMKVLVELFKNGDTSLQNVIEEYINSQAYLQTV
SNPSGDLSSGGLAEPKFNVDETAFTDAWGRPQRDGPALRATTLIDFGQWLIANGYTTQAT
QIVWPVVRNDLSYVAQYWNNTGFDLWEEVRGSSFFTIAVQHRALVEGSKFATQVGSSCSY
CDSQAPQVLCFLQSFWTGSYTLANFGSSRSGKDANTLLGSIHTFDPEAGCDDSTFQPCSA
RALANHKVVTDSFRSIYTLNSGIAAGSAVAIGRYPEDSYYNGNPWYLCTLAAAELLYDAV
YQWNRIGSLTIDSVSLGFFKDLYSSAATGTYSSSSATYSSIVSAVKTYADGYVSIVEKYA
MTNGSMSEQFSKSDGSLMSARDLTWSYAALLTANMRRNSVVPAAWGETSASGVPATCSAT
SATGTYSTATNTNWPGTLTSGTSATTTTGGTGGTTTTSTTTTTACTTPTSVAVTFDLTAT
TGYGENIKLSGSIPALGSWDTDNAVPMSADKYTSSDHLWYVAVDLPAGTSFQYKYIRVES
DGSIQWESDPNNSYTVPAACGTTTATHTDSWR

Enzyme Prediction     

EC	3.2.1.3:94	3.2.1.3:71

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH15	49	453	6.3e-82	0.9778393351800554
CBM20	531	622	1.3e-29	0.9777777777777777

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
395586	Glyco_hydro_15	2.25e-147	42	454	2	416	Glycosyl hydrolases family 15. In higher organisms this family is represented by phosphorylase kinase subunits.
99886	CBM20_glucoamylase	2.63e-48	531	631	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	6.24e-41	531	626	1	95	Starch binding domain.
99883	CBM20_alpha_amylase	7.35e-34	531	632	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.
119437	CBM20	5.54e-29	533	631	2	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
CAP92732.1|CBM20|GH15	3.26e-316	1	632	1	631
AYA22369.1|CBM20|GH15	9.18e-315	1	632	1	636
UPX44868.1|CBM20|GH15	1.75e-313	1	632	1	640
QQK46372.1|CBM20|GH15	1.40e-305	5	632	5	640
EDP53734.1|CBM20|GH15	5.88e-293	3	632	2	631

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6FRV_A	1.08e-285	31	632	2	616	Structure of the catalytic domain of Aspergillus niger Glucoamylase [Aspergillus niger]
1AGM_A	8.84e-246	31	471	2	442	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	9.17e-246	31	471	2	442	GLUCOAMYLASE-471 COMPLEXED WITH ACARBOSE [Aspergillus awamori]
1GAI_A	9.51e-246	31	471	2	442	GLUCOAMYLASE-471 COMPLEXED WITH D-GLUCO-DIHYDROACARBOSE [Aspergillus awamori]
3EQA_A	5.53e-242	31	471	2	443	Catalytic domain of glucoamylase from aspergillus niger complexed with tris and glycerol [Aspergillus niger]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|P22832|AMYG_ASPUS	6.37e-285	31	632	26	639	Glucoamylase OS=Aspergillus usamii OX=186680 GN=glaA PE=3 SV=1
sp|P69327|AMYG_ASPAW	1.33e-284	31	632	26	640	Glucoamylase OS=Aspergillus awamori OX=105351 GN=GLAA PE=1 SV=1
sp|P69328|AMYG_ASPNG	1.33e-284	31	632	26	640	Glucoamylase OS=Aspergillus niger OX=5061 GN=GLAA PE=1 SV=1
sp|P23176|AMYG_ASPKA	1.40e-281	31	632	26	639	Glucoamylase I OS=Aspergillus kawachii OX=1069201 GN=gaI PE=1 SV=1
sp|P36914|AMYG_ASPOR	7.59e-265	5	632	4	612	Glucoamylase OS=Aspergillus oryzae (strain ATCC 42149 / RIB 40) OX=510516 GN=glaA PE=2 SV=2

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000303	0.999659	CS pos: 27-28. Pr: 0.9571

TMHMM  Annotations     

There is no transmembrane helices in ODM22587.1.