CAZyme Information: P170DRAFT_411426-t37_1-p1

Basic Information

• Species: Aspergillus steynii
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus steynii
• CAZyme ID: P170DRAFT_411426-t37_1-p1
• CAZy Family: GH18
• CAZyme Description: putative glucan 1,4-alpha-glucosidase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
611		65262.85	5.0749

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AsteyniiIBT23096	13430	1392250	235	13195

• Gene Location: location=MSFO01000005:3165781-3167910(-)

Full Sequence      

MKALNLLLALVSPSLAIPSLSPRQSSLDTWLTQEAEISRTAILNNIGADGAWVPGARAGV
VIASPSRNDPDYFYTWTRDSGLVLKTLIDLFRTGDTTLLPTIEQFVTSQARIQGVSNPSG
DLASGAGLGEAKFNADESAFTGGWGRPQRDGPALRATALVGLGQWLVENGYTTVAKEIVW
PIARNDLSYVAQYWNQTGFDLWEEVQGSSFFTIAVSHRALVEGSTFAQSVGASCPYCDSQ
APQIRCYLQSFWSGTGKYILANFGGGRTGKDANTLLGSIHTFDPAAGCDDVTFQPCSPRA
LANHKAVTDSFRSIYAINSERKANEAVAVGRYAEDVYYGGNPWFLTTLAAAEQLYDALYQ
WEKLGELRITDVSLPFFQALDSSASVGSYAASSAKYTSLVNAVKAYADGYVGVVQTYAAS
NGSMAEQITRSDGKQTSARDLTWSYAALLTANNRRNAVMPPSWGEPAATSLPTKCSATSA
TGTYSSVAVTSWPPIGDTPGTSIPCVSPTAVAVTFEVTATTTWGQDVKVVGSTAELGSWS
PSAAIALSADRYTSSNPLWFGTVNVPVGKTIEYKYIRVQNGAVTWESDPNRSLRVEGGCG
VSGKVQKDSWR

Enzyme Prediction     

EC	3.2.1.3:94	1.14.99.55:4

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH15	46	451	3.7e-77	0.9722991689750693
CBM20	511	598	2.6e-29	0.9444444444444444

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
395586	Glyco_hydro_15	5.27e-150	36	453	1	417	Glycosyl hydrolases family 15. In higher organisms this family is represented by phosphorylase kinase subunits.
99886	CBM20_glucoamylase	3.84e-47	505	610	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	2.93e-37	511	602	1	92	Starch binding domain.
99883	CBM20_alpha_amylase	1.39e-31	511	611	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	1.74e-27	513	595	2	84	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
QRD92849.1|CBM20|GH15	0.0	8	611	11	612
QCL08961.1|CBM20|GH15	0.0	8	611	11	612
CAY05395.1|CBM20|GH15|3.2.1.3	0.0	8	611	11	612
BAE66563.1|CBM20|GH15|3.2.1.3	0.0	8	611	11	612
ABA62323.1|CBM20|GH15|3.2.1.3	0.0	8	611	11	612

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6FRV_A	1.75e-293	25	611	1	616	Structure of the catalytic domain of Aspergillus niger Glucoamylase [Aspergillus niger]
3EQA_A	3.02e-260	25	495	1	469	Catalytic domain of glucoamylase from aspergillus niger complexed with tris and glycerol [Aspergillus niger]
1AGM_A	4.28e-260	25	495	1	468	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	4.44e-260	25	495	1	468	GLUCOAMYLASE-471 COMPLEXED WITH ACARBOSE [Aspergillus awamori]
1GAI_A	4.61e-260	25	495	1	468	GLUCOAMYLASE-471 COMPLEXED WITH D-GLUCO-DIHYDROACARBOSE [Aspergillus awamori]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|P36914|AMYG_ASPOR	0.0	8	611	11	612	Glucoamylase OS=Aspergillus oryzae (strain ATCC 42149 / RIB 40) OX=510516 GN=glaA PE=2 SV=2
sp|P22832|AMYG_ASPUS	2.70e-295	2	611	4	639	Glucoamylase OS=Aspergillus usamii OX=186680 GN=glaA PE=3 SV=1
sp|P23176|AMYG_ASPKA	5.43e-295	23	611	23	639	Glucoamylase I OS=Aspergillus kawachii OX=1069201 GN=gaI PE=1 SV=1
sp|P69327|AMYG_ASPAW	7.55e-293	23	611	23	640	Glucoamylase OS=Aspergillus awamori OX=105351 GN=GLAA PE=1 SV=1
sp|P69328|AMYG_ASPNG	7.55e-293	23	611	23	640	Glucoamylase OS=Aspergillus niger OX=5061 GN=GLAA PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000324	0.999660	CS pos: 23-24. Pr: 0.9664

TMHMM  Annotations     

There is no transmembrane helices in P170DRAFT_411426-t37_1-p1.