CAZyme Information: THC96494.1

Basic Information

• Species: Aspergillus tanneri
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus tanneri
• CAZyme ID: THC96494.1
• CAZy Family: GH71
• CAZyme Description: 1,4-alpha-D-glucan glucohydrolase [Source:UniProtKB/TrEMBL;Acc:A0A4V3UPU3]

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
547	SOSA01000111|CGC1	59704.03	4.6478

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AtanneriNIH1004	13590	N/A	33	13557

• Gene Location: location=SOSA01000111:27388-29518(+)

Full Sequence      

MLVSVLVLSLFRTANASPAQIVLSGTTRSNPSLDSWLLAEIPEALDGVLNNIGADGAKAT
GARSGSVVASPNTKDPNYYYTWTRDAALTARCLVDIVVSSADPTLQSAVQDYISFQADLQ
AVSNPSGGLLSGGLGEPKFNVDGSAFTDSWGRPQRDGPALRAMTLMAYSNWLIDRNQSSL
AQTIWPIIRNDLSYVSEYWNSSTYDLWEEQNGSSFFTSAVQYRALSDGASLADRLNLSCP
NCLSQAPQTLCFLQYFWSPSDAFILSNLSPTASPGPNVTSPRSGKDINSILASIHTFNPT
SPCDDTTFQPCSSRALANLKSVVDAFRPLYDINRGIPSSHAIALGRYPEDVYQGGHPWYL
CTLAAAQLLYQAVSQWKYLGFVTIERTSLAFFRDVYPSARVGSYPSSERVYAEILDAVMV
LGDGYLGVVQKYTPSNGALAEQFSRDSGAPVSATDLTWSPLGEDVFLVGSVTQLGEWDVN
RAVPLDAHQYGVVSLWFTRVSLPVGMELEYKFFMRVGGKVVWESGLNRELQVRESCKNVS
MNAVWRD

Enzyme Prediction     

EC	3.2.1.3:94	1.14.99.55:4

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH15	48	459	4.2e-77	0.96398891966759
CBM20	460	537	5.8e-18	0.8444444444444444

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
395586	Glyco_hydro_15	9.17e-114	44	459	3	408	Glycosyl hydrolases family 15. In higher organisms this family is represented by phosphorylase kinase subunits.
395557	CBM_20	6.06e-22	461	540	13	93	Starch binding domain.
99886	CBM20_glucoamylase	3.55e-19	462	545	20	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.
99883	CBM20_alpha_amylase	8.60e-16	451	546	7	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	1.20e-15	461	545	12	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	9.73e-190	28	536	27	606
ABH92242.1|CBM20|GH15|3.2.1.3	9.73e-190	28	536	27	606
CAY05394.1|CBM20|GH15|3.2.1.3	9.73e-190	28	536	27	606
AAR61400.1|CBM20|GH15|3.2.1.3	9.73e-190	28	536	27	606
ABH92239.1|CBM20|GH15|3.2.1.3	4.51e-189	32	536	4	579

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6FHV_A	9.07e-167	32	546	7	593	Crystal structure of Penicillium oxalicum Glucoamylase [Penicillium oxalicum 114-2]
6FRV_A	1.48e-165	32	546	2	616	Structure of the catalytic domain of Aspergillus niger Glucoamylase [Aspergillus niger]
1AGM_A	1.31e-161	32	459	2	417	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	1.35e-161	32	459	2	417	GLUCOAMYLASE-471 COMPLEXED WITH ACARBOSE [Aspergillus awamori]
1GAI_A	1.40e-161	32	459	2	417	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|P0DN29|AMYG_ARTBC	6.88e-167	28	536	22	598	Glucoamylase ARB_02327-1 OS=Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) OX=663331 GN=ARB_02327-1 PE=1 SV=1
sp|P36914|AMYG_ASPOR	4.74e-165	28	546	25	612	Glucoamylase OS=Aspergillus oryzae (strain ATCC 42149 / RIB 40) OX=510516 GN=glaA PE=2 SV=2
sp|P69327|AMYG_ASPAW	8.17e-165	23	546	17	640	Glucoamylase OS=Aspergillus awamori OX=105351 GN=GLAA PE=1 SV=1
sp|P69328|AMYG_ASPNG	8.17e-165	23	546	17	640	Glucoamylase OS=Aspergillus niger OX=5061 GN=GLAA PE=1 SV=1
sp|P22832|AMYG_ASPUS	4.49e-164	23	546	17	639	Glucoamylase OS=Aspergillus usamii OX=186680 GN=glaA PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000271	0.999671	CS pos: 16-17. Pr: 0.9783

TMHMM  Annotations     

There is no transmembrane helices in THC96494.1.