CAZyme Information: EEQ33548.1

Basic Information

• Species: Microsporum canis
• Lineage: Ascomycota; Eurotiomycetes; ; Arthrodermataceae; Microsporum; Microsporum canis
• CAZyme ID: EEQ33548.1
• CAZy Family: GT2
• CAZyme Description: glucoamylase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
611		67911.38	5.5558

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_McanisCBS113480	8847	554155	82	8765

• Gene Location: location=DS995706:619149-621234(-)

Full Sequence      

MRLTSRLWSSLLVFPAVIAFQARFRTPAEFVLDTVDDGTLQSMLDNIGLNGSNAWDTRPG
LVIASPSRRDPDYFFTWTRDSALVLKYIVDAFAAGNTGLQGAIQEYISSQARIQLLNTRS
GGLSSGGLGEPKYQVDETPYMEDWGRPQADGPALRATAMIEYARWLLANGYYDVAKSIVW
PVVKNDLSYISERWNTSAFDLWEEVNGPSFFTTIVQHRALVEGGNMARALDETCPHCESQ
APQVLCYLQSYWTGTAVRSNYGQGRSGLDVASILGSIHTFDPEGECDDTTFQPCSARALA
NHKAVTDSFRTIYKINGGIKQGQAVAVGRYPEDVYFNGNPWYVATYAAAEQLYDAIHQWN
KVGKITVTEVSMPFFKDIYPQVQMGTHQSSSSEFGNIISVVKGYAEGYIEVAKKYTPCTG
MLSEQFSRDNGLPLSVSDLTWSYASYLTVMARRNSVVPSSWGEKNARELPSICMPSSARG
PYQAATITYWPPNLTPTAEPSPCPTALPTKNNVRFKLLATTQFGEDVFLVGSIKELGSWD
VKKAVPLNSDIYADNCHQWYADVELPTAVAFEYKFIRKRGGEVVWEQDPNRKYTVPQTCG
VSGSTKRDTWR

Enzyme Prediction     

EC	3.2.1.3:94	3.2.1.3:71

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH15	42	449	4.6e-76	0.9861495844875346
CBM20	512	599	2.5e-26	0.9444444444444444

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
395586	Glyco_hydro_15	3.17e-122	40	449	4	415	Glycosyl hydrolases family 15. In higher organisms this family is represented by phosphorylase kinase subunits.
99886	CBM20_glucoamylase	2.19e-35	503	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	2.18e-33	513	602	3	92	Starch binding domain.
119437	CBM20	8.49e-26	513	610	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.
99883	CBM20_alpha_amylase	1.79e-25	512	611	2	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CAC28076.1|CBM20|GH15|3.2.1.3	1.77e-254	22	611	26	618
ABH92242.1|CBM20|GH15|3.2.1.3	1.77e-254	22	611	26	618
CAY05394.1|CBM20|GH15|3.2.1.3	1.77e-254	22	611	26	618
AAR61400.1|CBM20|GH15|3.2.1.3	1.77e-254	22	611	26	618
ABH92239.1|CBM20|GH15|3.2.1.3	2.58e-252	40	611	17	591

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6FRV_A	1.98e-224	42	611	17	616	Structure of the catalytic domain of Aspergillus niger Glucoamylase [Aspergillus niger]
2VN4_A	2.13e-204	40	611	14	598	Chain A, GLUCOAMYLASE [Trichoderma reesei],2VN7_A Chain A, GLUCOAMYLASE [Trichoderma reesei]
6FHV_A	7.24e-204	39	611	19	593	Crystal structure of Penicillium oxalicum Glucoamylase [Penicillium oxalicum 114-2]
1AGM_A	2.91e-197	42	491	17	466	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	3.01e-197	42	491	17	466	GLUCOAMYLASE-471 COMPLEXED WITH ACARBOSE [Aspergillus awamori]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|P0DN29|AMYG_ARTBC	0.0	1	611	1	610	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	3.45e-248	16	611	16	612	Glucoamylase OS=Aspergillus oryzae (strain ATCC 42149 / RIB 40) OX=510516 GN=glaA PE=2 SV=2
sp|P22832|AMYG_ASPUS	7.93e-229	42	611	41	639	Glucoamylase OS=Aspergillus usamii OX=186680 GN=glaA PE=3 SV=1
sp|P23176|AMYG_ASPKA	6.88e-225	42	611	41	639	Glucoamylase I OS=Aspergillus kawachii OX=1069201 GN=gaI PE=1 SV=1
sp|P69327|AMYG_ASPAW	2.33e-223	42	611	41	640	Glucoamylase OS=Aspergillus awamori OX=105351 GN=GLAA PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
0.667125	0.332868

TMHMM  Annotations     

There is no transmembrane helices in EEQ33548.1.