CAZyme Information: GBF61895.1

Basic Information

• Species: Trichophyton mentagrophytes
• Lineage: Ascomycota; Eurotiomycetes; ; Arthrodermataceae; Trichophyton; Trichophyton mentagrophytes
• CAZyme ID: GBF61895.1
• CAZy Family: GH13
• CAZyme Description: glucoamylase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
610		67681.85	4.8666

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_TmentagrophytesTIMM2789	7958	N/A	98	7860

• Gene Location: location=BFBS01016029:329504-331577(+)

Full Sequence      

MRVTGLLWSSLVIPAAVGFQVRFRPSEDTTLDTVDDGTLQSLLDNIGLNGSNAWDTRPGL
VIASPSKKDPDYFFTWTRDSALVLKCITDAFAAGNTALQETIHEYISSQARIQLLNTRSG
GLSSGGLGEPKYRVDETPYNEDWGRPQADGPALRATALIAYARWLLENDYYDVAKSIVWP
VVKNDLSYVSEHWNTTAFDLWEEVNSPSFFTTIVQHRALVEGINMARALDETCPHCESQA
PQALCYLQSYWTGTAVRSNYGQGRSGLDVASILGSIHTFDPEGECDDTTFQPCSARALAN
HKAVTDSFRSVYKINGGINQGQAVAVGRYPEDVYFNGNPWYLATYAAAEQLYDAIYQWNK
IKKITVTDVSMPFFKDIYPEVQTGTHESSSPEFGNIIAAVKAYAEGYLEVAKKYTPCTGM
LSEQFSRDNGTPLSVADLTWSYASYLTVMARRNSVVPASWGEKNARDIPSTCVPSSATGP
YQTATITYWPPNLTPTAQPTPCPTALPTKNNVRFRLLATTQVGEDVFLVGSIPELGSWDV
KKAVPLNADIYADNCHQWYVDVELPTAVAFEYKFIRKRGGEVVWEQDPNRKYTVPQTCGV
SEVIKRDTWR

Enzyme Prediction     

EC	3.2.1.3:94	3.2.1.3:71

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH15	43	448	5.3e-78	0.9806094182825484
CBM20	511	598	1.3e-26	0.9444444444444444

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
395586	Glyco_hydro_15	3.60e-125	39	448	4	415	Glycosyl hydrolases family 15. In higher organisms this family is represented by phosphorylase kinase subunits.
99886	CBM20_glucoamylase	3.11e-36	502	609	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	9.56e-34	512	604	3	95	Starch binding domain.
119437	CBM20	6.37e-26	512	609	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	2.85e-25	511	610	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	1.48e-255	22	610	27	618
ABH92242.1|CBM20|GH15|3.2.1.3	1.48e-255	22	610	27	618
CAY05394.1|CBM20|GH15|3.2.1.3	1.48e-255	22	610	27	618
AAR61400.1|CBM20|GH15|3.2.1.3	1.48e-255	22	610	27	618
QSS49369.1|CBM20|GH15	1.31e-253	39	610	55	646

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6FRV_A	8.25e-226	41	610	17	616	Structure of the catalytic domain of Aspergillus niger Glucoamylase [Aspergillus niger]
2VN4_A	3.14e-206	26	610	1	598	Chain A, GLUCOAMYLASE [Trichoderma reesei],2VN7_A Chain A, GLUCOAMYLASE [Trichoderma reesei]
6FHV_A	2.61e-201	38	610	19	593	Crystal structure of Penicillium oxalicum Glucoamylase [Penicillium oxalicum 114-2]
1AGM_A	3.46e-198	41	490	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	3.59e-198	41	490	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	610	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	1.34e-247	28	610	31	612	Glucoamylase OS=Aspergillus oryzae (strain ATCC 42149 / RIB 40) OX=510516 GN=glaA PE=2 SV=2
sp|P22832|AMYG_ASPUS	1.08e-228	1	610	1	639	Glucoamylase OS=Aspergillus usamii OX=186680 GN=glaA PE=3 SV=1
sp|P69328|AMYG_ASPNG	6.86e-225	1	610	1	640	Glucoamylase OS=Aspergillus niger OX=5061 GN=GLAA PE=1 SV=1
sp|P69327|AMYG_ASPAW	6.86e-225	1	610	1	640	Glucoamylase OS=Aspergillus awamori OX=105351 GN=GLAA PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.004901	0.995068	CS pos: 18-19. Pr: 0.9569

TMHMM  Annotations     

There is no transmembrane helices in GBF61895.1.