CAZyme Information: EJT79232.1

Basic Information

• Species: Gaeumannomyces tritici
• Lineage: Ascomycota; Sordariomycetes; ; Magnaporthaceae; Gaeumannomyces; Gaeumannomyces tritici
• CAZyme ID: EJT79232.1
• CAZy Family: GH76
• CAZyme Description: glucoamylase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
655		69947.13	5.0444

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_GtriticiR3-111a-1	14749	644352	291	14458

• Gene Location: location=GL385396:5266998-5269362(-)

Full Sequence      

MASFGAQTSSLANGPGTTATSTAMHPLSSLALLGTYAAQIVLGRPNSHQTAARSVSDVDA
FIAEQRPIAMSGLLRNIGPDGAYAPGVAPGVVVASPTTVNPDYYYTWTRDSALVFKCLGD
ILSTEYDPSLQHLIEYYITTQARLQGVDNPAGSLTDGAGLGEAKFNVNLRPYKGSWGRPQ
RDGPALRAIAMMGYANWLLTNGYTSTIRDILWPVIRNDIAYVSQYWNQTGFDLWEEVHGS
SFFTVASQHRALVEGSTLAKALGTSCASCDRVAPQILCFLQSFWSPSGNYVVSNIHTDVK
RTGLDANSLLVSIHNFDPAAGCDDLTLQPCSSRSLANHKAVVDSFRFYAINSGIPAGQGI
AVGRYSEDVYYDGNPWYLATLAAAELLYDSVYTWKLYGAINVTETSLPFFQDLSSSVKTG
SYTSGSATFTELVDAVRVYADGFVGVAAKYTPSNGSMAEQFHKNDGHPLSAGDLTWSYAS
FLTATDRRAGIVPASWWMGGGGLPASCGTDSEPGTYSSVSPPPFPPSQTPITGAPPTPTT
TASTTATGCVVPVVVDVTFNVLVTTVPGETIKVVGDIEDLGKWNPENATPLDASAYTSSN
PLWKTDVTLKGGHVVKYKYVKVQSNGSVSWEADPDRTYTVPHSCATEAAISDRWQ

Enzyme Prediction     

EC	3.2.1.3:94	3.2.1.3:71

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH15	84	484	1.9e-75	0.9529085872576177
CBM20	555	645	3.4e-27	0.9666666666666667

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
395586	Glyco_hydro_15	3.51e-132	67	484	1	415	Glycosyl hydrolases family 15. In higher organisms this family is represented by phosphorylase kinase subunits.
99886	CBM20_glucoamylase	1.76e-42	549	654	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	6.93e-34	558	650	4	95	Starch binding domain.
119437	CBM20	2.87e-25	558	654	3	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	4.55e-25	558	654	4	94	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
QBZ62081.1|CBM20|GH15	6.42e-310	17	655	16	648
CAY05367.1|CBM20|GH15|3.2.1.3	9.11e-310	17	655	16	648
UPK89675.1|CBM20|GH15	5.87e-270	24	655	35	669
CEI69823.1|CBM20|GH15	1.70e-266	24	655	1	628
QPC79615.1|CBM20|GH15	5.89e-266	24	655	26	653

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2VN4_A	2.80e-251	58	655	2	598	Chain A, GLUCOAMYLASE [Trichoderma reesei],2VN7_A Chain A, GLUCOAMYLASE [Trichoderma reesei]
6FRV_A	7.81e-223	58	655	3	616	Structure of the catalytic domain of Aspergillus niger Glucoamylase [Aspergillus niger]
6FHV_A	1.33e-210	61	655	11	593	Crystal structure of Penicillium oxalicum Glucoamylase [Penicillium oxalicum 114-2]
3EQA_A	1.45e-198	58	520	3	462	Catalytic domain of glucoamylase from aspergillus niger complexed with tris and glycerol [Aspergillus niger]
6FHW_A	3.65e-195	57	654	30	606	Chain A, Glucoamylase P [Amorphotheca resinae],6FHW_B Chain B, Glucoamylase P [Amorphotheca resinae]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|P14804|AMYG_NEUCR	4.94e-253	24	655	1	626	Glucoamylase OS=Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987) OX=367110 GN=gla-1 PE=1 SV=3
sp|P36914|AMYG_ASPOR	4.95e-222	49	655	21	612	Glucoamylase OS=Aspergillus oryzae (strain ATCC 42149 / RIB 40) OX=510516 GN=glaA PE=2 SV=2
sp|P69328|AMYG_ASPNG	9.19e-222	58	655	27	640	Glucoamylase OS=Aspergillus niger OX=5061 GN=GLAA PE=1 SV=1
sp|P69327|AMYG_ASPAW	9.19e-222	58	655	27	640	Glucoamylase OS=Aspergillus awamori OX=105351 GN=GLAA PE=1 SV=1
sp|P22832|AMYG_ASPUS	6.66e-219	58	655	27	639	Glucoamylase OS=Aspergillus usamii OX=186680 GN=glaA PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
0.975311	0.024690

TMHMM  Annotations     

There is no transmembrane helices in EJT79232.1.