CAZyme Information: KLU91951.1

Basic Information

• Species: Magnaporthiopsis poae
• Lineage: Ascomycota; Sordariomycetes; ; Magnaporthaceae; Magnaporthiopsis; Magnaporthiopsis poae
• CAZyme ID: KLU91951.1
• CAZy Family: GT2
• CAZyme Description: glucoamylase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
661	GL876978|CGC1	70509.67	5.7190

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_MpoaeATCC64411	12363	644358	200	12163

• Gene Location: location=GL876978:662338-664713(-)

Full Sequence      

MASLSGQPSSLANGTATATSTSMHPLSSLLLLGAYAAQVVLGRPNSDRTAAVRSVSDVDT
FIAKQRPVALSGLLRNIGPDGAYAPGVAPGVVVASPTIVNPDYYYTWTRDSALVFKCLAD
ILADEYDPSLQHLIEYYITTQARLQGVDNPSGSLADGAGLGEAKFNVNLRPYKGSWGRPQ
RDGPALRAIAMIGYANWLLTNGYTSTIRDILWPVIRNDIAYVAQYWNETGFELWEEVHGS
SFFTVASQHRALVEGSTLAKALGTSCASCDRVAPHVLCFLQSFWSSSGGYVVSNIHTDIK
RTGLDANSLLGSIHNFDPAAGCDDLTFQPCSSRSLANHKAVVDSFRFYPINSGISAGQAV
AVGRYSEDVYYEGNPWYLATLAAAELLYDSVYTWKRYGVINVTETSLPFFKDLSSSVKTG
AYTSDSQTFAELVDAVRTYADGFVSVVAKYTPANGSMAEQFHKVDGHPLSAGDLTWSYAS
FLTAADRRAGTVPASWWTGGGGAGSLPGSCGTNSERGTYSSVSPPPFPPSQTPITGVPTT
TATATTTQTSTATGCVTPVVVDVAFNVLVTTVPGEAIKVVGDIEDLGKWHPGSGTPLDAS
NYTSDNPLWKTSITLKGGHVVQYKYVKVRSDGSVSWEGDPNHTYTVPHSCATEAAISDRW
Q

Enzyme Prediction     

EC	3.2.1.3:94	3.2.1.1:13

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH15	84	485	1.5e-76	0.9556786703601108
CBM20	561	651	3.6e-25	0.9666666666666667

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
395586	Glyco_hydro_15	1.53e-135	67	485	1	416	Glycosyl hydrolases family 15. In higher organisms this family is represented by phosphorylase kinase subunits.
99886	CBM20_glucoamylase	6.33e-43	555	660	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	5.63e-33	561	656	1	95	Starch binding domain.
99883	CBM20_alpha_amylase	1.75e-24	561	660	1	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.
119437	CBM20	2.22e-24	563	660	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QBZ62081.1|CBM20|GH15	1.68e-304	13	661	8	648
CAY05367.1|CBM20|GH15|3.2.1.3	2.38e-304	13	661	8	648
QKD49751.1|CBM20|GH15	1.15e-272	13	661	25	674
UPK89675.1|CBM20|GH15	1.11e-271	13	661	25	669
QGI80625.1|CBM20|GH15	2.75e-271	13	661	16	665

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2VN4_A	2.80e-255	58	661	2	598	Chain A, GLUCOAMYLASE [Trichoderma reesei],2VN7_A Chain A, GLUCOAMYLASE [Trichoderma reesei]
6FRV_A	5.22e-230	58	661	3	616	Structure of the catalytic domain of Aspergillus niger Glucoamylase [Aspergillus niger]
6FHV_A	8.82e-213	61	661	11	593	Crystal structure of Penicillium oxalicum Glucoamylase [Penicillium oxalicum 114-2]
3EQA_A	2.56e-203	58	528	3	467	Catalytic domain of glucoamylase from aspergillus niger complexed with tris and glycerol [Aspergillus niger]
1AGM_A	6.29e-199	58	528	3	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|P14804|AMYG_NEUCR	2.66e-254	23	661	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|P69328|AMYG_ASPNG	6.18e-229	58	661	27	640	Glucoamylase OS=Aspergillus niger OX=5061 GN=GLAA PE=1 SV=1
sp|P69327|AMYG_ASPAW	6.18e-229	58	661	27	640	Glucoamylase OS=Aspergillus awamori OX=105351 GN=GLAA PE=1 SV=1
sp|P22832|AMYG_ASPUS	1.70e-228	46	661	15	639	Glucoamylase OS=Aspergillus usamii OX=186680 GN=glaA PE=3 SV=1
sp|P23176|AMYG_ASPKA	9.02e-226	58	661	27	639	Glucoamylase I OS=Aspergillus kawachii OX=1069201 GN=gaI PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
0.757481	0.242522

TMHMM  Annotations     

There is no transmembrane helices in KLU91951.1.