CAZyme Information: KID61833.1

Basic Information

• Species: Metarhizium anisopliae
• Lineage: Ascomycota; Sordariomycetes; ; Clavicipitaceae; Metarhizium; Metarhizium anisopliae
• CAZyme ID: KID61833.1
• CAZy Family: AA7
• CAZyme Description: Glucan 1,4-alpha-glucosidase, starch-binding protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
586	AZNF01000013|CGC4	63304.92	6.3907

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_ManisopliaeARSEF549	10891	1276135	0	10891

• Gene Location: location=AZNF01000013:73417-75226(+)

Full Sequence      

MYKKLVSVLAVAGLWLDGAVARSRISCRDDLNAFITKQNHISLDGVLANIGSDGSRAQGA
AAGAVVASPSKSDPDYWYTWSRDSALTFKVLIELFVSGNKSLQPKIEQYMTAQAHLQGVS
NPSGGPDTGGLGEPKFHVNLTAFTGPWGRPQRDGPPLRATALTIYANWLIANGGQAQAAN
TVWPIIAKDLAYTVQYWNRTGFDLWEEINGSSFFTLSASFRALVEGATLAKALGKQCPDC
ETNAPRILCFLQSFWASGYIDSNINVNDGRTGKDVNSIISSIHTFDPAAACTDATFQPCS
SRALANHKAVVDSFRTIYTVNKGRTPGRAAAVGRYSEDVYYNGNPWYLATMAAAEQMYAA
VYQWRKIGSITVDATSLPFFSDLIPNIAAGTYAKDSDTFTSIIKAVTAYGDDFISVVKQY
TPADGSLVEQYDRETGSPKSAVHLTWSYASFVGAVERRSGVVPPSWGEPNANTVPKVCEA
LPSCDSTMTFNVKVTTVPGENIYVVGSITELKNWSPADAIPLDASQYTPSNPLWSAKVTI
PAGTNFEYKYIKKTSEGGVVWESDPNRSATSSTGCHSTGTLNDEWR

Enzyme Prediction     

EC	3.2.1.3:94	3.2.1.3:71

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH15	50	454	7.8e-76	0.9722991689750693
CBM20	488	576	2.5e-29	0.9444444444444444

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
395586	Glyco_hydro_15	1.98e-129	41	454	2	415	Glycosyl hydrolases family 15. In higher organisms this family is represented by phosphorylase kinase subunits.
99886	CBM20_glucoamylase	1.16e-43	489	585	10	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	2.56e-39	486	586	1	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.
395557	CBM_20	7.46e-38	489	578	4	92	Starch binding domain.
119437	CBM20	1.06e-26	489	585	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QLI65999.1|CBM20|GH15	0.0	1	586	1	586
QPH16390.1|CBM20|GH15	0.0	3	586	46	629
ANH22726.1|CBM20|GH15	1.16e-312	1	586	26	616
QUC20677.1|CBM20|GH15	5.18e-311	1	586	1	586
ABY89281.1|CBM20|GH15	6.33e-311	31	586	28	582

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2VN4_A	5.43e-221	34	586	5	598	Chain A, GLUCOAMYLASE [Trichoderma reesei],2VN7_A Chain A, GLUCOAMYLASE [Trichoderma reesei]
6FHV_A	1.97e-212	30	586	7	593	Crystal structure of Penicillium oxalicum Glucoamylase [Penicillium oxalicum 114-2]
6FRV_A	1.03e-207	31	586	3	616	Structure of the catalytic domain of Aspergillus niger Glucoamylase [Aspergillus niger]
6FHW_A	2.76e-192	30	553	30	574	Chain A, Glucoamylase P [Amorphotheca resinae],6FHW_B Chain B, Glucoamylase P [Amorphotheca resinae]
1AGM_A	6.78e-182	31	480	3	450	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	2.14e-236	31	586	37	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	2.68e-216	31	586	30	612	Glucoamylase OS=Aspergillus oryzae (strain ATCC 42149 / RIB 40) OX=510516 GN=glaA PE=2 SV=2
sp|P22832|AMYG_ASPUS	6.70e-211	7	586	5	639	Glucoamylase OS=Aspergillus usamii OX=186680 GN=glaA PE=3 SV=1
sp|P69328|AMYG_ASPNG	2.26e-209	7	586	5	640	Glucoamylase OS=Aspergillus niger OX=5061 GN=GLAA PE=1 SV=1
sp|P69327|AMYG_ASPAW	2.26e-209	7	586	5	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
0.000299	0.999662	CS pos: 21-22. Pr: 0.9740

TMHMM  Annotations     

There is no transmembrane helices in KID61833.1.