CAZyme Information: EEP80436.1

Basic Information

• Species: Uncinocarpus reesii
• Lineage: Ascomycota; Eurotiomycetes; ; Onygenaceae; Uncinocarpus; Uncinocarpus reesii
• CAZyme ID: EEP80436.1
• CAZy Family: GT15|GT15
• CAZyme Description: glucoamylase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
617	CH476617|CGC7	67505.79	6.4946

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_Ureesii1704	7856	336963	96	7760

• Gene Location: location=CH476617:1478570-1480661(-)

Full Sequence      

MMYSVLKALCAIPLLCSVAGSAKTSFALQQEETLDQWLEAEGTFALQAILDNIGPNGAKV
RGAHAGIVVASPSKSNPDYFYTWTRDAALVFKQLVDTFIAGNYDLQDKIHEFITAQAELQ
TVSNPSGTLSTGGLGEPKFHVNQTAFTGDWGRPQHDGPPLRATAMITYAKWLVDNGHVDA
ARSIVWPVVQNDLAYVGQYWNSTGFDLWEEVKGSSFFTAIAQHRALVEGGNLARQLGVDC
SQCESQAPQVLCFLQSFWSGTNIIANFGGDRSGLDTNSILGIIHNFDPEADCDDNTFQPC
SSRALANHKRVTDSFRSIYPINSRIPSDQAVAVGRYAEDVYYGGQPWYLATFAAAEMLYN
AIYQWNRTGEMSITDVSLPFFKGVYSSAQVGKYSASSRAFSDIMANVTKYADGYLNIARR
YTPCSGALAEQFSKADGRPLSASDLTWSYAALLTAKERRNAIVPGPWGQKSAHDVPTTCS
ASPAPGRYQTATITGWPSTLTPVPTSPTPCPAPNRVKVTFQSITETKWGENIFIVGSVAE
LGSWNPEAATPLRADKYEDSCHMWYAQVDLPAGARVEYKYIRKSGDGKVVWESDPNRSYK
IPKKCGVSSLTLKSSWR

Enzyme Prediction     

EC	3.2.1.3:94	3.2.1.3:71

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH15	51	455	5.2e-78	0.9778393351800554
CBM20	516	605	3.2e-28	0.9555555555555556

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
395586	Glyco_hydro_15	1.60e-136	45	455	3	415	Glycosyl hydrolases family 15. In higher organisms this family is represented by phosphorylase kinase subunits.
99886	CBM20_glucoamylase	5.53e-45	510	616	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	3.45e-33	516	609	1	93	Starch binding domain.
99883	CBM20_alpha_amylase	1.26e-32	516	617	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.
119437	CBM20	5.55e-26	517	608	1	91	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
QSS67842.1|CBM20|GH15	3.68e-272	34	617	43	646
CAC28076.1|CBM20|GH15|3.2.1.3	2.21e-271	8	617	8	618
ABH92242.1|CBM20|GH15|3.2.1.3	2.21e-271	8	617	8	618
CAY05394.1|CBM20|GH15|3.2.1.3	2.21e-271	8	617	8	618
AAR61400.1|CBM20|GH15|3.2.1.3	2.21e-271	8	617	8	618

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6FRV_A	6.45e-242	33	617	2	616	Structure of the catalytic domain of Aspergillus niger Glucoamylase [Aspergillus niger]
1AGM_A	3.53e-217	33	498	2	467	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	3.66e-217	33	498	2	467	GLUCOAMYLASE-471 COMPLEXED WITH ACARBOSE [Aspergillus awamori]
1GAI_A	3.79e-217	33	498	2	467	GLUCOAMYLASE-471 COMPLEXED WITH D-GLUCO-DIHYDROACARBOSE [Aspergillus awamori]
6FHV_A	3.47e-216	34	607	8	584	Crystal structure of Penicillium oxalicum Glucoamylase [Penicillium oxalicum 114-2]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|P0DN29|AMYG_ARTBC	2.52e-261	17	617	10	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	2.54e-259	28	617	24	612	Glucoamylase OS=Aspergillus oryzae (strain ATCC 42149 / RIB 40) OX=510516 GN=glaA PE=2 SV=2
sp|P22832|AMYG_ASPUS	1.58e-247	28	617	21	639	Glucoamylase OS=Aspergillus usamii OX=186680 GN=glaA PE=3 SV=1
sp|P23176|AMYG_ASPKA	5.99e-245	28	617	21	639	Glucoamylase I OS=Aspergillus kawachii OX=1069201 GN=gaI PE=1 SV=1
sp|P69327|AMYG_ASPAW	1.91e-241	15	617	6	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
0.033876	0.966096	CS pos: 22-23. Pr: 0.8705

TMHMM  Annotations     

There is no transmembrane helices in EEP80436.1.