CAZyme Information: AN11143-T-p1

Basic Information

• Species: Aspergillus nidulans
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus nidulans
• CAZyme ID: AN11143-T-p1
• CAZy Family: CBM21
• CAZyme Description: Glucan-alpha-1,4-glucosidase, putative

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
619	ChrVII_A_nidulans_FGSC_A4|CGC10	68712.04	5.0987

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AnidulansFGSCA4	10988	227321	276	10712

• Gene Location: location=ChrVII_A_nidulans_FGSC_A4:503758-505829(-)

Full Sequence      

MAFLSLYTQFFILGVVTLWVTHGPRPLQQTLAAGDLDIWLPSEANIARTALLDLIGDKGR
WAEGAAAGVLVASPSRSDPDYFYTWTRDSSLVFKTLVEMFRAGDSDLLPIIQDWISSQAR
IQGVENPSGGLADGRGLGEAKFTAEETAFAGSWGRPQRDGPALRATTMIEFGWWLLSQGY
HQLAANTVWPVVHNDISYLTEYWNQSGFDLWEDLYGRSFFTLAVTYRALTEASLFARSIG
SSCAECESQAPQVLCLLQSFWTGRFIRSNLDTGRTGKDASTLLGVIHTFSPRSECDDVTF
QPCSARALANHYRVVDAFRDLYDINADRSQDQAIAIGRYPEDQYFGGNPWFLCTIAAAEQ
LYSAIYQWTHLGSITITAVSLPFFQTLHPTAVPGTYSSSTEIYHQLIDAVRTYADGFMRI
VQTYASHNGSLAEQFSRYDGSHLSANDLAWSYASLLTAHRRRNAIAPSPWGNPGQPSIPS
YCEPTSASGTYSLATITTWPPMNGLPTTTSAPCQVPSLVSVTFELTASTVWGEEIRLVGS
SGELGYWVSERGITFSTDRYSSSQPIWWATVWLPAGQTVEYKYIRVREGYVVWEGDSNRL
LTIPAVCGVKSIYRRESWR

Enzyme Prediction     

EC	3.2.1.3:94	3.2.1.3:71

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH15	56	458	7.4e-72	0.9695290858725761
CBM20	519	607	4e-25	0.9555555555555556

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
395586	Glyco_hydro_15	1.83e-121	46	458	2	415	Glycosyl hydrolases family 15. In higher organisms this family is represented by phosphorylase kinase subunits.
99886	CBM20_glucoamylase	3.26e-41	513	608	1	97	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	4.87e-27	519	609	1	91	Starch binding domain.
99883	CBM20_alpha_amylase	2.07e-25	519	619	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	5.36e-21	520	605	1	86	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
EAA64118.1|CBM20|GH15	0.0	1	588	1	588
BCS21428.1|CBM20|GH15	0.0	5	619	5	631
QRD92849.1|CBM20|GH15	1.10e-270	33	619	27	612
QCL08961.1|CBM20|GH15	1.56e-270	33	619	27	612
CAY05395.1|CBM20|GH15|3.2.1.3	1.56e-270	33	619	27	612

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6FRV_A	4.84e-247	36	619	3	616	Structure of the catalytic domain of Aspergillus niger Glucoamylase [Aspergillus niger]
3EQA_A	9.37e-218	36	500	3	467	Catalytic domain of glucoamylase from aspergillus niger complexed with tris and glycerol [Aspergillus niger]
1AGM_A	3.79e-217	36	500	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]
1GAH_A	3.93e-217	36	500	3	466	GLUCOAMYLASE-471 COMPLEXED WITH ACARBOSE [Aspergillus awamori]
1GAI_A	4.07e-217	36	500	3	466	GLUCOAMYLASE-471 COMPLEXED WITH D-GLUCO-DIHYDROACARBOSE [Aspergillus awamori]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|P36914|AMYG_ASPOR	2.78e-271	33	619	27	612	Glucoamylase OS=Aspergillus oryzae (strain ATCC 42149 / RIB 40) OX=510516 GN=glaA PE=2 SV=2
sp|P22832|AMYG_ASPUS	1.04e-248	36	619	27	639	Glucoamylase OS=Aspergillus usamii OX=186680 GN=glaA PE=3 SV=1
sp|P69327|AMYG_ASPAW	5.80e-246	36	619	27	640	Glucoamylase OS=Aspergillus awamori OX=105351 GN=GLAA PE=1 SV=1
sp|P69328|AMYG_ASPNG	5.80e-246	36	619	27	640	Glucoamylase OS=Aspergillus niger OX=5061 GN=GLAA PE=1 SV=1
sp|P23176|AMYG_ASPKA	3.46e-242	36	619	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
0.519423	0.480569

TMHMM  Annotations     

There is no transmembrane helices in AN11143-T-p1.