CAZyme Information: EKG12865.1

Basic Information

• Species: Macrophomina phaseolina
• Lineage: Ascomycota; Dothideomycetes; ; Botryosphaeriaceae; Macrophomina; Macrophomina phaseolina
• CAZyme ID: EKG12865.1
• CAZy Family: CE1
• CAZyme Description: Glycoside hydrolase family 15

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
638	AHHD01000425|CGC1	67884.19	5.2645

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_MphaseolinaMS6	14712	1126212	906	13806

• Gene Location: location=AHHD01000425:17001-19379(+)

Full Sequence      

MLFPSKALALVGLLVGDALAIPATTLRKRQSSVDTFISTESPIAYAGVLANIGDDGSKVA
GAAAGIVVASPSKSNPDYFYTWTRDASLVFKALVDHFIAGDYSLQDEIEDFIISQAKLQG
VSNPSGDLRSGAGLGEPKFNVDLTQFTGAWGRPQRDGPALRATSMIAYAHWLINNGYSDT
ARDVVWPVIRNDLSYVSQYWNQTGFDLWEEVQGSSFFTIAVSHRALVEGSTLASALGQSC
SYCDSQAPQTLCFLQSFWTSNGNYVVSNINTNNGRTGKDANSILASIHTFDPDAGCDDST
FQPCSARALANHKAVTDSFRSIYNINSGIAQGRAVAVGRYAEDVYYNGNPWYLTTLAAAE
QLYDALYTWTREGTITITSVSLPFFRDIYSSAAVGTYASGSAAYTSILNAVKTYADGYVS
VVQKYTPSSGALAEQYSRNDGSPLSAADLTWSYAAFLTAIARRNSIVPASWGGETANVVP
GSCVATSAIGTYASATNTVFPTSQTSNPGATTTRPPTSSTTTTRVTSSTTTTTTNPTSVA
VTFNVIATTVFGENIFLAGSIAALGSWAPASAKALSADKYTSSNNLWYVTVSLAPGTSFQ
YKYIRKSSSGAYTWESDPNRSYTVPSGVATATISDTWR

Enzyme Prediction     

EC	3.2.1.3:94	1.14.99.55:4

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH15	48	460	6.6e-80	0.9861495844875346
CBM20	539	628	8.9e-28	0.9555555555555556

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
395586	Glyco_hydro_15	4.36e-140	42	460	1	416	Glycosyl hydrolases family 15. In higher organisms this family is represented by phosphorylase kinase subunits.
99886	CBM20_glucoamylase	1.17e-48	540	637	8	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	1.22e-37	540	634	2	95	Starch binding domain.
99883	CBM20_alpha_amylase	1.63e-34	540	638	2	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	1.34e-27	541	637	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
QSZ31699.1|CBM20|GH15	4.62e-286	30	638	66	676
APA12357.1|CBM20|GH15	4.96e-286	30	638	66	678
CCD49819.2|CBM20|GH15	3.49e-280	1	637	8	645
ATZ49247.1|CBM20|GH15	9.19e-280	1	637	35	672
ATZ49248.1|CBM20|GH15	9.19e-280	1	637	35	672

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6FRV_A	2.13e-265	31	638	1	616	Structure of the catalytic domain of Aspergillus niger Glucoamylase [Aspergillus niger]
2VN4_A	9.31e-248	32	638	1	598	Chain A, GLUCOAMYLASE [Trichoderma reesei],2VN7_A Chain A, GLUCOAMYLASE [Trichoderma reesei]
3EQA_A	5.49e-229	31	501	1	467	Catalytic domain of glucoamylase from aspergillus niger complexed with tris and glycerol [Aspergillus niger]
1AGM_A	2.77e-224	31	501	1	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	2.87e-224	31	501	1	466	GLUCOAMYLASE-471 COMPLEXED WITH ACARBOSE [Aspergillus awamori]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|P69327|AMYG_ASPAW	4.50e-265	28	638	22	640	Glucoamylase OS=Aspergillus awamori OX=105351 GN=GLAA PE=1 SV=1
sp|P69328|AMYG_ASPNG	4.50e-265	28	638	22	640	Glucoamylase OS=Aspergillus niger OX=5061 GN=GLAA PE=1 SV=1
sp|P22832|AMYG_ASPUS	4.70e-262	23	638	18	639	Glucoamylase OS=Aspergillus usamii OX=186680 GN=glaA PE=3 SV=1
sp|P36914|AMYG_ASPOR	7.26e-262	28	638	25	612	Glucoamylase OS=Aspergillus oryzae (strain ATCC 42149 / RIB 40) OX=510516 GN=glaA PE=2 SV=2
sp|P23176|AMYG_ASPKA	2.19e-260	28	638	22	639	Glucoamylase I OS=Aspergillus kawachii OX=1069201 GN=gaI PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000377	0.999617	CS pos: 29-30. Pr: 0.9166

TMHMM  Annotations     

There is no transmembrane helices in EKG12865.1.