CAZyme Information: FFUJ_12586-t31_1-p1

Basic Information

• Species: Fusarium fujikuroi
• Lineage: Ascomycota; Sordariomycetes; ; Nectriaceae; Fusarium; Fusarium fujikuroi
• CAZyme ID: FFUJ_12586-t31_1-p1
• CAZy Family: GH88
• CAZyme Description: probable glucan 1,4-alpha-glucosidase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
582		62734.34	8.8255

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_FfujikuroiIMI58289	15099	1279085	286	14813

• Gene Location: location=HF679030:2317553-2319354(+)

Full Sequence      

MFTQILYGLTALSALQGQATASPGGSSLDRFIAKEADISIKGVLANIGADGKRAQGAAPG
AVVASPSRADPDYWYTWTRDSALTYKVLVERFIHGDKSLQRKIDDYVSAQAKLQGVTNPS
GGPETGGLGEPKFHVNLTAFTGSWGRPQRDGPPLRATALTLYANWLVSHGDRSKAVDKVW
PVIEKDLAYTVKFWNRTGYDLWEEVNGSSFFTLSASHRALIEGAALAKKLGKSCSDCTAN
APRVLCFMQSFWTGSYIDSNINVNDGRKGLDANSILSSIHTFDPSSKCTDSTFQPCSSRA
LANHKAVVDSFRSIYGVNKNRGKGKAAAVGRYSEDVYYDGNPWYLATLAAAEQLYAAVYQ
WNKIGSITVDSVSLPFFSDLVPKVSKGTYRKNSKTYKAIVKAVTSYADGFVAVVQTYTPK
DGSLAEQFDKSTGTPKSAVHLTWSYASFVGAAERRTGVVPPAWGESSANKVPAVCEAAPA
CDTTITFSVKNVEVTSDQKVYIVGGITQLSNWAPADGIALEESTSTKGLWTVKVKIPSDT
SFEYKYIKKTSDGAVTWESDPNNSAATGSKCGSSSTINDEWR

Enzyme Prediction     

EC	3.2.1.3:94	3.2.1.3:71

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH15	44	452	2.2e-80	0.9833795013850416
CBM20	484	572	3e-24	0.9555555555555556

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
395586	Glyco_hydro_15	4.94e-138	38	452	2	416	Glycosyl hydrolases family 15. In higher organisms this family is represented by phosphorylase kinase subunits.
99883	CBM20_alpha_amylase	3.69e-33	483	582	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	3.07e-27	483	577	1	95	Starch binding domain.
99886	CBM20_glucoamylase	1.07e-26	478	581	2	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.
215006	CBM_2	4.85e-23	483	569	1	88	Starch binding domain.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QGI85549.1|CBM20|GH15	0.0	1	582	1	582
CCT72695.1|CBM20|GH15	0.0	1	582	1	582
QGI99224.1|CBM20|GH15	0.0	1	582	1	582
ABY89281.1|CBM20|GH15	0.0	1	582	1	582
QKD61891.1|CBM20|GH15	0.0	1	582	1	582

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6FHV_A	1.29e-209	23	582	3	593	Crystal structure of Penicillium oxalicum Glucoamylase [Penicillium oxalicum 114-2]
6FRV_A	1.17e-205	26	582	1	616	Structure of the catalytic domain of Aspergillus niger Glucoamylase [Aspergillus niger]
2VN4_A	5.32e-205	27	562	1	577	Chain A, GLUCOAMYLASE [Trichoderma reesei],2VN7_A Chain A, GLUCOAMYLASE [Trichoderma reesei]
1GAI_A	3.41e-189	26	504	1	472	GLUCOAMYLASE-471 COMPLEXED WITH D-GLUCO-DIHYDROACARBOSE [Aspergillus awamori]
1AGM_A	4.50e-189	26	483	1	456	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	1.41e-228	27	582	36	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	3.51e-213	2	582	4	612	Glucoamylase OS=Aspergillus oryzae (strain ATCC 42149 / RIB 40) OX=510516 GN=glaA PE=2 SV=2
sp|P22832|AMYG_ASPUS	2.84e-206	9	582	6	639	Glucoamylase OS=Aspergillus usamii OX=186680 GN=glaA PE=3 SV=1
sp|P69327|AMYG_ASPAW	1.68e-205	9	582	6	640	Glucoamylase OS=Aspergillus awamori OX=105351 GN=GLAA PE=1 SV=1
sp|P69328|AMYG_ASPNG	1.68e-205	9	582	6	640	Glucoamylase OS=Aspergillus niger OX=5061 GN=GLAA PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000279	0.999687	CS pos: 21-22. Pr: 0.9624

TMHMM  Annotations     

There is no transmembrane helices in FFUJ_12586-t31_1-p1.