dbCAN-seq: a database of CAZyme sequence and annotation

Basic Information help

Species

Fusarium oxysporum

Lineage

Ascomycota; Sordariomycetes; ; Nectriaceae; Fusarium; Fusarium oxysporum

CAZyme ID

FOMG_02397-t38_1-p1

CAZy Family

AA7

CAZyme Description

hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
374		40055.91	6.9923

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_Foxysporum26406	20033	1089452	372	19661

Gene Location

Enzyme Prediction help

EC	1.14.99.55:5	1.14.99.55:4

CAZyme Signature Domains help

Family	Start	End	Evalue	family coverage
AA13	19	250	2.5e-137	0.9956896551724138
CBM20	274	364	1.8e-27	0.9666666666666667

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
412056	AA13_LPMO-like	2.65e-164	19	251	1	233	AA13 lytic polysaccharide monooxygenase, and similar proteins. This family contains starch-degrading (also called starch-active) lytic polysaccharide monooxygenase (LPMO), a representative of the new CAZy AA13 family and classified as an auxiliary activity enzyme. This enzyme acts on alpha-linked glycosidic bonds and displays a binding surface that is quite different from those of LPMOs acting on beta-linked glycosidic bonds, indicating that the AA13 family proteins interact with their substrate in a distinct fashion. The active site contains an amino-terminal histidine-ligated mononuclear copper. This enzyme generates aldonic acid-terminated malto-oligosaccharides from retrograded starch and significantly boosts the conversion of this recalcitrant substrate to maltose by beta-amylase.
99886	CBM20_glucoamylase	5.60e-49	269	372	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.
395557	CBM_20	2.66e-42	274	369	1	95	Starch binding domain.
99883	CBM20_alpha_amylase	1.94e-32	274	373	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.
215006	CBM_2	3.79e-27	274	361	1	88	Starch binding domain.

CAZyme Hits help

Hit ID	E-Value	Query Start	Query End	Hit Start
6.29e-248	7	373	6	371
5.42e-196	1	373	1	381
5.62e-185	1	373	1	385
2.40e-179	1	373	1	405
2.06e-176	9	374	14	398

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
1.12e-134	20	250	2	232	AA13 Lytic polysaccharide monooxygenase from Aspergillus oryzae [Aspergillus oryzae RIB40],5LSV_A X-ray crystal structure of AA13 LPMO [Aspergillus oryzae RIB40],5T7J_A X-ray crystal structure of AA13 LPMO [Aspergillus oryzae RIB40],5T7K_A X-ray crystal structure of AA13 LPMO [Aspergillus oryzae RIB40],5T7N_A X-ray crystal structure of AA13 LPMO [Aspergillus oryzae RIB40],6TBQ_A AA13 Lytic polysaccharide monooxygenase from Aspergillus oryzae partially in Cu(II) state [Aspergillus oryzae RIB40],6TBR_A Glycosylated AA13 Lytic polysaccharide monooxygenase from Aspergillus oryzae in P1 space group [Aspergillus oryzae RIB40],6TBR_B Glycosylated AA13 Lytic polysaccharide monooxygenase from Aspergillus oryzae in P1 space group [Aspergillus oryzae RIB40],6TC4_A AA13 Lytic polysaccharide monooxygenase from Aspergillus oryzae measured with SSX [Aspergillus oryzae RIB40]
3.44e-32	269	373	2	108	GLUCOAMYLASE, GRANULAR STARCH-BINDING DOMAIN COMPLEX WITH CYCLODEXTRIN, NMR, MINIMIZED AVERAGE STRUCTURE [Aspergillus niger],1ACZ_A GLUCOAMYLASE, GRANULAR STARCH-BINDING DOMAIN COMPLEX WITH CYCLODEXTRIN, NMR, 5 STRUCTURES [Aspergillus niger],1KUL_A Chain A, GLUCOAMYLASE [Aspergillus niger],1KUM_A Chain A, GLUCOAMYLASE [Aspergillus niger],5GHL_A Crystal structure Analysis of the starch-binding domain of glucoamylase from Aspergillus niger [Aspergillus niger],5GHL_B Crystal structure Analysis of the starch-binding domain of glucoamylase from Aspergillus niger [Aspergillus niger],5GHL_C Crystal structure Analysis of the starch-binding domain of glucoamylase from Aspergillus niger [Aspergillus niger],5GHL_D Crystal structure Analysis of the starch-binding domain of glucoamylase from Aspergillus niger [Aspergillus niger]
8.14e-27	277	373	518	616	Structure of the catalytic domain of Aspergillus niger Glucoamylase [Aspergillus niger]
2.89e-25	233	362	441	585	Chain A, GLUCOAMYLASE [Trichoderma reesei],2VN7_A Chain A, GLUCOAMYLASE [Trichoderma reesei]
3.87e-12	233	363	451	582	Crystal structure of Penicillium oxalicum Glucoamylase [Penicillium oxalicum 114-2]

Swiss-Prot Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
3.48e-30	258	373	505	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
2.06e-29	272	363	510	600	Glucoamylase OS=Aspergillus oryzae (strain ATCC 42149 / RIB 40) OX=510516 GN=glaA PE=2 SV=2
1.19e-27	274	373	538	639	Glucoamylase I OS=Aspergillus kawachii OX=1069201 GN=gaI PE=1 SV=1
9.84e-27	274	373	538	639	Glucoamylase OS=Aspergillus usamii OX=186680 GN=glaA PE=3 SV=1
4.45e-26	277	373	542	640	Glucoamylase OS=Aspergillus niger OX=5061 GN=GLAA PE=1 SV=1

SignalP and Lipop Annotations help

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000500	0.999455	CS pos: 18-19. Pr: 0.9729

TMHMM Annotations help

There is no transmembrane helices in FOMG_02397-t38_1-p1.

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