Species | Fusarium proliferatum | |||||||||||
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Lineage | Ascomycota; Sordariomycetes; ; Nectriaceae; Fusarium; Fusarium proliferatum | |||||||||||
CAZyme ID | FPRO_11517-t41_1-p1 | |||||||||||
CAZy Family | GH32|CBM38 | |||||||||||
CAZyme Description | related to glucoamylase precursor | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location |
EC | 1.14.99.55:5 |
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Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
AA13 | 19 | 251 | 2.7e-144 | 0.9956896551724138 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
412056 | AA13_LPMO-like | 8.74e-170 | 19 | 252 | 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. |
397269 | LPMO_10 | 0.007 | 19 | 103 | 1 | 101 | Lytic polysaccharide mono-oxygenase, cellulose-degrading. This domain is found associated with a wide variety of cellulose binding domains. This is a family of two very closely related proteins that together act as both a C1- and a C4-oxidising lytic polysaccharide mono-oxygenase, degrading cellulose. This domain is also found in baculoviral spheroidins and spindolins, protein of unknown function. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
2.85e-193 | 1 | 253 | 1 | 253 | |
8.18e-193 | 1 | 253 | 1 | 253 | |
1.25e-190 | 1 | 253 | 1 | 256 | |
1.25e-190 | 1 | 253 | 1 | 256 | |
2.07e-189 | 1 | 253 | 1 | 256 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
1.98e-130 | 20 | 251 | 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] |
Other | SP_Sec_SPI | CS Position |
---|---|---|
0.000435 | 0.999536 | CS pos: 18-19. Pr: 0.9776 |
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