Species | Aspergillus niger | |||||||||||
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Lineage | Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus niger | |||||||||||
CAZyme ID | M747DRAFT_327224-t43_1-p1 | |||||||||||
CAZy Family | GH51 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location |
EC | 3.2.1.23:18 | 2.4.1.-:1 |
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Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH35 | 49 | 397 | 1.7e-85 | 0.9771986970684039 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
396048 | Glyco_hydro_35 | 2.98e-96 | 51 | 397 | 6 | 313 | Glycosyl hydrolases family 35. |
402180 | BetaGal_dom2 | 4.55e-69 | 411 | 584 | 2 | 180 | Beta-galactosidase, domain 2. This is the second domain of the five-domain beta-galactosidase enzyme that altogether catalyzes the hydrolysis of beta(1-3) and beta(1-4) galactosyl bonds in oligosaccharides as well as the inverse reaction of enzymatic condensation and trans-glycosylation. This domain is made up of 16 antiparallel beta-strands and an alpha-helix at its C-terminus. The fold of this domain appears to be unique. In addition, the last seven strands of the domain form a subdomain with an immunoglobulin-like (I-type Ig) fold in which the first strand is divided between the two beta-sheets. In penicillin spp this strand is interrupted by a 12-residue insertion which forms an additional edge-strand to the second beta-sheet of the sub-domain. The remainder of the second domain forms a series of beta-hairpins at its N-terminus, four strands of which are contiguous with part of the Ig-like sub-domain, forming in total a seven-stranded antiparallel beta-sheet. This domain is associated with family Glyco_hydro_35, pfam01301, which is N-terminal to it, but itself has no metazoan members. |
198097 | BetaGal_dom2 | 9.31e-53 | 414 | 585 | 7 | 182 | Beta-galactosidase, domain 2. This is the second domain of the five-domain beta-galactosidase enzyme that altogether catalyses the hydrolysis of beta(1-3) and beta(1-4) galactosyl bonds in oligosaccharides as well as the inverse reaction of enzymatic condensation and trans-glycosylation. This domain is made up of 16 antiparallel beta-strands and an alpha-helix at its C terminus. The fold of this domain appears to be unique. In addition, the last seven strands of the domain form a subdomain with an immunoglobulin-like (I-type Ig) fold in which the first strand is divided between the two beta-sheets. In penicillin spp this strand is interrupted by a 12-residue insertion which forms an additional edge-strand to the second beta-sheet of the sub-domain. The remainder of the second domain forms a series of beta-hairpins at its N terminus, four strands of which are contiguous with part of the Ig-like sub-domain, forming in total a seven-stranded antiparallel beta-sheet. This domain is associated with family Glyco_hydro_35, which is N-terminal to it, but itself has no metazoan members. |
404274 | BetaGal_dom4_5 | 8.01e-35 | 873 | 992 | 1 | 110 | Beta-galactosidase jelly roll domain. This domain is found in beta galactosidase enzymes. It has a jelly roll fold. |
404274 | BetaGal_dom4_5 | 6.07e-28 | 703 | 816 | 1 | 111 | Beta-galactosidase jelly roll domain. This domain is found in beta galactosidase enzymes. It has a jelly roll fold. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
0.0 | 1 | 1030 | 1 | 1030 | |
0.0 | 1 | 1030 | 1 | 1015 | |
0.0 | 1 | 1030 | 1 | 1029 | |
0.0 | 1 | 1030 | 1 | 1029 | |
0.0 | 36 | 1030 | 39 | 1017 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
0.0 | 36 | 1030 | 2 | 971 | Native structure of beta-galactosidase from Penicillium sp. [Penicillium sp.],1XC6_A Native Structure Of Beta-Galactosidase from Penicillium sp. in complex with Galactose [Penicillium sp.] |
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0.0 | 36 | 1030 | 42 | 1005 | Crystal structure of beta-galactosidase from Aspergillus oryzae in complex with galactose [Aspergillus oryzae] |
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0.0 | 1 | 1030 | 1 | 1007 | Structure Of Beta-galactosidase From Aspergillus Niger [Aspergillus niger CBS 513.88] |
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0.0 | 1 | 1030 | 1 | 1007 | STRUCTURE OF E298Q-BETA-GALACTOSIDASE FROM ASPERGILLUS NIGER IN COMPLEX WITH 3-b-Galactopyranosyl glucose [Aspergillus niger CBS 513.88],5IHR_A Structure Of E298q-beta-galactosidase From Aspergillus Niger In Complex With Allolactose [Aspergillus niger CBS 513.88],5JUV_A STRUCTURE OF E298Q-BETA-GALACTOSIDASE FROM ASPERGILLUS NIGER IN COMPLEX WITH 6-b-Galactopyranosyl galactose [Aspergillus niger CBS 513.88],5MGC_A STRUCTURE OF E298Q-BETA-GALACTOSIDASE FROM ASPERGILLUS NIGER IN COMPLEX WITH 4-Galactosyl-lactose [Aspergillus niger CBS 513.88],5MGD_A STRUCTURE OF E298Q-BETA-GALACTOSIDASE FROM ASPERGILLUS NIGER IN COMPLEX WITH 6-Galactosyl-lactose [Aspergillus niger CBS 513.88] |
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2.52e-317 | 36 | 1030 | 22 | 1003 | Chain A, Beta-galactosidase [Trichoderma reesei],3OGR_A Chain A, Beta-galactosidase [Trichoderma reesei],3OGS_A Chain A, Beta-galactosidase [Trichoderma reesei],3OGV_A Chain A, Beta-galactosidase [Trichoderma reesei] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
0.0 | 36 | 1030 | 42 | 1006 | Probable beta-galactosidase A OS=Neosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163) OX=451804 GN=lacA PE=3 SV=2 |
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0.0 | 36 | 1030 | 42 | 1006 | Probable beta-galactosidase A OS=Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181 / WB 181) OX=331117 GN=lacA PE=3 SV=1 |
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0.0 | 5 | 1030 | 3 | 1011 | Probable beta-galactosidase E OS=Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181 / WB 181) OX=331117 GN=lacE PE=3 SV=1 |
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0.0 | 1 | 1030 | 1 | 1007 | Beta-galactosidase A OS=Aspergillus niger (strain CBS 513.88 / FGSC A1513) OX=425011 GN=lacA PE=1 SV=1 |
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0.0 | 36 | 1030 | 42 | 1011 | Probable beta-galactosidase A OS=Penicillium expansum OX=27334 GN=lacA PE=2 SV=1 |
Other | SP_Sec_SPI | CS Position |
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0.000655 | 0.999328 | CS pos: 18-19. Pr: 0.9406 |
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