Species | Aspergillus flavus | |||||||||||
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Lineage | Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus flavus | |||||||||||
CAZyme ID | QRD83561.1 | |||||||||||
CAZy Family | AA7 | |||||||||||
CAZyme Description | beta-galactosidase | |||||||||||
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 | 51 | 391 | 2.9e-87 | 0.9804560260586319 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
396048 | Glyco_hydro_35 | 1.80e-89 | 49 | 391 | 1 | 313 | Glycosyl hydrolases family 35. |
402180 | BetaGal_dom2 | 3.38e-62 | 404 | 566 | 1 | 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 | 1.67e-40 | 402 | 567 | 1 | 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. |
166698 | PLN03059 | 3.17e-23 | 43 | 205 | 30 | 197 | beta-galactosidase; Provisional |
404273 | BetaGal_dom3 | 1.22e-20 | 587 | 652 | 2 | 65 | Beta-galactosidase, domain 3. 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 has an Ig-like fold. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
0.0 | 1 | 906 | 1 | 906 | |
0.0 | 1 | 906 | 1 | 909 | |
0.0 | 26 | 906 | 15 | 846 | |
0.0 | 26 | 906 | 15 | 846 | |
0.0 | 26 | 552 | 6 | 532 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
7.14e-289 | 39 | 890 | 2 | 925 | 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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5.95e-285 | 21 | 890 | 26 | 961 | Structure Of Beta-galactosidase From Aspergillus Niger [Aspergillus niger CBS 513.88] |
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1.69e-284 | 21 | 890 | 26 | 961 | 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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2.09e-283 | 34 | 890 | 35 | 959 | Crystal structure of beta-galactosidase from Aspergillus oryzae in complex with galactose [Aspergillus oryzae] |
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2.35e-265 | 33 | 889 | 16 | 956 | 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 |
---|---|---|---|---|---|---|
6.91e-304 | 17 | 890 | 29 | 965 | 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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1.58e-302 | 16 | 890 | 28 | 965 | Probable beta-galactosidase E OS=Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) OX=330879 GN=lacE PE=3 SV=1 |
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1.58e-302 | 16 | 890 | 28 | 965 | Probable beta-galactosidase E OS=Neosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163) OX=451804 GN=lacE PE=3 SV=1 |
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4.86e-288 | 5 | 890 | 1 | 965 | Beta-galactosidase A OS=Penicillium sp. OX=5081 GN=lacA PE=1 SV=1 |
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2.51e-284 | 21 | 890 | 26 | 961 | Beta-galactosidase A OS=Aspergillus niger (strain CBS 513.88 / FGSC A1513) OX=425011 GN=lacA PE=1 SV=1 |
Other | SP_Sec_SPI | CS Position |
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1.000065 | 0.000000 |
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