Species | Aspergillus fumigatus | |||||||||||
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Lineage | Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus fumigatus | |||||||||||
CAZyme ID | AFUB_016080-T-p1 | |||||||||||
CAZy Family | CBM21 | |||||||||||
CAZyme Description | Ortholog(s) have beta-galactosidase activity and role in carbohydrate metabolic process | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH35 | 47 | 393 | 4.1e-85 | 0.9869706840390879 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
396048 | Glyco_hydro_35 | 9.57e-85 | 46 | 394 | 1 | 315 | Glycosyl hydrolases family 35. |
198097 | BetaGal_dom2 | 7.08e-80 | 402 | 583 | 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. |
402180 | BetaGal_dom2 | 4.00e-79 | 403 | 582 | 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. |
404274 | BetaGal_dom4_5 | 4.17e-36 | 858 | 976 | 1 | 111 | Beta-galactosidase jelly roll domain. This domain is found in beta galactosidase enzymes. It has a jelly roll fold. |
404274 | BetaGal_dom4_5 | 3.11e-31 | 689 | 802 | 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 | 1015 | 1 | 1014 | |
0.0 | 1 | 1015 | 1 | 1036 | |
0.0 | 1 | 1015 | 1 | 1015 | |
0.0 | 22 | 1015 | 1 | 1001 | |
0.0 | 1 | 1015 | 1 | 1014 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
3.89e-189 | 36 | 978 | 2 | 936 | 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.] |
|
1.21e-173 | 36 | 980 | 22 | 970 | 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] |
|
4.73e-172 | 36 | 981 | 42 | 975 | Structure Of Beta-galactosidase From Aspergillus Niger [Aspergillus niger CBS 513.88] |
|
1.31e-171 | 36 | 981 | 42 | 975 | 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] |
|
2.80e-167 | 30 | 978 | 36 | 970 | Crystal structure of beta-galactosidase from Aspergillus oryzae in complex with galactose [Aspergillus oryzae] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
0.0 | 18 | 1015 | 15 | 1007 | Probable beta-galactosidase B OS=Botryotinia fuckeliana (strain B05.10) OX=332648 GN=lacB PE=3 SV=1 |
|
0.0 | 1 | 1015 | 1 | 1015 | Probable beta-galactosidase B OS=Neosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163) OX=451804 GN=lacB PE=3 SV=1 |
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0.0 | 21 | 1015 | 18 | 1008 | Probable beta-galactosidase B OS=Sclerotinia sclerotiorum (strain ATCC 18683 / 1980 / Ss-1) OX=665079 GN=lacB PE=3 SV=1 |
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0.0 | 20 | 1015 | 26 | 1009 | Probable beta-galactosidase B OS=Pyrenophora tritici-repentis (strain Pt-1C-BFP) OX=426418 GN=lacB PE=3 SV=1 |
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0.0 | 1 | 1015 | 1 | 1017 | Probable beta-galactosidase B OS=Aspergillus niger (strain CBS 513.88 / FGSC A1513) OX=425011 GN=lacB PE=3 SV=2 |
Other | SP_Sec_SPI | CS Position |
---|---|---|
0.000212 | 0.999765 | CS pos: 21-22. Pr: 0.7566 |
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