Species | Arthrobotrys flagrans | |||||||||||
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Lineage | Ascomycota; Orbiliomycetes; ; Orbiliaceae; Arthrobotrys; Arthrobotrys flagrans | |||||||||||
CAZyme ID | RVD88656.1 | |||||||||||
CAZy Family | GT15 | |||||||||||
CAZyme Description | Beta-galactosidase [Source:UniProtKB/TrEMBL;Acc:A0A437ABZ8] | |||||||||||
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 | 110 | 437 | 6.4e-86 | 0.9837133550488599 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
396048 | Glyco_hydro_35 | 2.17e-95 | 109 | 437 | 1 | 313 | Glycosyl hydrolases family 35. |
402180 | BetaGal_dom2 | 4.89e-47 | 461 | 629 | 14 | 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 | 7.86e-34 | 461 | 630 | 15 | 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 | 1.72e-32 | 903 | 1013 | 1 | 111 | Beta-galactosidase jelly roll domain. This domain is found in beta galactosidase enzymes. It has a jelly roll fold. |
166698 | PLN03059 | 7.59e-26 | 103 | 679 | 30 | 524 | beta-galactosidase; Provisional |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
0.0 | 66 | 1050 | 1 | 985 | |
0.0 | 83 | 1050 | 26 | 982 | |
6.20e-309 | 96 | 1050 | 37 | 992 | |
8.31e-309 | 95 | 1050 | 38 | 1011 | |
8.31e-309 | 95 | 1050 | 38 | 1011 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
2.98e-310 | 100 | 1050 | 3 | 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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3.07e-297 | 65 | 1050 | 2 | 1005 | Crystal structure of beta-galactosidase from Aspergillus oryzae in complex with galactose [Aspergillus oryzae] |
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6.61e-293 | 95 | 1050 | 38 | 1007 | Structure Of Beta-galactosidase From Aspergillus Niger [Aspergillus niger CBS 513.88] |
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1.87e-292 | 95 | 1050 | 38 | 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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7.27e-284 | 100 | 1050 | 23 | 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 |
---|---|---|---|---|---|---|
1.48e-309 | 95 | 1050 | 38 | 1011 | Beta-galactosidase A OS=Penicillium sp. OX=5081 GN=lacA PE=1 SV=1 |
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7.88e-297 | 65 | 1050 | 2 | 1005 | Beta-galactosidase A OS=Aspergillus oryzae (strain ATCC 42149 / RIB 40) OX=510516 GN=lacA PE=1 SV=1 |
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7.88e-297 | 65 | 1050 | 2 | 1005 | Probable beta-galactosidase A OS=Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC 167) OX=332952 GN=lacA PE=3 SV=1 |
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6.53e-296 | 65 | 1050 | 2 | 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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5.94e-294 | 65 | 1050 | 2 | 1006 | Probable beta-galactosidase A OS=Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) OX=330879 GN=lacA PE=3 SV=2 |
Other | SP_Sec_SPI | CS Position |
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1.000066 | 0.000001 |
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