dbCAN-seq: a database of CAZyme sequence and annotation

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CAZyme Information: KLU89827.1

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Basic Information help

Species

Magnaporthiopsis poae

Lineage

Ascomycota; Sordariomycetes; ; Magnaporthaceae; Magnaporthiopsis; Magnaporthiopsis poae

CAZyme ID

KLU89827.1

CAZy Family

GH47

CAZyme Description

Beta-galactosidase [Source:UniProtKB/TrEMBL;Acc:A0A0C4E899]

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
886		95500.70	6.6911

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_MpoaeATCC64411	12363	644358	200	12163

Gene Location

Full Sequence Download help

Enzyme Prediction help

EC	3.2.1.23:18	2.4.1.-:1

CAZyme Signature Domains help

Family	Start	End	Evalue	family coverage
GH35	46	378	1.1e-88	0.9869706840390879

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
396048	Glyco_hydro_35	1.31e-94	44	379	1	316	Glycosyl hydrolases family 35.
402180	BetaGal_dom2	5.76e-40	390	585	1	178	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.
166698	PLN03059	6.10e-30	38	393	30	354	beta-galactosidase; Provisional
198097	BetaGal_dom2	1.74e-29	427	588	32	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	1.18e-26	707	837	1	108	Beta-galactosidase jelly roll domain. This domain is found in beta galactosidase enzymes. It has a jelly roll fold.

CAZyme Hits help

Hit ID	E-Value	Query Start	Query End	Hit Start
8.36e-255	1	886	1	1007
8.36e-255	1	886	1	1007
1.51e-252	1	886	1	1007
1.51e-252	1	886	1	1007
1.82e-252	26	886	16	989

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
6.30e-254	1	886	1	1007	Structure Of Beta-galactosidase From Aspergillus Niger [Aspergillus niger CBS 513.88]
1.78e-253	1	886	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]
3.91e-253	1	886	4	1005	Crystal structure of beta-galactosidase from Aspergillus oryzae in complex with galactose [Aspergillus oryzae]
2.27e-240	34	886	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.]
1.96e-226	30	886	18	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]

Swiss-Prot Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
2.82e-258	10	886	13	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
4.07e-255	1	886	4	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
8.14e-255	1	886	4	1006	Probable beta-galactosidase A OS=Neosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163) OX=451804 GN=lacA PE=3 SV=2
2.68e-253	1	886	1	1007	Beta-galactosidase A OS=Aspergillus niger (strain CBS 513.88 / FGSC A1513) OX=425011 GN=lacA PE=1 SV=1
1.42e-252	1	886	4	1005	Beta-galactosidase A OS=Aspergillus oryzae (strain ATCC 42149 / RIB 40) OX=510516 GN=lacA PE=1 SV=1

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
0.992566	0.007456

TMHMM Annotations help

There is no transmembrane helices in KLU89827.1.