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CAZyme Information: FOIG_05427-t36_2-p1

You are here: Home > Sequence: FOIG_05427-t36_2-p1

Basic Information | Genomic context | Full Sequence | Enzyme annotations |  CAZy signature domains |  CDD domains | CAZyme hits | PDB hits | Swiss-Prot hits | SignalP and Lipop annotations | TMHMM annotations

Basic Information help

Species Fusarium odoratissimum
Lineage Ascomycota; Sordariomycetes; ; Nectriaceae; Fusarium; Fusarium odoratissimum
CAZyme ID FOIG_05427-t36_2-p1
CAZy Family CE4
CAZyme Description beta-glucosidase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
893 96206.28 5.1002
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_FodoratissimumNRRL54006 16975 1089451 341 16634
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.21:43 3.2.1.-:1

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH3 100 321 6.3e-57 0.9861111111111112

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
396478 Glyco_hydro_3_C 9.96e-53 422 654 2 216
Glycosyl hydrolase family 3 C-terminal domain. This domain is involved in catalysis and may be involved in binding beta-glucan. This domain is found associated with pfam00933.
224389 BglX 4.95e-39 101 469 55 388
Periplasmic beta-glucosidase and related glycosidases [Carbohydrate transport and metabolism].
178629 PLN03080 6.27e-31 66 707 51 654
Probable beta-xylosidase; Provisional
395747 Glyco_hydro_3 1.68e-29 112 361 74 316
Glycosyl hydrolase family 3 N terminal domain.
185053 PRK15098 1.49e-28 127 696 120 658
beta-glucosidase BglX.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
0.0 1 893 1 893
0.0 1 893 1 893
0.0 1 893 1 921
0.0 1 893 1 921
0.0 1 893 1 921

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
0.0 31 893 11 852
Chain A, Beta-glucosidase [Rasamsonia emersonii],5JU6_B Chain B, Beta-glucosidase [Rasamsonia emersonii],5JU6_C Chain C, Beta-glucosidase [Rasamsonia emersonii],5JU6_D Chain D, Beta-glucosidase [Rasamsonia emersonii]
0.0 39 892 1 838
Three-dimensional structures of two heavily N-glycosylated Aspergillus sp. Family GH3 beta-D-glucosidases [Aspergillus oryzae],5FJJ_B Three-dimensional structures of two heavily N-glycosylated Aspergillus sp. Family GH3 beta-D-glucosidases [Aspergillus oryzae],5FJJ_C Three-dimensional structures of two heavily N-glycosylated Aspergillus sp. Family GH3 beta-D-glucosidases [Aspergillus oryzae],5FJJ_D Three-dimensional structures of two heavily N-glycosylated Aspergillus sp. Family GH3 beta-D-glucosidases [Aspergillus oryzae]
0.0 42 892 3 840
Three-dimensional structures of two heavily N-glycosylated Aspergillus sp. Family GH3 beta-D-glucosidases [Aspergillus fumigatus],5FJI_B Three-dimensional structures of two heavily N-glycosylated Aspergillus sp. Family GH3 beta-D-glucosidases [Aspergillus fumigatus]
0.0 40 892 1 837
Crystal structure of beta-glucosidase 1 from Aspergillus aculeatus [Aspergillus aculeatus],4IIB_B Crystal structure of beta-glucosidase 1 from Aspergillus aculeatus [Aspergillus aculeatus],4IIC_A Crystal structure of beta-glucosidase 1 from Aspergillus aculeatus in complex with isofagomine [Aspergillus aculeatus],4IIC_B Crystal structure of beta-glucosidase 1 from Aspergillus aculeatus in complex with isofagomine [Aspergillus aculeatus],4IID_A Crystal structure of beta-glucosidase 1 from Aspergillus aculeatus in complex with 1-deoxynojirimycin [Aspergillus aculeatus],4IID_B Crystal structure of beta-glucosidase 1 from Aspergillus aculeatus in complex with 1-deoxynojirimycin [Aspergillus aculeatus],4IIE_A Crystal structure of beta-glucosidase 1 from Aspergillus aculeatus in complex with calystegine B(2) [Aspergillus aculeatus],4IIE_B Crystal structure of beta-glucosidase 1 from Aspergillus aculeatus in complex with calystegine B(2) [Aspergillus aculeatus],4IIF_A Crystal structure of beta-glucosidase 1 from Aspergillus aculeatus in complex with castanospermine [Aspergillus aculeatus],4IIF_B Crystal structure of beta-glucosidase 1 from Aspergillus aculeatus in complex with castanospermine [Aspergillus aculeatus],4IIG_A Crystal structure of beta-glucosidase 1 from Aspergillus aculeatus in complex with D-glucose [Aspergillus aculeatus],4IIG_B Crystal structure of beta-glucosidase 1 from Aspergillus aculeatus in complex with D-glucose [Aspergillus aculeatus],4IIH_A Crystal structure of beta-glucosidase 1 from Aspergillus aculeatus in complex with thiocellobiose [Aspergillus aculeatus],4IIH_B Crystal structure of beta-glucosidase 1 from Aspergillus aculeatus in complex with thiocellobiose [Aspergillus aculeatus]
0.0 37 892 12 856
Structural studies of a Glycoside Hydrolase Family 3 beta-glucosidase from the Model Fungus Neurospora crassa [Neurospora crassa OR74A],5NBS_B Structural studies of a Glycoside Hydrolase Family 3 beta-glucosidase from the Model Fungus Neurospora crassa [Neurospora crassa OR74A]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
0.0 26 892 7 857
Probable beta-glucosidase A OS=Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC 167) OX=332952 GN=bglA PE=3 SV=1
0.0 26 892 7 857
Probable beta-glucosidase A OS=Aspergillus oryzae (strain ATCC 42149 / RIB 40) OX=510516 GN=bglA PE=1 SV=1
0.0 26 892 7 857
Probable beta-glucosidase A OS=Aspergillus terreus (strain NIH 2624 / FGSC A1156) OX=341663 GN=bglA PE=3 SV=1
0.0 31 892 11 856
Beta-glucosidase A OS=Aspergillus kawachii (strain NBRC 4308) OX=1033177 GN=bglA PE=1 SV=2
0.0 42 892 32 869
Probable beta-glucosidase A OS=Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) OX=330879 GN=bglA PE=1 SV=1

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI CS Position
0.006647 0.993343 CS pos: 24-25. Pr: 0.4239

TMHMM  Annotations      help

There is no transmembrane helices in FOIG_05427-t36_2-p1.