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CAZyme Information: ATEG_05860-t26_1-p1

You are here: Home > Sequence: ATEG_05860-t26_1-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 Aspergillus terreus
Lineage Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus terreus
CAZyme ID ATEG_05860-t26_1-p1
CAZy Family GH3
CAZyme Description predicted protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
584 65771.19 6.1038
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_AterreusNIH2624 10551 341663 150 10401
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.26:2

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH32 18 365 3.9e-60 0.9658703071672355

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
350133 GH32_XdINV-like 7.87e-163 24 365 1 337
glycoside hydrolase family 32 protein such as Xanthophyllomyces dendrorhous beta-fructofuranosidase (Inv;Xd-INV;XdINV). This subfamily of glycosyl hydrolase family GH32 includes fructan:fructan 1-fructosyltransferase (FT, EC 2.4.1.100) and beta-fructofuranosidase (invertase or Inv, EC 3.2.1.26), among others. These enzymes cleave sucrose into fructose and glucose via beta-fructofuranosidase activity, producing invert sugar that is a mixture of dextrorotatory D-glucose and levorotatory D-fructose, thus named invertase (EC 3.2.1.26). These retaining enzymes (i.e. they retain the configuration at anomeric carbon atom of the substrate) catalyze hydrolysis in two steps involving a covalent glycosyl enzyme intermediate: an aspartate located close to the N-terminus acts as the catalytic nucleophile and a glutamate acts as the general acid/base; a conserved aspartate residue in the Arg-Asp-Pro (RDP) motif stabilizes the transition state. Xanthophyllomyces dendrorhous beta-fructofuranosidase (XdINV) also catalyzes the synthesis of fructooligosaccharides (FOS, a beneficial prebiotic), producing neo-FOS, making it an interesting biotechnology target. Structural studies show plasticity of its active site, having a flexible loop that is essential in binding sucrose and beta(2-1)-linked oligosaccharide, making it a valuable biocatalyst to produce novel bioconjugates. The breakdown of sucrose is widely used as a carbon or energy source by bacteria, fungi, and plants. Invertase is used commercially in the confectionery industry, since fructose has a sweeter taste than sucrose and a lower tendency to crystallize. A common structural feature of all these enzymes is a 5-bladed beta-propeller domain, similar to GH43, that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.
350110 GH32_FFase 2.84e-58 24 363 1 281
Glycosyl hydrolase family 32, beta-fructosidases. Glycosyl hydrolase family GH32 cleaves sucrose into fructose and glucose via beta-fructofuranosidase activity, producing invert sugar that is a mixture of dextrorotatory D-glucose and levorotatory D-fructose, thus named invertase (EC 3.2.1.26). This family also contains other fructofuranosidases such as inulinase (EC 3.2.1.7), exo-inulinase (EC 3.2.1.80), levanase (EC 3.2.1.65), and transfructosidases such sucrose:sucrose 1-fructosyltransferase (EC 2.4.1.99), fructan:fructan 1-fructosyltransferase (EC 2.4.1.100), sucrose:fructan 6-fructosyltransferase (EC 2.4.1.10), fructan:fructan 6G-fructosyltransferase (EC 2.4.1.243) and levan fructosyltransferases (EC 2.4.1.-). These retaining enzymes (i.e. they retain the configuration at anomeric carbon atom of the substrate) catalyze hydrolysis in two steps involving a covalent glycosyl enzyme intermediate: an aspartate located close to the N-terminus acts as the catalytic nucleophile and a glutamate acts as the general acid/base; a conserved aspartate residue in the Arg-Asp-Pro (RDP) motif stabilizes the transition state. These enzymes are predicted to display a 5-fold beta-propeller fold as found for GH43 and CH68. The breakdown of sucrose is widely used as a carbon or energy source by bacteria, fungi, and plants. Invertase is used commercially in the confectionery industry, since fructose has a sweeter taste than sucrose and a lower tendency to crystallize. A common structural feature of all these enzymes is a 5-bladed beta-propeller domain, similar to GH43, that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.
214757 Glyco_32 6.55e-58 18 535 1 436
Glycosyl hydrolases family 32.
395193 Glyco_hydro_32N 3.15e-43 21 365 4 299
Glycosyl hydrolases family 32 N-terminal domain. This domain corresponds to the N-terminal domain of glycosyl hydrolase family 32 which forms a five bladed beta propeller structure.
224536 SacC 6.38e-43 13 547 28 461
Sucrose-6-phosphate hydrolase SacC, GH32 family [Carbohydrate transport and metabolism].

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
4.47e-145 5 578 40 635
3.80e-143 13 549 46 596
1.47e-142 13 546 19 588
1.89e-142 13 578 46 624
1.77e-141 4 544 38 585

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1.36e-44 11 541 24 594
Crystal structure of fructosyltransferase (wild-type) from A. japonicus [Aspergillus japonicus],3LFI_A Crystal structure of fructosyltransferase (wild-type) from A. japonicus in complex with glucose [Aspergillus japonicus],3LFI_B Crystal structure of fructosyltransferase (wild-type) from A. japonicus in complex with glucose [Aspergillus japonicus]
1.89e-44 13 562 65 609
Chain A, Beta-fructofuranosidase [Phaffia rhodozyma],5ANN_B Chain B, Beta-fructofuranosidase [Phaffia rhodozyma]
1.89e-44 13 562 65 609
Chain A, Beta-fructofuranosidase [Phaffia rhodozyma],6S82_B Chain B, Beta-fructofuranosidase [Phaffia rhodozyma]
1.64e-43 11 541 24 594
Crystal Structure of A. japonicus CB05 [Aspergillus japonicus],3LDR_A Crystal structure of fructosyltransferase (D191A) from A. japonicus in complex with 1-Kestose [Aspergillus japonicus],3LEM_A Crystal structure of fructosyltransferase (D191A) from A. japonicus in complex with Nystose [Aspergillus japonicus],3LIG_A Crystal structure of fructosyltransferase (D191A) from A. japonicus [Aspergillus japonicus],3LIH_A Crystal structure of fructosyltransferase (D191A) from A. japonicus in complex with raffinose [Aspergillus japonicus]
2.21e-43 13 562 63 607
Chain A, Beta-fructofuranosidase [Phaffia rhodozyma],5FK7_B Chain B, Beta-fructofuranosidase [Phaffia rhodozyma],5FK8_A Chain A, Beta-fructofuranosidase [Phaffia rhodozyma],5FK8_B Chain B, Beta-fructofuranosidase [Phaffia rhodozyma],5FKB_A Chain A, BETA-FRUCTOFURANOSIDASE [Phaffia rhodozyma],5FKB_B Chain B, BETA-FRUCTOFURANOSIDASE [Phaffia rhodozyma],5FKC_A Chain A, BETA-FRUCTOFURANOSIDASE [Phaffia rhodozyma],5FKC_B Chain B, BETA-FRUCTOFURANOSIDASE [Phaffia rhodozyma],5FMC_A Chain A, Beta-fructofuranosidase [Phaffia rhodozyma],5FMC_B Chain B, Beta-fructofuranosidase [Phaffia rhodozyma]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
5.36e-27 1 550 14 511
Extracellular exo-inulinase inuE OS=Aspergillus awamori OX=105351 GN=inuE PE=1 SV=1
1.36e-25 14 582 125 657
Beta-fructofuranosidase 1 OS=Zea mays OX=4577 GN=IVR1 PE=3 SV=1
7.18e-25 14 544 116 602
Acid beta-fructofuranosidase OS=Vigna radiata var. radiata OX=3916 GN=INVA PE=1 SV=1
3.92e-24 14 544 108 594
Acid beta-fructofuranosidase OS=Vicia faba OX=3906 GN=VCINV PE=2 SV=1
9.49e-24 14 544 116 604
Acid beta-fructofuranosidase OS=Phaseolus vulgaris OX=3885 PE=2 SV=1

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI CS Position
0.999949 0.000123

TMHMM  Annotations      help

There is no transmembrane helices in ATEG_05860-t26_1-p1.