logo
sublogo
You are browsing environment: FUNGIDB
help

CAZyme Information: GAQ10219.1

You are here: Home > Sequence: GAQ10219.1

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 lentulus
Lineage Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus lentulus
CAZyme ID GAQ10219.1
CAZy Family GH71|CBM24|CBM24
CAZyme Description extracellular endo-inulinase inu2
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
1419 152167.56 4.9057
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_AlentulusIFM54703 9916 N/A 259 9657
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.80:10 3.2.1.65:10 3.2.1.26:7 3.2.1.153:5 3.2.1.64:3 2.4.1.99:3 3.2.1.80:2 3.2.1.26:1 3.2.1.80:2 3.2.1.26:1 3.2.1.7:10

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH32 935 1260 3.9e-76 0.9965870307167235
GH32 34 297 1.3e-72 0.764505119453925
CBM38 339 466 2.1e-34 0.9612403100775194
CBM38 506 621 3.4e-31 0.9147286821705426

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
350134 GH32_Inu-like 8.97e-114 940 1246 1 289
glycoside hydrolase family 32 protein such as Aspergillus ficuum endo-inulinase (Inu2). This subfamily of glycosyl hydrolase family GH32 includes endo-inulinase (inu2, EC 3.2.1.7), exo-inulinase (Inu1, EC 3.2.1.80), invertase (EC 3.2.1.26), and levan fructotransferase (LftA, EC 4.2.2.16), 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. 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 4.89e-110 935 1381 1 437
Glycosyl hydrolases family 32.
350134 GH32_Inu-like 1.02e-106 40 298 2 232
glycoside hydrolase family 32 protein such as Aspergillus ficuum endo-inulinase (Inu2). This subfamily of glycosyl hydrolase family GH32 includes endo-inulinase (inu2, EC 3.2.1.7), exo-inulinase (Inu1, EC 3.2.1.80), invertase (EC 3.2.1.26), and levan fructotransferase (LftA, EC 4.2.2.16), 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. 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.
224536 SacC 7.45e-91 925 1409 23 477
Sucrose-6-phosphate hydrolase SacC, GH32 family [Carbohydrate transport and metabolism].
395193 Glyco_hydro_32N 3.61e-89 935 1260 1 308
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.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
0.0 599 1417 2 833
3.02e-275 10 879 8 702
2.79e-269 9 870 10 692
1.01e-267 924 1417 14 505
5.64e-254 929 1415 35 519

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1.38e-237 922 1417 20 513
First crystal structure of an endo-inulinase, from Aspergillus ficuum: structural analysis and comparison with other GH32 enzymes. [Aspergillus ficuum],3SC7_X First crystal structure of an endo-inulinase, from Aspergillus ficuum: structural analysis and comparison with other GH32 enzymes. [Aspergillus ficuum]
9.45e-167 25 879 3 517
Crystal structure of exo-inulinase from Aspergillus awamori in spacegroup P21 [Aspergillus awamori],1Y9G_A Crystal structure of exo-inulinase from Aspergillus awamori complexed with fructose [Aspergillus awamori],1Y9M_A Crystal structure of exo-inulinase from Aspergillus awamori in spacegroup P212121 [Aspergillus awamori]
5.50e-55 30 295 8 252
Structure of Saccharomyces cerevisiae invertase [Saccharomyces cerevisiae S288C],4EQV_B Structure of Saccharomyces cerevisiae invertase [Saccharomyces cerevisiae S288C],4EQV_C Structure of Saccharomyces cerevisiae invertase [Saccharomyces cerevisiae S288C],4EQV_D Structure of Saccharomyces cerevisiae invertase [Saccharomyces cerevisiae S288C],4EQV_E Structure of Saccharomyces cerevisiae invertase [Saccharomyces cerevisiae S288C],4EQV_F Structure of Saccharomyces cerevisiae invertase [Saccharomyces cerevisiae S288C],4EQV_G Structure of Saccharomyces cerevisiae invertase [Saccharomyces cerevisiae S288C],4EQV_H Structure of Saccharomyces cerevisiae invertase [Saccharomyces cerevisiae S288C]
6.98e-55 931 1261 10 330
Chain A, Invertase [Schwanniomyces occidentalis],3KF3_B Chain B, Invertase [Schwanniomyces occidentalis]
7.44e-55 931 1261 13 333
Chain A, Invertase [Schwanniomyces occidentalis],3KF5_B Chain B, Invertase [Schwanniomyces occidentalis]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
2.00e-247 25 879 28 702
Putative glycosyl hydrolase ecdE OS=Aspergillus rugulosus OX=41736 GN=ecdE PE=3 SV=1
3.49e-241 929 1413 17 499
Putative glycosyl hydrolase ecdF OS=Aspergillus rugulosus OX=41736 GN=ecdF PE=3 SV=1
5.05e-237 922 1417 20 513
Extracellular endo-inulinase inuA OS=Aspergillus niger OX=5061 GN=inuA PE=1 SV=1
7.12e-237 922 1417 20 513
Extracellular endo-inulinase inu2 OS=Aspergillus ficuum OX=5058 GN=inu2 PE=1 SV=1
7.91e-236 922 1417 20 513
Extracellular endo-inulinase inuB OS=Aspergillus niger OX=5061 GN=inuB PE=1 SV=1

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI CS Position
0.000185 0.999803 CS pos: 22-23. Pr: 0.9778

TMHMM  Annotations      help

There is no transmembrane helices in GAQ10219.1.