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CAZyme Information: MGYG000000400_00448

You are here: Home > Sequence: MGYG000000400_00448

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
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Muribaculaceae; UBA7173;
CAZyme ID MGYG000000400_00448
CAZy Family GH32
CAZyme Description Levanase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
547 62249.11 6.8935
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000400 2908659 MAG Sweden Europe
Gene Location Start: 57052;  End: 58695  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000000400_00448.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH32 121 405 1.7e-80 0.9965870307167235

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd18622 GH32_Inu-like 3.82e-133 126 392 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.
smart00640 Glyco_32 2.42e-97 121 507 1 437
Glycosyl hydrolases family 32.
pfam00251 Glyco_hydro_32N 3.19e-96 121 405 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.
COG1621 SacC 2.08e-90 108 507 20 449
Sucrose-6-phosphate hydrolase SacC, GH32 family [Carbohydrate transport and metabolism].
cd08996 GH32_FFase 1.20e-82 127 392 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.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QQA08746.1 8.21e-228 18 545 19 548
QUT41042.1 1.17e-227 18 545 19 548
ALJ39638.1 1.17e-227 18 545 19 548
AAO78188.1 1.65e-227 18 545 19 548
QUT73199.1 1.65e-227 18 545 19 548

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1Y4W_A 1.13e-64 112 545 3 517
Crystalstructure 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]
3RWK_X 4.42e-51 117 443 29 394
Firstcrystal 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]
3KF3_A 5.37e-51 114 370 7 284
ChainA, Invertase [Schwanniomyces occidentalis],3KF3_B Chain B, Invertase [Schwanniomyces occidentalis]
3KF5_A 5.68e-51 114 370 10 287
ChainA, Invertase [Schwanniomyces occidentalis],3KF5_B Chain B, Invertase [Schwanniomyces occidentalis]
3U75_A 6.06e-50 114 370 33 310
ChainA, Fructofuranosidase [Schwanniomyces occidentalis],3U75_B Chain B, Fructofuranosidase [Schwanniomyces occidentalis],3U75_C Chain C, Fructofuranosidase [Schwanniomyces occidentalis],3U75_D Chain D, Fructofuranosidase [Schwanniomyces occidentalis]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
P05656 7.15e-88 108 545 26 513
Levanase OS=Bacillus subtilis (strain 168) OX=224308 GN=sacC PE=1 SV=1
Q96TU3 9.45e-64 112 545 22 536
Extracellular exo-inulinase inuE OS=Aspergillus awamori OX=105351 GN=inuE PE=1 SV=1
A2R0E0 1.88e-62 112 545 22 536
Extracellular exo-inulinase inuE OS=Aspergillus niger (strain CBS 513.88 / FGSC A1513) OX=425011 GN=inuE PE=2 SV=1
E1ABX2 5.10e-62 112 507 22 496
Extracellular exo-inulinase inuE OS=Aspergillus ficuum OX=5058 GN=exoI PE=1 SV=1
Q76HP6 5.10e-62 112 507 22 496
Extracellular exo-inulinase inuE OS=Aspergillus niger OX=5061 GN=inuE PE=1 SV=1

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI LIPO_Sec_SPII TAT_Tat_SPI TATLIP_Sec_SPII PILIN_Sec_SPIII
0.003361 0.988364 0.007441 0.000290 0.000252 0.000254

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000000400_00448.