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CAZyme Information: MGYG000000012_02573

You are here: Home > Sequence: MGYG000000012_02573

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 Bacillus subtilis
Lineage Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; Bacillus subtilis
CAZyme ID MGYG000000012_02573
CAZy Family GH32
CAZyme Description Levanase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
677 MGYG000000012_3|CGC6 75887.3 9.04
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000012 4053580 Isolate United Kingdom Europe
Gene Location Start: 413998;  End: 416031  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000000012_02573.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH32 39 349 4.3e-109 0.9965870307167235
CBM66 520 673 7.1e-55 0.9935483870967742

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
COG1621 SacC 0.0 7 511 1 486
Sucrose-6-phosphate hydrolase SacC, GH32 family [Carbohydrate transport and metabolism].
cd18622 GH32_Inu-like 2.03e-177 44 336 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 5.84e-173 39 473 1 437
Glycosyl hydrolases family 32.
pfam00251 Glyco_hydro_32N 6.13e-138 39 349 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.
cd08996 GH32_FFase 1.23e-100 45 336 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
QRZ91563.1 0.0 1 677 1 677
AFI29216.1 0.0 1 677 9 685
ASB61793.1 0.0 1 677 1 677
AUS10781.1 0.0 1 677 1 677
AUZ39607.1 0.0 1 677 1 677

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1Y4W_A 1.78e-122 30 513 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]
4B1L_A 1.74e-102 515 677 3 165
CarbohydrateBinding Module Cbm66 From Bacillus Subtilis [Bacillus subtilis]
4AZZ_A 2.22e-102 515 677 2 164
Carbohydratebinding module CBM66 from Bacillus subtilis [Bacillus subtilis],4AZZ_B Carbohydrate binding module CBM66 from Bacillus subtilis [Bacillus subtilis]
3RWK_X 2.73e-102 33 506 27 510
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]
4B1M_A 3.49e-102 515 677 23 185
CarbohydrateBinding Module Cbm66 From Bacillus Subtilis [Bacillus subtilis],4B1M_B Carbohydrate Binding Module Cbm66 From Bacillus Subtilis [Bacillus subtilis],4B1M_C Carbohydrate Binding Module Cbm66 From Bacillus Subtilis [Bacillus subtilis]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
P05656 0.0 1 677 1 677
Levanase OS=Bacillus subtilis (strain 168) OX=224308 GN=sacC PE=1 SV=1
O31411 7.33e-143 27 513 390 879
Levanase (Fragment) OS=Bacillus sp. (strain L7) OX=62626 PE=1 SV=2
Q76HP6 5.09e-124 16 513 8 536
Extracellular exo-inulinase inuE OS=Aspergillus niger OX=5061 GN=inuE PE=1 SV=1
E1ABX2 5.09e-124 16 513 8 536
Extracellular exo-inulinase inuE OS=Aspergillus ficuum OX=5058 GN=exoI PE=1 SV=1
A2R0E0 4.00e-123 16 513 8 536
Extracellular exo-inulinase inuE OS=Aspergillus niger (strain CBS 513.88 / FGSC A1513) OX=425011 GN=inuE PE=2 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
0.000274 0.998857 0.000247 0.000225 0.000197 0.000184

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000000012_02573.