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CAZyme Information: MGYG000002762_01463

You are here: Home > Sequence: MGYG000002762_01463

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 CAG-485 sp900554845
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Muribaculaceae; CAG-485; CAG-485 sp900554845
CAZyme ID MGYG000002762_01463
CAZy Family GH32
CAZyme Description Levanase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
611 MGYG000002762_68|CGC1 67797.25 5.7718
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000002762 3275168 MAG Netherlands Europe
Gene Location Start: 11437;  End: 13272  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.26 3.2.1.64 3.2.1.80 3.2.1.65 3.2.1.153

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH32 144 445 3.3e-88 0.9829351535836177

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd18622 GH32_Inu-like 5.82e-152 150 437 2 289
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.
COG1621 SacC 9.57e-135 132 611 21 485
Sucrose-6-phosphate hydrolase SacC, GH32 family [Carbohydrate transport and metabolism].
smart00640 Glyco_32 2.01e-132 144 574 1 437
Glycosyl hydrolases family 32.
pfam00251 Glyco_hydro_32N 1.33e-105 144 446 1 305
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.
TIGR01322 scrB_fam 2.88e-79 132 584 6 444
sucrose-6-phosphate hydrolase. [Energy metabolism, Biosynthesis and degradation of polysaccharides]

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
ASB38314.1 0.0 3 611 3 612
ANU64796.2 0.0 3 611 3 612
QQR09059.1 0.0 3 611 3 612
QCD36721.1 0.0 4 611 4 613
QJR98329.1 0.0 8 610 1 604

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1Y4W_A 1.04e-101 137 610 5 513
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 1.23e-80 139 610 28 513
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 2.26e-78 133 586 2 479
ChainA, Invertase [Schwanniomyces occidentalis],3KF3_B Chain B, Invertase [Schwanniomyces occidentalis]
3KF5_A 2.44e-78 133 586 5 482
ChainA, Invertase [Schwanniomyces occidentalis],3KF5_B Chain B, Invertase [Schwanniomyces occidentalis]
3U75_A 3.27e-77 133 586 28 505
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 9.17e-122 125 611 16 510
Levanase OS=Bacillus subtilis (strain 168) OX=224308 GN=sacC PE=1 SV=1
Q96TU3 3.51e-101 125 610 16 532
Extracellular exo-inulinase inuE OS=Aspergillus awamori OX=105351 GN=inuE PE=1 SV=1
A2R0E0 1.37e-100 137 610 24 532
Extracellular exo-inulinase inuE OS=Aspergillus niger (strain CBS 513.88 / FGSC A1513) OX=425011 GN=inuE PE=2 SV=1
E1ABX2 2.72e-100 137 610 24 532
Extracellular exo-inulinase inuE OS=Aspergillus ficuum OX=5058 GN=exoI PE=1 SV=1
Q76HP6 2.72e-100 137 610 24 532
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
0.000275 0.998963 0.000192 0.000197 0.000185 0.000168

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000002762_01463.