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CAZyme Information: MGYG000000824_01566

You are here: Home > Sequence: MGYG000000824_01566

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 sp900552315
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Muribaculaceae; CAG-485; CAG-485 sp900552315
CAZyme ID MGYG000000824_01566
CAZy Family GH32
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
613 67187.51 5.0819
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000824 2120674 MAG China Asia
Gene Location Start: 2702;  End: 4543  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 142 443 2e-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 2.44e-147 148 435 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.
smart00640 Glyco_32 4.40e-124 142 572 1 437
Glycosyl hydrolases family 32.
COG1621 SacC 8.66e-121 137 610 28 486
Sucrose-6-phosphate hydrolase SacC, GH32 family [Carbohydrate transport and metabolism].
pfam00251 Glyco_hydro_32N 1.88e-103 142 435 1 297
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 2.76e-78 148 435 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
QJR98329.1 0.0 5 608 1 604
QCD36721.1 1.57e-306 5 609 12 613
ASB38314.1 1.93e-303 1 609 4 612
ANU64796.2 1.93e-303 1 609 4 612
QQR09059.1 1.93e-303 1 609 4 612

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1Y4W_A 2.80e-102 134 611 4 516
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 7.37e-79 121 608 16 513
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]
3U75_A 1.19e-78 121 584 18 505
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]
3U14_A 2.34e-78 121 584 18 505
ChainA, Fructofuranosidase [Schwanniomyces occidentalis],3U14_B Chain B, Fructofuranosidase [Schwanniomyces occidentalis],6S1T_A Chain A, Fructofuranosidase [Schwanniomyces occidentalis],6S1T_B Chain B, Fructofuranosidase [Schwanniomyces occidentalis],6S2B_A Chain A, Fructofuranosidase [Schwanniomyces occidentalis],6S2B_B Chain B, Fructofuranosidase [Schwanniomyces occidentalis]
3KF5_A 3.58e-78 127 584 1 482
ChainA, 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
P05656 5.13e-114 126 609 23 510
Levanase OS=Bacillus subtilis (strain 168) OX=224308 GN=sacC PE=1 SV=1
Q96TU3 2.64e-101 134 611 23 535
Extracellular exo-inulinase inuE OS=Aspergillus awamori OX=105351 GN=inuE PE=1 SV=1
Q76HP6 2.88e-100 134 611 23 535
Extracellular exo-inulinase inuE OS=Aspergillus niger OX=5061 GN=inuE PE=1 SV=1
E1ABX2 2.88e-100 134 611 23 535
Extracellular exo-inulinase inuE OS=Aspergillus ficuum OX=5058 GN=exoI PE=1 SV=1
A2R0E0 1.58e-99 134 611 23 535
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
0.000969 0.640398 0.357641 0.000378 0.000323 0.000264

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000000824_01566.