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CAZyme Information: MGYG000003799_00293

You are here: Home > Sequence: MGYG000003799_00293

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; Sodaliphilus;
CAZyme ID MGYG000003799_00293
CAZy Family GH20
CAZyme Description N,N'-diacetylchitobiase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
818 91767.54 5.5337
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000003799 2146274 MAG Canada North America
Gene Location Start: 139873;  End: 142329  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000003799_00293.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH20 292 707 1.1e-88 0.9762611275964391

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd06569 GH20_Sm-chitobiase-like 1.10e-164 294 724 1 433
The chitobiase of Serratia marcescens is a beta-N-1,4-acetylhexosaminidase with a glycosyl hydrolase family 20 (GH20) domain that hydrolyzes the beta-1,4-glycosidic linkages in oligomers derived from chitin. Chitin is degraded by a two step process: i) a chitinase hydrolyzes the chitin to oligosaccharides and disaccharides such as di-N-acetyl-D-glucosamine and chitobiose, ii) chitobiase then further degrades these oligomers into monomers. The GH20 hexosaminidases are thought to act via a catalytic mechanism in which the catalytic nucleophile is not provided by solvent or the enzyme, but by the substrate itself.
pfam00728 Glyco_hydro_20 6.07e-95 298 707 1 345
Glycosyl hydrolase family 20, catalytic domain. This domain has a TIM barrel fold.
cd06563 GH20_chitobiase-like 4.38e-89 298 713 1 352
The chitobiase of Serratia marcescens is a beta-N-1,4-acetylhexosaminidase with a glycosyl hydrolase family 20 (GH20) domain that hydrolyzes the beta-1,4-glycosidic linkages in oligomers derived from chitin. Chitin is degraded by a two step process: i) a chitinase hydrolyzes the chitin to oligosaccharides and disaccharides such as di-N-acetyl-D-glucosamine and chitobiose, ii) chitobiase then further degrades these oligomers into monomers. This GH20 domain family includes an N-acetylglucosamidase (GlcNAcase A) from Pseudoalteromonas piscicida and an N-acetylhexosaminidase (SpHex) from Streptomyces plicatus. SpHex lacks the C-terminal PKD (polycystic kidney disease I)-like domain found in the chitobiases. The GH20 hexosaminidases are thought to act via a catalytic mechanism in which the catalytic nucleophile is not provided by solvent or the enzyme, but by the substrate itself.
COG3525 Chb 4.82e-78 247 776 206 699
N-acetyl-beta-hexosaminidase [Carbohydrate transport and metabolism].
cd06562 GH20_HexA_HexB-like 3.50e-54 298 714 1 332
Beta-N-acetylhexosaminidases catalyze the removal of beta-1,4-linked N-acetyl-D-hexosamine residues from the non-reducing ends of N-acetyl-beta-D-hexosaminides including N-acetylglucosides and N-acetylgalactosides. The hexA and hexB genes encode the alpha- and beta-subunits of the two major beta-N-acetylhexosaminidase isoenzymes, N-acetyl-beta-D-hexosaminidase A (HexA) and beta-N-acetylhexosaminidase B (HexB). Both the alpha and the beta catalytic subunits have a TIM-barrel fold and belong to the glycosyl hydrolase family 20 (GH20). The HexA enzyme is a heterodimer containing one alpha and one beta subunit while the HexB enzyme is a homodimer containing two beta-subunits. Hexosaminidase mutations cause an inability to properly hydrolyze certain sphingolipids which accumulate in lysosomes within the brain, resulting in the lipid storage disorders Tay-Sachs and Sandhoff. Mutations in the alpha subunit cause in a deficiency in the HexA enzyme and result in Tay-Sachs, mutations in the beta-subunit cause in a deficiency in both HexA and HexB enzymes and result in Sandhoff disease. In both disorders GM(2) gangliosides accumulate in lysosomes. The GH20 hexosaminidases are thought to act via a catalytic mechanism in which the catalytic nucleophile is not provided by solvent or the enzyme, but by the substrate itself.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
AHF12728.1 7.91e-225 1 812 1 829
QMI79073.1 1.47e-201 21 814 29 831
QBJ17558.1 4.15e-201 21 814 29 831
VTZ55501.1 7.32e-201 21 814 14 816
QUT34090.1 8.29e-201 21 814 29 831

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1C7T_A 5.38e-80 31 797 23 842
ChainA, BETA-N-ACETYLHEXOSAMINIDASE [Serratia marcescens]
1QBA_A 7.43e-80 31 797 23 842
BACTERIALCHITOBIASE, GLYCOSYL HYDROLASE FAMILY 20 [Serratia marcescens],1QBB_A BACTERIAL CHITOBIASE COMPLEXED WITH CHITOBIOSE (DINAG) [Serratia marcescens]
1C7S_A 2.69e-79 31 797 23 842
ChainA, BETA-N-ACETYLHEXOSAMINIDASE [Serratia marcescens]
6EZR_A 2.96e-61 248 746 210 638
Crystalstructure of GH20 Exo beta-N-Acetylglucosaminidase from Vibrio harveyi [Vibrio harveyi],6EZR_B Crystal structure of GH20 Exo beta-N-Acetylglucosaminidase from Vibrio harveyi [Vibrio harveyi],6EZS_A Crystal structure of GH20 Exo beta-N-Acetylglucosaminidase from Vibrio harveyi in complex with N-acetylglucosamine [Vibrio harveyi],6EZS_B Crystal structure of GH20 Exo beta-N-Acetylglucosaminidase from Vibrio harveyi in complex with N-acetylglucosamine [Vibrio harveyi],6K35_A Crystal structure of GH20 exo beta-N-acetylglucosaminidase from Vibrio harveyi in complex with NAG-thiazoline [Vibrio harveyi],6K35_B Crystal structure of GH20 exo beta-N-acetylglucosaminidase from Vibrio harveyi in complex with NAG-thiazoline [Vibrio harveyi]
6EZT_A 3.51e-60 248 746 207 635
Crystalstructure of GH20 Exo beta-N-Acetylglucosaminidase D437A inactive mutant from Vibrio harveyi [Vibrio harveyi],6EZT_B Crystal structure of GH20 Exo beta-N-Acetylglucosaminidase D437A inactive mutant from Vibrio harveyi [Vibrio harveyi]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
P13670 8.37e-87 7 776 12 846
N,N'-diacetylchitobiase OS=Vibrio harveyi OX=669 GN=chb PE=1 SV=1
Q04786 6.46e-79 182 776 200 809
Beta-hexosaminidase OS=Vibrio vulnificus OX=672 GN=hex PE=3 SV=1
Q54468 1.19e-78 10 797 26 869
Chitobiase OS=Serratia marcescens OX=615 GN=chb PE=1 SV=1
P49007 9.91e-69 182 711 211 731
Beta-hexosaminidase B OS=Pseudoalteromonas piscicida OX=43662 GN=nag096 PE=3 SV=1
P96155 8.12e-58 231 700 193 600
Beta-hexosaminidase OS=Vibrio furnissii OX=29494 GN=exoI 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
0.000377 0.998723 0.000226 0.000228 0.000210 0.000194

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000003799_00293.