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CAZyme Information: MGYG000001360_02268

You are here: Home > Sequence: MGYG000001360_02268

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 Prevotella salivae
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Prevotella; Prevotella salivae
CAZyme ID MGYG000001360_02268
CAZy Family GH20
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
644 73902.41 8.5938
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001360 3139873 Isolate not provided not provided
Gene Location Start: 2717887;  End: 2719821  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000001360_02268.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH20 145 468 5e-71 0.9703264094955489

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd06564 GH20_DspB_LnbB-like 1.30e-114 152 468 3 326
Glycosyl hydrolase family 20 (GH20) catalytic domain of dispersin B (DspB), lacto-N-biosidase (LnbB) and related proteins. Dispersin B is a soluble beta-N-acetylglucosamidase found in bacteria that hydrolyzes the beta-1,6-linkages of PGA (poly-beta-(1,6)-N-acetylglucosamine), a major component of the extracellular polysaccharide matrix. Lacto-N-biosidase hydrolyzes lacto-N-biose (LNB) type I oligosaccharides at the nonreducing terminus to produce lacto-N-biose as part of the GNB/LNB (galacto-N-biose/lacto-N-biose I) degradation pathway. The lacto-N-biosidase from Bifidobacterium bifidum has this GH20 domain, a carbohydrate binding module 32, and a bacterial immunoglobulin-like domain 2, as well as a YSIRK signal peptide and a G5 membrane anchor at the N and C termini, respectively. 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 5.62e-42 149 468 1 345
Glycosyl hydrolase family 20, catalytic domain. This domain has a TIM barrel fold.
cd06563 GH20_chitobiase-like 6.31e-42 149 481 1 356
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.
cd02742 GH20_hexosaminidase 2.61e-38 152 466 2 302
Beta-N-acetylhexosaminidases of glycosyl hydrolase family 20 (GH20) 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. These enzymes are broadly distributed in microorganisms, plants and animals, and play roles in various key physiological and pathological processes. These processes include cell structural integrity, energy storage, cellular signaling, fertilization, pathogen defense, viral penetration, the development of carcinomas, inflammatory events and lysosomal storage disorders. The GH20 enzymes include the eukaryotic beta-N-acetylhexosaminidases A and B, the bacterial chitobiases, dispersin B, and lacto-N-biosidase. The GH20 hexosaminidases are thought to act via a catalytic mechanism in which the catalytic nucleophile is not provided by the solvent or the enzyme, but by the substrate itself.
COG3525 Chb 4.24e-37 54 467 148 614
N-acetyl-beta-hexosaminidase [Carbohydrate transport and metabolism].

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QUT50012.1 7.62e-271 23 640 25 649
QUU08144.1 2.27e-254 11 640 11 650
ASM65959.1 9.17e-254 11 640 11 650
QRP57273.1 9.17e-254 11 640 11 650
QQT77483.1 9.17e-254 11 640 11 650

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
6JQF_A 8.71e-86 23 643 86 734
Crystallizationanalysis of a beta-N-acetylhexosaminidase (Am2136) from Akkermansia muciniphila [Akkermansia muciniphila ATCC BAA-835]
6EZR_A 8.13e-27 45 493 162 637
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 7.87e-26 45 493 159 634
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]
7DUP_A 2.53e-25 50 496 33 523
ChainA, Beta-N-acetylhexosaminidase [Bacteroides thetaiotaomicron],7DVA_A Chain A, Beta-N-acetylhexosaminidase [Bacteroides thetaiotaomicron],7DVA_B Chain B, Beta-N-acetylhexosaminidase [Bacteroides thetaiotaomicron]
4C7D_A 3.36e-25 54 493 38 485
Structureand activity of the GH20 beta-N-acetylhexosaminidase from Streptomyces coelicolor A3(2) [Streptomyces coelicolor],4C7D_B Structure and activity of the GH20 beta-N-acetylhexosaminidase from Streptomyces coelicolor A3(2) [Streptomyces coelicolor],4C7F_A Structure and activity of the GH20 beta-N-acetylhexosaminidase from Streptomyces coelicolor A3(2) [Streptomyces coelicolor],4C7F_B Structure and activity of the GH20 beta-N-acetylhexosaminidase from Streptomyces coelicolor A3(2) [Streptomyces coelicolor]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
B2UPR7 1.77e-89 23 643 108 756
Beta-hexosaminidase Amuc_2136 OS=Akkermansia muciniphila (strain ATCC BAA-835 / DSM 22959 / JCM 33894 / BCRC 81048 / CCUG 64013 / CIP 107961 / Muc) OX=349741 GN=Amuc_2136 PE=1 SV=1
P96155 4.60e-22 85 462 196 601
Beta-hexosaminidase OS=Vibrio furnissii OX=29494 GN=exoI PE=1 SV=1
P29416 1.33e-21 99 467 114 485
Beta-hexosaminidase subunit alpha OS=Mus musculus OX=10090 GN=Hexa PE=1 SV=2
Q0V8R6 4.13e-20 99 476 114 496
Beta-hexosaminidase subunit alpha OS=Bos taurus OX=9913 GN=HEXA PE=2 SV=1
Q641X3 9.66e-20 99 467 114 485
Beta-hexosaminidase subunit alpha OS=Rattus norvegicus OX=10116 GN=Hexa 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
0.000895 0.903083 0.095191 0.000289 0.000273 0.000241

TMHMM  Annotations      download full data without filtering help

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