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CAZyme Information: MGYG000001526_00548

You are here: Home > Sequence: MGYG000001526_00548

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 Paenibacillus_A senegalimassiliensis
Lineage Bacteria; Firmicutes; Bacilli; Paenibacillales; Paenibacillaceae; Paenibacillus_A; Paenibacillus_A senegalimassiliensis
CAZyme ID MGYG000001526_00548
CAZy Family GH20
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
622 71893.48 4.743
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001526 5059338 Isolate not provided not provided
Gene Location Start: 80100;  End: 81968  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000001526_00548.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH20 153 463 1.3e-36 0.9554896142433235

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd06565 GH20_GcnA-like 3.64e-60 171 461 19 300
Glycosyl hydrolase family 20 (GH20) catalytic domain of N-acetyl-beta-D-glucosaminidase (GcnA, also known as BhsA) and related proteins. GcnA is an exoglucosidase which cleaves N-acetyl-beta-D-galactosamine (NAG) and N-acetyl-beta-D-galactosamine residues from 4-methylumbelliferylated (4MU) substrates, as well as cleaving NAG from chito-oligosaccharides (i.e. NAG polymers). In contrast, sulfated forms of the substrate are unable to be cleaved and act instead as mild competitive inhibitors. Additionally, the enzyme is known to be poisoned by several first-row transition metals as well as by mercury. GcnA forms a homodimer with subunits comprised of three domains, an N-terminal zincin-like domain, this central catalytic GH20 domain, and a C-terminal alpha helical domain. 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 1.44e-20 154 378 1 226
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.
pfam00728 Glyco_hydro_20 1.96e-14 162 362 12 240
Glycosyl hydrolase family 20, catalytic domain. This domain has a TIM barrel fold.
COG3525 Chb 2.78e-14 94 370 197 518
N-acetyl-beta-hexosaminidase [Carbohydrate transport and metabolism].
pfam02838 Glyco_hydro_20b 7.18e-11 88 148 63 123
Glycosyl hydrolase family 20, domain 2. This domain has a zincin-like fold.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
AIQ58793.1 7.33e-199 15 611 15 606
QUL55868.1 4.89e-198 5 617 5 624
QUL52138.1 1.02e-196 15 611 15 608
AIQ75797.1 1.57e-195 1 615 1 601
AWV35100.1 3.59e-194 102 613 89 599

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
7BWG_A 1.88e-11 101 339 85 352
AGlycoside Hydrolase Family 20 beta-N-Acetylglucosaminidase [Microbacterium sp. HJ5],7BWG_B A Glycoside Hydrolase Family 20 beta-N-Acetylglucosaminidase [Microbacterium sp. HJ5]
4C7D_A 1.62e-10 103 343 80 338
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]
6Q63_A 2.96e-10 103 370 106 414
BT0459[Bacteroides thetaiotaomicron],6Q63_B BT0459 [Bacteroides thetaiotaomicron],6Q63_C BT0459 [Bacteroides thetaiotaomicron]
4C7G_A 3.75e-10 103 343 80 338
Structureand activity of the GH20 beta-N-acetylhexosaminidase from Streptomyces coelicolor A3(2) [Streptomyces coelicolor]
1HP4_A 1.57e-09 103 343 98 356
ChainA, Beta-n-acetylhexosaminidase [Streptomyces plicatus],1HP5_A Chain A, Beta-n-acetylhexosaminidase [Streptomyces plicatus],1JAK_A Chain A, Beta-N-acetylhexosaminidase [Streptomyces plicatus],1M01_A Chain A, Beta-N-acetylhexosaminidase [Streptomyces plicatus],5FCZ_A Chain A, B-N-acetylhexosaminidase [Streptomyces plicatus],5FD0_A Chain A, B-N-acetylhexosaminidase [Streptomyces plicatus]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
Q3U4H6 4.99e-32 154 433 9 298
Hexosaminidase D OS=Mus musculus OX=10090 GN=Hexd PE=1 SV=1
A6QNR0 5.34e-31 154 433 1 290
Hexosaminidase D OS=Bos taurus OX=9913 GN=HEXD PE=2 SV=2
Q8WVB3 5.47e-28 154 433 9 298
Hexosaminidase D OS=Homo sapiens OX=9606 GN=HEXD PE=1 SV=3

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI LIPO_Sec_SPII TAT_Tat_SPI TATLIP_Sec_SPII PILIN_Sec_SPIII
1.000020 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000001526_00548.