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CAZyme Information: MGYG000000170_00681

You are here: Home > Sequence: MGYG000000170_00681

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 Alistipes_A sp900240235
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Rikenellaceae; Alistipes_A; Alistipes_A sp900240235
CAZyme ID MGYG000000170_00681
CAZy Family GH20
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
700 79407.79 6.0087
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000170 3119069 Isolate China Asia
Gene Location Start: 147971;  End: 150073  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000000170_00681.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH20 176 471 5.5e-37 0.9525222551928784

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd06565 GH20_GcnA-like 2.39e-72 183 471 7 301
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 5.19e-26 191 454 14 283
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.
pfam02838 Glyco_hydro_20b 9.30e-23 31 171 1 123
Glycosyl hydrolase family 20, domain 2. This domain has a zincin-like fold.
COG3525 Chb 4.72e-20 28 363 123 490
N-acetyl-beta-hexosaminidase [Carbohydrate transport and metabolism].
pfam00728 Glyco_hydro_20 9.34e-19 177 412 3 265
Glycosyl hydrolase family 20, catalytic domain. This domain has a TIM barrel fold.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QGA23073.1 0.0 1 700 1 700
QNI31352.1 8.48e-125 16 665 22 668
AHG90566.1 9.21e-125 2 693 5 694
SDF25835.1 4.69e-116 31 693 25 694
QNI34778.1 3.58e-114 34 693 26 681

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
6Q63_A 1.47e-18 121 316 104 333
BT0459[Bacteroides thetaiotaomicron],6Q63_B BT0459 [Bacteroides thetaiotaomicron],6Q63_C BT0459 [Bacteroides thetaiotaomicron]
1HP4_A 3.23e-18 108 367 87 358
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]
1M04_A 1.33e-17 108 367 87 358
ChainA, Beta-N-acetylhexosaminidase [Streptomyces plicatus]
4C7D_A 2.16e-17 120 367 77 340
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]
1M03_A 3.11e-17 108 367 87 358
ChainA, Beta-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
P96155 3.67e-19 114 382 199 502
Beta-hexosaminidase OS=Vibrio furnissii OX=29494 GN=exoI PE=1 SV=1
Q3U4H6 8.31e-16 186 468 17 321
Hexosaminidase D OS=Mus musculus OX=10090 GN=Hexd PE=1 SV=1
P49008 2.46e-14 32 362 35 387
Beta-hexosaminidase OS=Porphyromonas gingivalis (strain ATCC BAA-308 / W83) OX=242619 GN=nahA PE=3 SV=2
A6QNR0 3.15e-14 186 474 9 321
Hexosaminidase D OS=Bos taurus OX=9913 GN=HEXD PE=2 SV=2
P20060 2.73e-13 123 380 126 402
Beta-hexosaminidase subunit beta OS=Mus musculus OX=10090 GN=Hexb PE=1 SV=2

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
0.000292 0.999027 0.000183 0.000170 0.000152 0.000138

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000000170_00681.