logo
sublogo
You are browsing environment: HUMAN GUT
help

CAZyme Information: MGYG000001461_00146

You are here: Home > Sequence: MGYG000001461_00146

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 Bacteroides neonati
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Bacteroides; Bacteroides neonati
CAZyme ID MGYG000001461_00146
CAZy Family GH20
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
688 MGYG000001461_1|CGC5 79526.49 6.9384
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001461 5024706 Isolate not provided not provided
Gene Location Start: 185465;  End: 187531  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000001461_00146.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH20 144 467 6.7e-40 0.9643916913946587

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd06565 GH20_GcnA-like 1.44e-82 148 466 1 301
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.
COG3525 Chb 1.25e-16 19 329 128 488
N-acetyl-beta-hexosaminidase [Carbohydrate transport and metabolism].
pfam00728 Glyco_hydro_20 7.69e-16 147 330 2 222
Glycosyl hydrolase family 20, catalytic domain. This domain has a TIM barrel fold.
cd02742 GH20_hexosaminidase 4.70e-15 148 330 1 193
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 5.11e-14 24 142 1 123
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
QUT49641.1 0.0 5 683 6 683
ADV43364.1 0.0 17 688 18 688
QQY42843.1 0.0 18 686 19 686
QQY39583.1 0.0 18 686 19 686
ABR38110.1 0.0 18 686 19 686

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
6Q63_A 2.36e-21 90 330 103 391
BT0459[Bacteroides thetaiotaomicron],6Q63_B BT0459 [Bacteroides thetaiotaomicron],6Q63_C BT0459 [Bacteroides thetaiotaomicron]
6YHH_A 2.81e-18 38 333 37 372
X-rayStructure of Flavobacterium johnsoniae chitobiase (FjGH20) [Flavobacterium johnsoniae UW101],6YHH_B X-ray Structure of Flavobacterium johnsoniae chitobiase (FjGH20) [Flavobacterium johnsoniae UW101]
4C7D_A 3.70e-17 26 285 8 302
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]
4C7G_A 8.65e-17 26 285 8 302
Structureand activity of the GH20 beta-N-acetylhexosaminidase from Streptomyces coelicolor A3(2) [Streptomyces coelicolor]
1HP4_A 9.31e-17 89 469 94 478
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
P49008 1.72e-20 75 330 94 387
Beta-hexosaminidase OS=Porphyromonas gingivalis (strain ATCC BAA-308 / W83) OX=242619 GN=nahA PE=3 SV=2
Q7WUL4 1.59e-11 79 328 69 346
Beta-N-acetylhexosaminidase OS=Cellulomonas fimi OX=1708 GN=hex20 PE=1 SV=1
Q3U4H6 3.58e-11 149 443 10 298
Hexosaminidase D OS=Mus musculus OX=10090 GN=Hexd PE=1 SV=1
Q641X3 5.23e-11 90 330 111 375
Beta-hexosaminidase subunit alpha OS=Rattus norvegicus OX=10116 GN=Hexa PE=2 SV=1
A6QNR0 1.04e-09 149 443 2 290
Hexosaminidase D OS=Bos taurus OX=9913 GN=HEXD PE=2 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
0.000334 0.999023 0.000200 0.000151 0.000146 0.000136

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000001461_00146.