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CAZyme Information: MGYG000000971_00651

You are here: Home > Sequence: MGYG000000971_00651

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 UMGS1518 sp900552575
Lineage Bacteria; Verrucomicrobiota; Lentisphaeria; Victivallales; Victivallaceae; UMGS1518; UMGS1518 sp900552575
CAZyme ID MGYG000000971_00651
CAZy Family GH20
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
617 68187.43 6.1688
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000971 3501016 MAG Australia Oceania
Gene Location Start: 8910;  End: 10763  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000000971_00651.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH20 126 441 2.7e-40 0.9673590504451038

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd06565 GH20_GcnA-like 3.96e-84 132 441 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.
cd02742 GH20_hexosaminidase 1.11e-18 133 355 2 212
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.
cd06564 GH20_DspB_LnbB-like 7.55e-15 131 355 1 224
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.
COG3525 Chb 1.16e-12 41 334 173 491
N-acetyl-beta-hexosaminidase [Carbohydrate transport and metabolism].
pfam02838 Glyco_hydro_20b 6.06e-12 3 126 4 123
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
AUS98665.1 4.54e-140 80 605 77 612
APC41628.1 2.48e-133 1 485 1 482
QAS62105.1 8.73e-133 67 560 68 556
AYE33954.1 8.73e-133 67 560 68 556
ATD58120.1 3.46e-132 67 599 68 603

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
6JQF_A 2.15e-13 2 377 90 471
Crystallizationanalysis of a beta-N-acetylhexosaminidase (Am2136) from Akkermansia muciniphila [Akkermansia muciniphila ATCC BAA-835]
2GK1_I 1.46e-11 74 352 20 304
X-raycrystal structure of NGT-bound HexA [Homo sapiens],2GK1_J X-ray crystal structure of NGT-bound HexA [Homo sapiens],2GK1_K X-ray crystal structure of NGT-bound HexA [Homo sapiens],2GK1_L X-ray crystal structure of NGT-bound HexA [Homo sapiens]
2GJX_A 1.76e-11 74 352 86 370
Crystallographicstructure of human beta-Hexosaminidase A [Homo sapiens],2GJX_D Crystallographic structure of human beta-Hexosaminidase A [Homo sapiens],2GJX_E Crystallographic structure of human beta-Hexosaminidase A [Homo sapiens],2GJX_H Crystallographic structure of human beta-Hexosaminidase A [Homo sapiens]
4C7D_A 9.16e-11 78 337 78 340
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]
4C7G_A 2.12e-10 78 337 78 340
Structureand 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 3.27e-14 2 377 112 493
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
Q0V8R6 1.89e-11 74 332 108 376
Beta-hexosaminidase subunit alpha OS=Bos taurus OX=9913 GN=HEXA PE=2 SV=1
Q3U4H6 2.99e-11 143 357 22 228
Hexosaminidase D OS=Mus musculus OX=10090 GN=Hexd PE=1 SV=1
P06865 1.01e-10 74 352 108 392
Beta-hexosaminidase subunit alpha OS=Homo sapiens OX=9606 GN=HEXA PE=1 SV=2
P49008 1.02e-10 32 381 63 425
Beta-hexosaminidase OS=Porphyromonas gingivalis (strain ATCC BAA-308 / W83) OX=242619 GN=nahA PE=3 SV=2

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
1.000046 0.000002 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000000971_00651.