logo
sublogo
You are browsing environment: HUMAN GUT
help

CAZyme Information: MGYG000004499_00958

You are here: Home > Sequence: MGYG000004499_00958

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 Victivallis sp900551245
Lineage Bacteria; Verrucomicrobiota; Lentisphaeria; Victivallales; Victivallaceae; Victivallis; Victivallis sp900551245
CAZyme ID MGYG000004499_00958
CAZy Family GH20
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
601 MGYG000004499_7|CGC2 67628.13 6.8408
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000004499 4071424 MAG Israel Asia
Gene Location Start: 41394;  End: 43199  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000004499_00958.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH20 128 380 2.6e-40 0.744807121661721

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd06565 GH20_GcnA-like 3.75e-99 131 435 2 301
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 4.20e-20 131 434 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 9.85e-17 25 346 156 510
N-acetyl-beta-hexosaminidase [Carbohydrate transport and metabolism].
pfam02838 Glyco_hydro_20b 4.80e-14 3 124 4 123
Glycosyl hydrolase family 20, domain 2. This domain has a zincin-like fold.
cd06564 GH20_DspB_LnbB-like 5.97e-14 130 326 2 203
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.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
AVM44585.1 0.0 1 599 1 599
ABU56649.1 1.80e-131 3 597 6 607
ABQ91971.1 1.01e-130 3 597 6 607
AJC73967.1 1.29e-130 30 599 12 601
QXD32698.1 7.85e-127 27 599 11 593

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
5A6B_D 1.72e-12 85 414 55 399
GH20C,Beta-hexosaminidase from Streptococcus pneumoniae in complex with PUGNAc [Streptococcus pneumoniae TIGR4]
5A69_A 2.27e-12 85 414 55 400
GH20C,Beta-hexosaminidase from Streptococcus pneumoniae in complex with Gal-PUGNAc [Streptococcus pneumoniae TIGR4],5A6A_A GH20C, Beta-hexosaminidase from Streptococcus pneumoniae in complex with NGT [Streptococcus pneumoniae TIGR4],5A6A_B GH20C, Beta-hexosaminidase from Streptococcus pneumoniae in complex with NGT [Streptococcus pneumoniae TIGR4],5A6J_A GH20C, Beta-hexosaminidase from Streptococcus pneumoniae [Streptococcus pneumoniae TIGR4],5A6J_B GH20C, Beta-hexosaminidase from Streptococcus pneumoniae [Streptococcus pneumoniae TIGR4],5A6J_C GH20C, Beta-hexosaminidase from Streptococcus pneumoniae [Streptococcus pneumoniae TIGR4],5A6J_D GH20C, Beta-hexosaminidase from Streptococcus pneumoniae [Streptococcus pneumoniae TIGR4],5A6K_A GH20C, Beta-hexosaminidase from Streptococcus pneumoniae in complex with Gal-NGT [Streptococcus pneumoniae TIGR4],5A6K_B GH20C, Beta-hexosaminidase from Streptococcus pneumoniae in complex with Gal-NGT [Streptococcus pneumoniae TIGR4],5AC5_A GH20C, Beta-hexosaminidase from Streptococcus pneumoniae in complex with GlcNAc [Streptococcus pneumoniae TIGR4],5AC5_B GH20C, Beta-hexosaminidase from Streptococcus pneumoniae in complex with GlcNAc [Streptococcus pneumoniae TIGR4]
5A6B_A 2.27e-12 85 414 55 400
GH20C,Beta-hexosaminidase from Streptococcus pneumoniae in complex with PUGNAc [Streptococcus pneumoniae TIGR4],5A6B_B GH20C, Beta-hexosaminidase from Streptococcus pneumoniae in complex with PUGNAc [Streptococcus pneumoniae TIGR4],5A6B_C GH20C, Beta-hexosaminidase from Streptococcus pneumoniae in complex with PUGNAc [Streptococcus pneumoniae TIGR4]
6JE8_A 4.97e-12 66 330 24 317
crystalstructure of a beta-N-acetylhexosaminidase [Akkermansia muciniphila ATCC BAA-835],6JEA_A crystal structure of a beta-N-acetylhexosaminidase [Akkermansia muciniphila ATCC BAA-835],6JEB_A crystal structure of a beta-N-acetylhexosaminidase [Akkermansia muciniphila ATCC BAA-835]
5AC4_A 5.22e-12 85 414 55 400
GH20C,Beta-hexosaminidase from Streptococcus pneumoniae in complex with GalNAc [Streptococcus pneumoniae TIGR4],5AC4_B GH20C, Beta-hexosaminidase from Streptococcus pneumoniae in complex with GalNAc [Streptococcus pneumoniae TIGR4]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
B2UP57 2.90e-11 66 330 45 338
Beta-hexosaminidase Amuc_2018 OS=Akkermansia muciniphila (strain ATCC BAA-835 / DSM 22959 / JCM 33894 / BCRC 81048 / CCUG 64013 / CIP 107961 / Muc) OX=349741 GN=Amuc_2018 PE=1 SV=1
Q8WVB3 1.91e-09 143 366 21 247
Hexosaminidase D OS=Homo sapiens OX=9606 GN=HEXD PE=1 SV=3
Q3U4H6 4.42e-09 143 350 21 228
Hexosaminidase D OS=Mus musculus OX=10090 GN=Hexd PE=1 SV=1
A6QNR0 8.45e-09 143 350 13 220
Hexosaminidase D OS=Bos taurus OX=9913 GN=HEXD PE=2 SV=2
Q86M34 1.07e-07 79 279 133 347
Beta-hexosaminidase subunit beta OS=Entamoeba histolytica OX=5759 GN=HEXB PE=1 SV=1

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
1.000064 0.000001 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000004499_00958.