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CAZyme Information: MGYG000003869_00206

You are here: Home > Sequence: MGYG000003869_00206

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
Lineage Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Oscillospiraceae; Flavonifractor;
CAZyme ID MGYG000003869_00206
CAZy Family GH20
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
667 MGYG000003869_4|CGC1 75721.15 4.6469
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000003869 2306830 MAG United States North America
Gene Location Start: 22618;  End: 24621  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000003869_00206.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH20 125 353 3.1e-31 0.712166172106825

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd06565 GH20_GcnA-like 1.87e-68 126 418 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.
pfam02838 Glyco_hydro_20b 5.29e-17 5 120 4 123
Glycosyl hydrolase family 20, domain 2. This domain has a zincin-like fold.
COG3525 Chb 6.67e-11 71 265 204 436
N-acetyl-beta-hexosaminidase [Carbohydrate transport and metabolism].
cd06564 GH20_DspB_LnbB-like 1.08e-10 125 335 1 230
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.
cd02742 GH20_hexosaminidase 3.58e-10 126 332 1 212
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.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
CRY94532.1 6.70e-266 42 667 6 629
ACM06734.1 1.12e-107 124 664 2 522
QPC84066.1 1.34e-70 73 454 79 477
APT74174.1 1.78e-69 64 474 66 485
ABR31079.1 3.84e-69 64 474 103 522

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
7BWG_A 9.55e-09 64 135 78 150
AGlycoside Hydrolase Family 20 beta-N-Acetylglucosaminidase [Microbacterium sp. HJ5],7BWG_B A Glycoside Hydrolase Family 20 beta-N-Acetylglucosaminidase [Microbacterium sp. HJ5]
2GK1_I 1.85e-08 65 343 18 318
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 2.11e-08 65 343 84 384
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]
6EZR_A 5.70e-08 71 302 207 472
Crystalstructure of GH20 Exo beta-N-Acetylglucosaminidase from Vibrio harveyi [Vibrio harveyi],6EZR_B Crystal structure of GH20 Exo beta-N-Acetylglucosaminidase from Vibrio harveyi [Vibrio harveyi],6EZS_A Crystal structure of GH20 Exo beta-N-Acetylglucosaminidase from Vibrio harveyi in complex with N-acetylglucosamine [Vibrio harveyi],6EZS_B Crystal structure of GH20 Exo beta-N-Acetylglucosaminidase from Vibrio harveyi in complex with N-acetylglucosamine [Vibrio harveyi],6K35_A Crystal structure of GH20 exo beta-N-acetylglucosaminidase from Vibrio harveyi in complex with NAG-thiazoline [Vibrio harveyi],6K35_B Crystal structure of GH20 exo beta-N-acetylglucosaminidase from Vibrio harveyi in complex with NAG-thiazoline [Vibrio harveyi]
6EZT_A 5.15e-07 71 302 204 469
Crystalstructure of GH20 Exo beta-N-Acetylglucosaminidase D437A inactive mutant from Vibrio harveyi [Vibrio harveyi],6EZT_B Crystal structure of GH20 Exo beta-N-Acetylglucosaminidase D437A inactive mutant from Vibrio harveyi [Vibrio harveyi]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
P43077 7.56e-12 19 373 55 435
Beta-hexosaminidase OS=Candida albicans OX=5476 GN=HEX1 PE=1 SV=1
P06865 1.20e-07 65 343 106 406
Beta-hexosaminidase subunit alpha OS=Homo sapiens OX=9606 GN=HEXA PE=1 SV=2
Q5RC84 1.58e-07 65 343 106 406
Beta-hexosaminidase subunit alpha OS=Pongo abelii OX=9601 GN=HEXA PE=3 SV=1
Q86M34 2.62e-06 72 175 132 241
Beta-hexosaminidase subunit beta OS=Entamoeba histolytica OX=5759 GN=HEXB PE=1 SV=1
Q04786 3.13e-06 46 136 227 327
Beta-hexosaminidase OS=Vibrio vulnificus OX=672 GN=hex PE=3 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
1.000024 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000003869_00206.