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CAZyme Information: MGYG000001888_00671

You are here: Home > Sequence: MGYG000001888_00671

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_A; Christensenellales; Borkfalkiaceae; UMGS775;
CAZyme ID MGYG000001888_00671
CAZy Family GH20
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
320 36815.14 6.3838
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001888 1136142 MAG Denmark Europe
Gene Location Start: 1176;  End: 2138  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.52

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH20 76 269 5.3e-31 0.6350148367952523

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd06565 GH20_GcnA-like 8.39e-83 84 296 2 205
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 1.10e-35 83 269 1 195
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 5.58e-13 85 270 4 205
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.
cd06568 GH20_SpHex_like 6.19e-12 85 257 5 188
A subgroup of the Glycosyl hydrolase family 20 (GH20) catalytic domain found in proteins similar to the N-acetylhexosaminidase from Streptomyces plicatus (SpHex). SpHex catalyzes the hydrolysis of N-acetyl-beta-hexosaminides. An Asp residue within the active site plays a critical role in substrate-assisted catalysis by orienting the 2-acetamido group and stabilizing the transition state. 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. Proteins belonging to this subgroup lack the C-terminal PKD (polycystic kidney disease I)-like domain found in the chitobiases.
cd06563 GH20_chitobiase-like 4.66e-10 85 222 5 177
The chitobiase of Serratia marcescens is a beta-N-1,4-acetylhexosaminidase with a glycosyl hydrolase family 20 (GH20) domain that hydrolyzes the beta-1,4-glycosidic linkages in oligomers derived from chitin. Chitin is degraded by a two step process: i) a chitinase hydrolyzes the chitin to oligosaccharides and disaccharides such as di-N-acetyl-D-glucosamine and chitobiose, ii) chitobiase then further degrades these oligomers into monomers. This GH20 domain family includes an N-acetylglucosamidase (GlcNAcase A) from Pseudoalteromonas piscicida and an N-acetylhexosaminidase (SpHex) from Streptomyces plicatus. SpHex lacks the C-terminal PKD (polycystic kidney disease I)-like domain found in the chitobiases. 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
QCJ40720.1 5.60e-88 1 298 1 303
ABX43920.1 5.91e-84 19 298 20 304
AIQ24479.1 3.25e-83 3 298 5 305
AWV34232.1 6.43e-83 1 298 1 305
AIQ74915.1 1.38e-81 1 298 1 305

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
2EPL_X 4.38e-69 7 298 6 304
N-acetyl-B-D-glucosaminidase(GCNA) from Streptococcus gordonii [Streptococcus gordonii],2EPM_X N-acetyl-B-D-glucoasminidase (GCNA) from Stretococcus gordonii [Streptococcus gordonii],2EPN_A N-acetyl-B-D-glucosaminidase (GCNA) from Streptococcus gordonii [Streptococcus gordonii],2EPN_B N-acetyl-B-D-glucosaminidase (GCNA) from Streptococcus gordonii [Streptococcus gordonii],2EPO_A N-acetyl-B-D-glucosaminidase (GCNA) from Streptococcus gordonii [Streptococcus gordonii],2EPO_B N-acetyl-B-D-glucosaminidase (GCNA) from Streptococcus gordonii [Streptococcus gordonii]
5A6B_D 1.95e-66 22 298 40 325
GH20C,Beta-hexosaminidase from Streptococcus pneumoniae in complex with PUGNAc [Streptococcus pneumoniae TIGR4]
5A69_A 1.48e-65 22 298 40 326
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 1.48e-65 22 298 40 326
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]
5AC4_A 4.03e-65 22 298 40 326
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      help

has no Swissprot hit.

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 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000001888_00671.