CAZyme Information: MGYG000000162_01327

Basic Information

• Species: Enterococcus_B durans
• Lineage: Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae; Enterococcus_B; Enterococcus_B durans
• CAZyme ID: MGYG000000162_01327
• CAZy Family: GH20
• CAZyme Description: Beta-N-acetylhexosaminidase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
346		39702.92	4.6822

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000162	3083618	Isolate	China	Asia

• Gene Location: Start: 15658; End: 16698 Strand: +

Full Sequence      

MKKILSIDAGRKYFSKEQLETIIEKASQAGFTGIEVILANNGLRFILDDMAINGQVQYYE
SEKVKEELIKGTKKYYDDPNGCYLSQKDMDYLLQSAKERSIELIPVINSPGHMDAIVEGM
KHLGIQAPAFRTSRSTIDLANQEAVDFTRQLVKKYIDYFSGKVGYFNLGCDEYANDVKTE
GGWLGLLDKGDYAKFIDYTNELAAIVKNNKMEPIVFNDGIYYHADERYGQFDPAIIVAYW
TAGWKGYEVCPPEFLVAKGHRLLNTNDSWYWVIGRNTEKDGYYHFEQVLEGIERTEISQV
PAAVEKLPIIGSMFGIWADDPERQFEMQALDQLITRYSSYWNQQFQ

Enzyme Prediction     

EC	3.2.1.52	3.2.1.96

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH20	5	334	1.8e-42	0.9169139465875371

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06564	GH20_DspB_LnbB-like	5.89e-84	1	322	1	300	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	1.35e-29	2	344	12	346	N-acetyl-beta-hexosaminidase [Carbohydrate transport and metabolism].
COG3525	Chb	9.60e-27	1	321	424	720	N-acetyl-beta-hexosaminidase [Carbohydrate transport and metabolism].
cd02742	GH20_hexosaminidase	9.35e-18	7	320	6	279	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.
cd06565	GH20_GcnA-like	2.14e-10	81	240	55	210	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ASV94111.1	5.48e-262	1	346	1	346
QED59370.1	1.14e-254	1	346	1	346
QCJ56761.1	2.69e-130	1	334	1	332
BBM13708.1	2.69e-130	1	334	1	332
BAO07371.1	2.69e-130	1	334	1	332

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
7PUL_A	1.77e-126	1	343	9	348	ChainA, Beta-N-acetylhexosaminidase [Enterococcus faecalis]
4AZ7_A	1.79e-114	2	339	7	359	Differentialinhibition of the tandem GH20 catalytic modules in the pneumococcal exo-beta-D-N-acetylglucosaminidase, StrH [Streptococcus pneumoniae TIGR4]
2YL6_A	1.85e-114	2	339	7	359	Inhibitionof the pneumococcal virulence factor StrH and molecular insights into N-glycan recognition and hydrolysis [Streptococcus pneumoniae TIGR4],4AZ5_A Differential inhibition of the tandem GH20 catalytic modules in the pneumococcal exo-beta-D-N-acetylglucosaminidase, StrH [Streptococcus pneumoniae TIGR4]
4AZ6_A	1.91e-114	2	339	9	361	Differentialinhibition of the tandem GH20 catalytic modules in the pneumococcal exo-beta-D-N-acetylglucosaminidase, StrH [Streptococcus pneumoniae TIGR4]
2YLL_A	3.46e-114	2	339	27	379	Inhibitionof the pneumococcal virulence factor StrH and molecular insights into N-glycan recognition and hydrolysis [Streptococcus pneumoniae TIGR4]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P49610	9.68e-106	2	339	187	539	Beta-N-acetylhexosaminidase OS=Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4) OX=170187 GN=strH PE=1 SV=2

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
1.000051	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000162_01327.