CAZyme Information: MGYG000000298_00359

Basic Information

• Lineage: Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; Streptococcus
• CAZyme ID: MGYG000000298_00359
• CAZy Family: GH20
• CAZyme Description: Beta-N-acetylhexosaminidase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1306	MGYG000000298_9|CGC1	143067.47	4.5807

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000298	1627980	MAG	Sweden	Europe

• Gene Location: Start: 14645; End: 18565 Strand: -

Full Sequence      

MKPENKQRFSIRKYAIGAASVLIGFAFQAQAVAADGVVPATTENQPAVQTTGEVTPPTSE
EKVETAPSTEKATPAAPATNSEAPKVEVAPAPAVANPVTSEEAPAKPAVTEEAKKTESEK
QEEKKEVAKVEAPVVATERATQVNEKLAKKKIVSIDAGRKYFSPDQLKEIIDKAKHYGYT
DLHLLVGNDGLRFMLDDMSLTVGDKTYASDDVKRAVENGTNAYYNDPNGNHLTESQMTDL
ISYAKDKGIGLIPTVNSPGHMDAILNAMKELGIEKPNFNYFGKESARTVDLDNEKAVAFT
KALIDKYAAYFAGKSEIFNIGLDEYANDATDAKGWSVLQAYKWYPEDGFPDKGYDKFIAY
ANDLARIVKSHGLKPMAFNDGIYYNSDTTFGTFDKDIIVSMWTGGWGGYDVASSKLLAEK
GHEILNTNDAWYYVLGRNADGQGWYNLDQGLNGIKSTPITSVPKTEGADVPIIGGMVAAW
ADTPSARYSPSRLFKLMRQFANSNAEYFAADYESADQALKEVPTDLSRYTAESVAAVKEA
EKAIRSLDSNLSRAQQDSIDQAIAKLQEAVSNLTFTPEAQKEEDAKREVEKLEKNKVISI
DAGRKYFTLDQLKRIVDKASELGYSDLHLLLGNDGLRFLLDDMTITANGKTYASDDVKNA
IIEGTKAYYDDPNGTTLSQAEITELIQYAKDRGIGIIPAINSPGHMDAMLVAMEKLGIAN
PQANFDKVSKTTMDLENEEAMNFTKALIGKYMDFFAGKTKIFNYGTDEYANDATNAQGWY
YLKWYGLYGKFADYANGLAAMAKEKGLQPMAFNDGFYYEDKDDVEFDKDVIISYWSKGWW
GYNLASPQYLASKGYKFLNTNGDWYYILGQKPEDGGGFLKKAIENTEKTPFNQLASTKYP
EVDLPTVGSMVAIWADRPSAEYKEEEIFELMTAFADHNKDYFRADYKALREELAQIPENL
EGYSTESLDALKAAKEALNYNLNRNKQAELDTLVANLKAARLGLKPAATHSGSLDESETS
AAVENRPELITRTEEILFETVKKENPNLPAGQEKVVTEGAKGERTIYVSVTTENGKETET
VLEEKVTKEAVNQVVEVGTPVTHVGDEEGVAPVADAKPRVVIEDEEIPFTTITRETDALT
KGETRVVTEGVKGRRSHFYSVSTAADGSEVKTLVTSVVAQEPVTQIIEVGTPVTHVGDEK
GLAPVAEEKPKLEIPNIPAPIAEEKPALEIPNVPAPIAEEKPKLEIPSKPAPATVPAEEN
KPLPQGPAPVAKENKLPETGSQGSEWLIATGLMAALTAYGLSKKKD

Enzyme Prediction     

EC	3.2.1.96

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH20	598	936	1.3e-53	0.9287833827893175
GH20	153	501	1.7e-53	0.9258160237388724

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
COG3525	Chb	0.0	143	930	6	732	N-acetyl-beta-hexosaminidase [Carbohydrate transport and metabolism].
cd06564	GH20_DspB_LnbB-like	8.31e-109	594	941	1	326	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.
cd06564	GH20_DspB_LnbB-like	1.15e-108	149	507	1	326	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	2.24e-40	588	972	6	380	N-acetyl-beta-hexosaminidase [Carbohydrate transport and metabolism].
cd02742	GH20_hexosaminidase	1.17e-29	598	867	4	240	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     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QLF54782.1	0.0	1	1306	1	1310
AMD96210.1	0.0	1	1306	1	1291
VFH75263.1	0.0	1	1306	1	1287
VFI18189.1	0.0	1	1306	1	1287
VFI14896.1	0.0	1	1306	1	1293

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3RPM_A	3.34e-292	139	605	1	467	Crystalstructure of the first GH20 domain of a novel Beta-N-acetyl-hexosaminidase StrH from Streptococcus pneumoniae R6 [Streptococcus pneumoniae R6],3RPM_B Crystal structure of the first GH20 domain of a novel Beta-N-acetyl-hexosaminidase StrH from Streptococcus pneumoniae R6 [Streptococcus pneumoniae R6]
2YL5_A	1.01e-283	589	1027	4	442	Inhibitionof the pneumococcal virulence factor StrH and molecular insights into N-glycan recognition and hydrolysis [Streptococcus pneumoniae TIGR4],2YL5_B Inhibition of the pneumococcal virulence factor StrH and molecular insights into N-glycan recognition and hydrolysis [Streptococcus pneumoniae TIGR4],2YL5_C Inhibition of the pneumococcal virulence factor StrH and molecular insights into N-glycan recognition and hydrolysis [Streptococcus pneumoniae TIGR4],2YL5_D Inhibition of the pneumococcal virulence factor StrH and molecular insights into N-glycan recognition and hydrolysis [Streptococcus pneumoniae TIGR4],4AZC_B Differential inhibition of the tandem GH20 catalytic modules in the pneumococcal exo-beta-D-N-acetylglucosaminidase, StrH [Streptococcus pneumoniae TIGR4],4AZC_C Differential inhibition of the tandem GH20 catalytic modules in the pneumococcal exo-beta-D-N-acetylglucosaminidase, StrH [Streptococcus pneumoniae TIGR4],4AZC_D Differential inhibition of the tandem GH20 catalytic modules in the pneumococcal exo-beta-D-N-acetylglucosaminidase, StrH [Streptococcus pneumoniae TIGR4]
4AZG_A	1.05e-283	589	1027	5	443	Differentialinhibition of the tandem GH20 catalytic modules in the pneumococcal exo-beta-D-N-acetylglucosaminidase, StrH [Streptococcus pneumoniae TIGR4],4AZG_B Differential inhibition of the tandem GH20 catalytic modules in the pneumococcal exo-beta-D-N-acetylglucosaminidase, StrH [Streptococcus pneumoniae TIGR4],4AZH_A Differential inhibition of the tandem GH20 catalytic modules in the pneumococcal exo-beta-D-N-acetylglucosaminidase, StrH [Streptococcus pneumoniae TIGR4],4AZH_B Differential inhibition of the tandem GH20 catalytic modules in the pneumococcal exo-beta-D-N-acetylglucosaminidase, StrH [Streptococcus pneumoniae TIGR4],4AZH_C Differential inhibition of the tandem GH20 catalytic modules in the pneumococcal exo-beta-D-N-acetylglucosaminidase, StrH [Streptococcus pneumoniae TIGR4],4AZH_D Differential inhibition of the tandem GH20 catalytic modules in the pneumococcal exo-beta-D-N-acetylglucosaminidase, StrH [Streptococcus pneumoniae TIGR4]
2YL6_A	1.06e-283	144	577	1	434	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]
2YLL_A	1.59e-283	143	577	20	454	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	0.0	1	1306	1	1311	Beta-N-acetylhexosaminidase OS=Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4) OX=170187 GN=strH PE=1 SV=2
B2UPR7	5.36e-08	155	482	239	538	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
B2UQG6	8.07e-06	155	324	157	327	Beta-hexosaminidase Amuc_0868 OS=Akkermansia muciniphila (strain ATCC BAA-835 / DSM 22959 / JCM 33894 / BCRC 81048 / CCUG 64013 / CIP 107961 / Muc) OX=349741 GN=Amuc_0868 PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.000723	0.998398	0.000326	0.000201	0.000175	0.000152

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000298_00359.