CAZyme Information: MGYG000003637_00347

Basic Information

• Species: W0P29-029 sp004558035
• Lineage: Bacteria; Verrucomicrobiota; Verrucomicrobiae; Opitutales; UBA953; W0P29-029; W0P29-029 sp004558035
• CAZyme ID: MGYG000003637_00347
• CAZy Family: GH20
• CAZyme Description: Beta-hexosaminidase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
542		61025.47	9.1572

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003637	1987494	MAG	Fiji	Oceania

• Gene Location: Start: 539; End: 2167 Strand: +

Full Sequence      

MRMRKLFFVCSAFVVSCFAAFAAGVPAESLPLVPAPKEIRSTGPGTFVVPSSATVAAPKP
LAGEAALLKSVLKKRLSVSASVSGATGSPATFTLAISTKIKNPEGYELKISKNGVTITGK
TAAGVYYGVRTLEQLFVAEKKNLPELRVVDEPRFAYRGLMLDPARNFIPLADVKRFVETM
AAFKFNTLHFHISEDQGWRVEIKNPKYKRLMTVGAQKNRPEGTRGYYTQKEITELVKFAE
RHHVEVVPEIDMPGHSMGAICAFPELTCEYVRRVNADPELLRQNPKMKLEIWSKAGVSEA
LLCAGKDSTYAFYDDVLAELCGLFPSKKFHIGGDEAPAKCWSQCADCRARMKKEKLENTQ
ELMAFFFQRNFDALAKAGKTALYWYELDVPRYPKNAIMYSWRMGRTREAIDRALREGYKV
ICCPGEYAYFDYPQIKGDSNHGWMPLTTLKRAYEFDPGYGRPKKEQESILGCEGTLWGEH
LPTLEKIYYQAFPRALALVEAGWTPMERRSWESFKERAAPIVRDLRANGVAARWPEEEFG
KE

Enzyme Prediction     

No EC number prediction in MGYG000003637_00347.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH20	149	505	8.3e-104	0.973293768545994

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06563	GH20_chitobiase-like	3.00e-150	154	518	1	357	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.
pfam00728	Glyco_hydro_20	3.51e-129	154	505	1	345	Glycosyl hydrolase family 20, catalytic domain. This domain has a TIM barrel fold.
cd06568	GH20_SpHex_like	8.60e-95	154	517	1	328	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.
COG3525	Chb	1.37e-90	24	533	128	643	N-acetyl-beta-hexosaminidase [Carbohydrate transport and metabolism].
cd02742	GH20_hexosaminidase	7.84e-75	156	503	1	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CDN32424.1	3.76e-145	91	537	70	503
QDH78557.1	4.93e-141	100	540	92	526
QGS17260.1	1.78e-134	99	537	47	477
ATA82469.1	1.42e-133	99	537	47	477
ASF43782.1	2.31e-132	100	537	48	477

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6JE8_A	3.93e-111	104	519	37	442	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]
6Q63_A	3.01e-90	32	529	31	533	BT0459[Bacteroides thetaiotaomicron],6Q63_B BT0459 [Bacteroides thetaiotaomicron],6Q63_C BT0459 [Bacteroides thetaiotaomicron]
7CBN_A	7.61e-85	104	536	78	514	Crystalstructure of beta-N-acetylhexosaminidase Am0868 from Akkermansia muciniphila [Akkermansia muciniphila ATCC BAA-835],7CBO_A Crystal structure of beta-N-acetylhexosaminidase Am0868 from Akkermansia muciniphila in complex with GlcNAc [Akkermansia muciniphila ATCC BAA-835]
4C7D_A	1.35e-79	104	530	80	483	Structureand activity of the GH20 beta-N-acetylhexosaminidase from Streptomyces coelicolor A3(2) [Streptomyces coelicolor],4C7D_B Structure and activity of the GH20 beta-N-acetylhexosaminidase from Streptomyces coelicolor A3(2) [Streptomyces coelicolor],4C7F_A Structure and activity of the GH20 beta-N-acetylhexosaminidase from Streptomyces coelicolor A3(2) [Streptomyces coelicolor],4C7F_B Structure and activity of the GH20 beta-N-acetylhexosaminidase from Streptomyces coelicolor A3(2) [Streptomyces coelicolor]
4C7G_A	3.74e-79	104	530	80	483	Structureand activity of the GH20 beta-N-acetylhexosaminidase from Streptomyces coelicolor A3(2) [Streptomyces coelicolor]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
B2UP57	4.47e-110	104	519	58	463	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
P49008	1.36e-87	104	530	111	530	Beta-hexosaminidase OS=Porphyromonas gingivalis (strain ATCC BAA-308 / W83) OX=242619 GN=nahA PE=3 SV=2
B2UQG6	5.53e-84	104	536	97	533	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
P96155	3.82e-63	106	502	210	604	Beta-hexosaminidase OS=Vibrio furnissii OX=29494 GN=exoI PE=1 SV=1
Q7WUL4	2.88e-50	87	519	64	464	Beta-N-acetylhexosaminidase OS=Cellulomonas fimi OX=1708 GN=hex20 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
0.000774	0.965331	0.033171	0.000266	0.000236	0.000214

TMHMM  Annotations     

start	end
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