CAZyme Information: MGYG000002587_02192

Basic Information

• Species: Parabacteroides sp900760525
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Tannerellaceae; Parabacteroides; Parabacteroides sp900760525
• CAZyme ID: MGYG000002587_02192
• CAZy Family: GH20
• CAZyme Description: Beta-hexosaminidase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
524	MGYG000002587_43|CGC2	59658.33	6.4478

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002587	4423098	MAG	China	Asia

• Gene Location: Start: 20507; End: 22081 Strand: +

Full Sequence      

MRKLIYLSTLLLLFVLPLMAQQPLFPTPAKVQNAKGSFIVGKNLQVQGNGGYADKLAAGL
QAELKEAGMQSSLASGTIRLELTDDCKMVDEAYTLVVESNSILLQASSEAGLFYAKEALL
QLSRFGKGNVRACKIQDQPRYGWRGFMLDESRHFFGKEKVKQYLDIMASLRLNVFHWHLT
DEPGWRIEIKRYPKLTTEGAVGNWHDPKAPATFYTQEEIKEIVAYAADRQIMVVPEFDMP
GHATAVCRSYPEISGGGEGKWQHFTFHPCKEETFEFISNVLDEIVALFPSPYIHIGGDEV
HYGNQSWFTDPEIQQFIKDKNLGNETGLEQYFIRRAADIVASKGKTMIGWDEMIDAGVSP
DKAVIMWWRHDRKHQLVKALENGYRVIMTPRRPLYADFIQYGGHKVGRVWGGYNAIEDIC
RFPEPIIHLTRDYEDQVMGMQFSLWTERVADAKRLDYMTFPRLVAVAESAWTPAKSKECS
LFMQKLPYFLQFLGEKGIYYFNPFNPESTPEPGAPDKEDVLKNG

Enzyme Prediction     

No EC number prediction in MGYG000002587_02192.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH20	136	473	2.7e-111	0.973293768545994

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06563	GH20_chitobiase-like	7.73e-167	141	486	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	3.06e-146	141	473	1	345	Glycosyl hydrolase family 20, catalytic domain. This domain has a TIM barrel fold.
cd06568	GH20_SpHex_like	1.03e-96	141	474	1	317	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.
cd06562	GH20_HexA_HexB-like	7.83e-92	141	489	1	340	Beta-N-acetylhexosaminidases 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. The hexA and hexB genes encode the alpha- and beta-subunits of the two major beta-N-acetylhexosaminidase isoenzymes, N-acetyl-beta-D-hexosaminidase A (HexA) and beta-N-acetylhexosaminidase B (HexB). Both the alpha and the beta catalytic subunits have a TIM-barrel fold and belong to the glycosyl hydrolase family 20 (GH20). The HexA enzyme is a heterodimer containing one alpha and one beta subunit while the HexB enzyme is a homodimer containing two beta-subunits. Hexosaminidase mutations cause an inability to properly hydrolyze certain sphingolipids which accumulate in lysosomes within the brain, resulting in the lipid storage disorders Tay-Sachs and Sandhoff. Mutations in the alpha subunit cause in a deficiency in the HexA enzyme and result in Tay-Sachs, mutations in the beta-subunit cause in a deficiency in both HexA and HexB enzymes and result in Sandhoff disease. In both disorders GM(2) gangliosides accumulate in lysosomes. 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	1.10e-91	24	505	136	647	N-acetyl-beta-hexosaminidase [Carbohydrate transport and metabolism].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QUT50216.1	0.0	1	524	1	524
AUI48789.1	6.71e-255	10	524	22	511
CBW20983.1	1.35e-254	10	524	22	511
QCQ40074.1	1.35e-254	10	524	22	511
ALJ59064.1	1.48e-254	13	524	12	504

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
7CBN_A	1.07e-98	26	505	17	515	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]
6EZR_A	5.45e-83	22	504	140	641	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	7.53e-82	22	504	137	638	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]
6Q63_A	1.36e-78	91	500	106	536	BT0459[Bacteroides thetaiotaomicron],6Q63_B BT0459 [Bacteroides thetaiotaomicron],6Q63_C BT0459 [Bacteroides thetaiotaomicron]
3RCN_A	1.27e-76	78	486	67	498	CrystalStructure of Beta-N-Acetylhexosaminidase from Arthrobacter aurescens [Paenarthrobacter aurescens TC1]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
B2UQG6	7.91e-98	17	505	25	534	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
P49008	2.39e-85	53	503	74	535	Beta-hexosaminidase OS=Porphyromonas gingivalis (strain ATCC BAA-308 / W83) OX=242619 GN=nahA PE=3 SV=2
P96155	3.20e-76	24	469	141	603	Beta-hexosaminidase OS=Vibrio furnissii OX=29494 GN=exoI PE=1 SV=1
Q7WUL4	6.17e-63	74	514	65	490	Beta-N-acetylhexosaminidase OS=Cellulomonas fimi OX=1708 GN=hex20 PE=1 SV=1
P06865	2.82e-55	91	498	114	512	Beta-hexosaminidase subunit alpha OS=Homo sapiens OX=9606 GN=HEXA PE=1 SV=2

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
0.000269	0.999088	0.000181	0.000149	0.000146	0.000139

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002587_02192.