CAZyme Information: MGYG000000138_00853

Basic Information

• Species: Parabacteroides johnsonii
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Tannerellaceae; Parabacteroides; Parabacteroides johnsonii
• CAZyme ID: MGYG000000138_00853
• CAZy Family: GH20
• CAZyme Description: Beta-hexosaminidase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
346		39812.71	6.5834

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000138	4917599	Isolate	United Kingdom	Europe

• Gene Location: Start: 124388; End: 125428 Strand: -

Full Sequence      

MPDFIGKDRASRNRRSTPFRLPRLTEKGEFYTQEELKDLVHYAAERNVQIIPELDIPGHT
VAVLDAYPELGCSHTDTIPKIVGETVNLMLCANNDKVYSLYKDILTEVASIFPAPYIHLG
GDEAIIETNWGKCEHSQSLMKQLSYTKPTELMNYFFGKILPVVRENGKKPMLWCELDNIR
IPAHEYLFDYPKDAVLITWRYGLTPLCMELTARHGNTLIMAPGKYTYLDYPQYKNDFPEF
NNWGMPVTTLETTYQFDPGYGLPASQQAHIAGVNGILWAEAMPDINRVTYMTYPRGLALA
EAGWTQMEHRDWESFKKRICPNLSELMKRGVSVRAPFEIVRYPQKR

Enzyme Prediction     

No EC number prediction in MGYG000000138_00853.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH20	20	306	2.2e-71	0.8100890207715133

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06563	GH20_chitobiase-like	1.03e-113	14	319	62	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	1.64e-99	20	306	51	345	Glycosyl hydrolase family 20, catalytic domain. This domain has a TIM barrel fold.
cd06568	GH20_SpHex_like	6.52e-72	26	319	67	329	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	1.03e-45	19	330	50	348	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	3.66e-45	28	336	340	645	N-acetyl-beta-hexosaminidase [Carbohydrate transport and metabolism].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QCQ50973.1	2.45e-180	22	341	204	523
QKH83770.1	2.45e-180	22	341	204	523
QLK83321.1	2.45e-180	22	341	204	523
QRM71007.1	2.45e-180	22	341	204	523
QCQ55023.1	2.45e-180	22	341	204	523

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6JE8_A	5.21e-64	31	329	165	451	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]
6EZR_A	3.78e-48	28	338	342	642	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]
7CBN_A	1.13e-47	31	336	213	513	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]
6EZT_A	4.88e-47	28	338	339	639	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	2.56e-43	25	319	235	522	BT0459[Bacteroides thetaiotaomicron],6Q63_B BT0459 [Bacteroides thetaiotaomicron],6Q63_C BT0459 [Bacteroides thetaiotaomicron]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
B2UP57	4.95e-63	31	329	186	472	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
B2UQG6	7.34e-47	31	336	232	532	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	5.55e-43	22	336	222	535	Beta-hexosaminidase OS=Porphyromonas gingivalis (strain ATCC BAA-308 / W83) OX=242619 GN=nahA PE=3 SV=2
P96155	4.47e-35	24	303	334	604	Beta-hexosaminidase OS=Vibrio furnissii OX=29494 GN=exoI PE=1 SV=1
Q7WUL4	4.91e-29	28	319	203	463	Beta-N-acetylhexosaminidase OS=Cellulomonas fimi OX=1708 GN=hex20 PE=1 SV=1

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
1.000061	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000138_00853.