CAZyme Information: MGYG000001963_00767

Basic Information

• Species: Phocaeicola sp000434735
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Phocaeicola; Phocaeicola sp000434735
• CAZyme ID: MGYG000001963_00767
• CAZy Family: GH20
• CAZyme Description: Beta-hexosaminidase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
541	MGYG000001963_11|CGC2	62039.81	5.9856

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001963	3288738	MAG	Denmark	Europe

• Gene Location: Start: 54495; End: 56120 Strand: +

Full Sequence      

MTSKIIHILLLCCSFFGPMTVVSACSDKQNIESTNNALTSVALIPQPESLVYGSNNIVLP
SVITLTNEIKGVPASLLVSTLEQVCNEVQTVSNDNAFVRVLHNSNWGDDEYSINIGAENI
QIEYSQPQGLLWGIQTLRQIILQCSTDNIGNKTIPMLSLQDKPKKNWRGFHVDVARHAFT
MNYLKKIVDCLSFYKINKLQLHLTDDQGWRIEIKKYPALTSVGGWRQFDEYDKRCIELSN
TDTDYLIDSRFIRNGNEYGGYYTQEELKDFVKYALDRGIDVIPEIDMPGHFSAAIKAFPN
LSCTGGADWGKEFSFPVCAGKTENYAFMKNILDEVLAIFPSEYIHIGADEVETDNWTVCP
YCQKMIKDNNLMNTSGLLNYFVKDISDYLKSKGKKVMVWDDAFYKRKPLDLIYTYWRDWL
PEQPGDITQSGHSMIFMEWGRFYLSGTPSDKALKSLYTFTYEPQFPGIIQSKVTGFQACV
WTEMIPNERKFGEHVFPSLQAFAEVAWGSTRDWDRFVRYLPWHLKWLNSNGIHCRKPDFL
K

Enzyme Prediction     

EC	3.2.1.52	3.2.1.-

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH20	166	508	2.1e-101	0.9525222551928784

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06563	GH20_chitobiase-like	5.91e-151	167	518	3	355	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	3.46e-109	167	507	3	343	Glycosyl hydrolase family 20, catalytic domain. This domain has a TIM barrel fold.
COG3525	Chb	1.32e-81	111	532	208	640	N-acetyl-beta-hexosaminidase [Carbohydrate transport and metabolism].
cd06568	GH20_SpHex_like	1.20e-74	166	516	2	325	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.
cd02742	GH20_hexosaminidase	1.89e-66	167	508	1	303	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
QDM09387.1	3.35e-236	17	540	18	542
QNL38882.1	2.98e-232	17	540	18	542
SCV11006.1	1.20e-231	17	540	18	542
QRQ58194.1	1.20e-231	17	540	18	542
ALJ46646.1	1.20e-231	17	540	18	542

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
7CBN_A	1.57e-78	94	538	63	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]
6Q63_A	8.32e-72	95	539	92	541	BT0459[Bacteroides thetaiotaomicron],6Q63_B BT0459 [Bacteroides thetaiotaomicron],6Q63_C BT0459 [Bacteroides thetaiotaomicron]
6EZR_A	9.73e-71	90	537	189	640	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	1.30e-69	90	537	186	637	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]
4PYS_A	3.84e-65	111	531	80	488	Thecrystal structure of beta-N-acetylhexosaminidase from Bacteroides fragilis NCTC 9343 [Bacteroides fragilis NCTC 9343],4PYS_B The crystal structure of beta-N-acetylhexosaminidase from Bacteroides fragilis NCTC 9343 [Bacteroides fragilis NCTC 9343]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
B2UQG6	1.12e-77	94	538	82	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
P49008	1.26e-69	108	537	110	535	Beta-hexosaminidase OS=Porphyromonas gingivalis (strain ATCC BAA-308 / W83) OX=242619 GN=nahA PE=3 SV=2
P96155	7.19e-59	18	503	118	601	Beta-hexosaminidase OS=Vibrio furnissii OX=29494 GN=exoI PE=1 SV=1
B2UP57	1.01e-51	109	527	58	469	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
Q7WUL4	7.20e-48	107	532	80	475	Beta-N-acetylhexosaminidase OS=Cellulomonas fimi OX=1708 GN=hex20 PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as LIPO

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.000001	0.000195	0.999853	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001963_00767.