CAZyme Information: MGYG000002560_02572

Basic Information

• Species: Phocaeicola sp902388365
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Phocaeicola; Phocaeicola sp902388365
• CAZyme ID: MGYG000002560_02572
• CAZy Family: GH20
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
669	MGYG000002560_15|CGC2	76877.05	6.8452

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002560	5390440	MAG	China	Asia

• Gene Location: Start: 53303; End: 55312 Strand: -

Full Sequence      

MKHKFACFIGMILVCAVTMAQASICPLLPVPRQYRETGKAFAMGKVKLSTPVLKSEWEAF
IVNAGGKIADRASLEVSVEIVPTIDEARINADEAYHLSVSHKGIKVEATTERGVYWALQT
LRQLEKKTGGRSSFAGCEIVDWPAFRIRGFMQDVGRSYISMEELKREIEILSRFKINVFH
WHLTENQAWRLESKIFPMLNDSANITRMPGKYYTLAEARELVDFCKKHQVMLIPEIDMPG
HSAAFIRTFRHDMQSPEGMKILKLLIEEVCETFDVPYLHIGTDEVEFTNPDFVPQMVAFV
RSKGKKVISWNPGWHYQPGEIDMTHLWSYRGKAQPGIPAIDSKFHYLNHFDTFADIVALY
NSRIYNQAEGSDDIAGTILALWHDRLIDNERDIILENGFYPNMLAIAERAWRGGGTEYFD
GNGTMLPAEDSKEFKEFADFEKRMLWHKEHTFQGYPFAYVKQTNVKWNITDAFPNGGDLS
KAFPPEQELKDVYQYEGNRYGVRQAIGAGIYLRHVWGTLVPGFYADPKENHTAYAYTWVY
SPKEQEVGLWAEFQNYSRSEMDLAPLPGKWDYKGSRIWINDKEIMPPVWTATHRVKSNET
PLGNENCVVRPPLPVHLNKGWNKVFLKLPIGAFRMDETRLVKWMFTTVFVTLDGEKAVEG
LIYSPEKQR

Enzyme Prediction     

No EC number prediction in MGYG000002560_02572.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH20	141	412	2.3e-61	0.9673590504451038

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd02742	GH20_hexosaminidase	8.26e-98	147	412	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.
cd06563	GH20_chitobiase-like	1.90e-49	145	444	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	2.96e-44	145	411	1	343	Glycosyl hydrolase family 20, catalytic domain. This domain has a TIM barrel fold.
COG3525	Chb	1.44e-43	93	429	206	631	N-acetyl-beta-hexosaminidase [Carbohydrate transport and metabolism].
cd06568	GH20_SpHex_like	1.32e-38	145	411	1	314	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QQY43256.1	0.0	1	669	1	668
QEW35773.1	0.0	1	669	1	668
ABR41744.1	0.0	1	669	1	668
QQY39977.1	0.0	1	669	1	668
VTZ55339.1	0.0	1	669	1	668

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4PYS_A	8.49e-36	93	468	78	506	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]
7DUP_A	8.92e-36	93	284	79	316	ChainA, Beta-N-acetylhexosaminidase [Bacteroides thetaiotaomicron],7DVA_A Chain A, Beta-N-acetylhexosaminidase [Bacteroides thetaiotaomicron],7DVA_B Chain B, Beta-N-acetylhexosaminidase [Bacteroides thetaiotaomicron]
6EZR_A	2.66e-35	26	285	141	439	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]
7DVB_A	4.03e-35	93	284	79	316	ChainA, Beta-N-acetylhexosaminidase [Bacteroides thetaiotaomicron],7DVB_B Chain B, Beta-N-acetylhexosaminidase [Bacteroides thetaiotaomicron],7DVB_C Chain C, Beta-N-acetylhexosaminidase [Bacteroides thetaiotaomicron],7DVB_D Chain D, Beta-N-acetylhexosaminidase [Bacteroides thetaiotaomicron]
6EZT_A	2.74e-34	26	285	138	436	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P49008	4.70e-35	27	411	37	503	Beta-hexosaminidase OS=Porphyromonas gingivalis (strain ATCC BAA-308 / W83) OX=242619 GN=nahA PE=3 SV=2
P96155	1.26e-31	70	304	191	455	Beta-hexosaminidase OS=Vibrio furnissii OX=29494 GN=exoI PE=1 SV=1
Q7WUL4	2.59e-26	92	411	81	448	Beta-N-acetylhexosaminidase OS=Cellulomonas fimi OX=1708 GN=hex20 PE=1 SV=1
Q619W7	1.72e-25	91	411	111	499	Beta-hexosaminidase A OS=Caenorhabditis briggsae OX=6238 GN=hex-1 PE=3 SV=2
E9DFH0	9.16e-25	60	286	87	343	Beta-hexosaminidase 1 OS=Coccidioides posadasii (strain RMSCC 757 / Silveira) OX=443226 GN=HEX1 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
0.000399	0.997935	0.001110	0.000186	0.000171	0.000169

TMHMM  Annotations     

start	end
5	24