CAZyme Information: MGYG000003480_01563

Basic Information

• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Prevotella
• CAZyme ID: MGYG000003480_01563
• CAZy Family: GH20
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
469		54347.3	6.7235

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003480	2592239	MAG	Fiji	Oceania

• Gene Location: Start: 3500; End: 4909 Strand: -

Full Sequence      

MESKLYPQLNAAKNMERDKGKFYTLKQAAELADFCRAHNMTLIPEIDMPGHSAAFERTFG
FGMQTEEGKRIMKDIISEVCDAIDVPWLHIGTDEVQFTDPTFVPEMVAYVRSKGKKVISW
NPGWKYKKGEIDMTQLWSYRGKAQPGIPAIDCRYHYANHFDNYADLVALFNSRIYNQPMG
SDDLAGCIVAFWNDRNIDNTRQLLDENFFYPYMLTLAERAWRGGGNCYFDGKGTVLWDDE
PEQKKEFAEFENRMLWHKTHTLSSEPFSYERQSDVVWSITDAFPNDGDLARSFPPELYLH
GDLSPVDDPTIFSYKRKTYKSRTFTGNGFYLRHVWGTLVPGVYANPEENHTAYATRWIYS
KKARTAKLSLEFQNYSRSESDLPPLQGTWDYKGSRAWINGEEIQPPVWQNTNTERSNELP
LRNENAVSREPIEIHLRQGWNKLVLKLPVGKFSGKETRLVKWMFSATVK

Enzyme Prediction     

No EC number prediction in MGYG000003480_01563.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH20	2	222	8.4e-28	0.8160237388724035

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd02742	GH20_hexosaminidase	1.22e-56	2	222	46	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.
cd06564	GH20_DspB_LnbB-like	2.54e-19	19	223	75	326	Glycosyl hydrolase family 20 (GH20) catalytic domain of dispersin B (DspB), lacto-N-biosidase (LnbB) and related proteins. Dispersin B is a soluble beta-N-acetylglucosamidase found in bacteria that hydrolyzes the beta-1,6-linkages of PGA (poly-beta-(1,6)-N-acetylglucosamine), a major component of the extracellular polysaccharide matrix. Lacto-N-biosidase hydrolyzes lacto-N-biose (LNB) type I oligosaccharides at the nonreducing terminus to produce lacto-N-biose as part of the GNB/LNB (galacto-N-biose/lacto-N-biose I) degradation pathway. The lacto-N-biosidase from Bifidobacterium bifidum has this GH20 domain, a carbohydrate binding module 32, and a bacterial immunoglobulin-like domain 2, as well as a YSIRK signal peptide and a G5 membrane anchor at the N and C termini, respectively. 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.
cd06563	GH20_chitobiase-like	1.93e-16	20	254	80	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.
cd06568	GH20_SpHex_like	9.86e-16	19	151	68	225	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.
pfam00728	Glyco_hydro_20	1.39e-14	1	221	47	343	Glycosyl hydrolase family 20, catalytic domain. This domain has a TIM barrel fold.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QRO26489.1	5.36e-234	1	466	171	627
VDS02388.1	3.36e-221	1	466	192	648
VDS02709.1	1.29e-219	1	465	175	630
AVM59031.1	1.36e-218	1	465	189	645
QQY43256.1	2.30e-216	1	466	190	646

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3GH4_A	5.21e-09	20	250	250	519	Crystalstructure of beta-hexosaminidase from Paenibacillus sp. TS12 [Paenibacillus sp.],3GH5_A Crystal structure of beta-hexosaminidase from Paenibacillus sp. TS12 in complex with GlcNAc [Paenibacillus sp.],3GH7_A Crystal structure of beta-hexosaminidase from Paenibacillus sp. TS12 in complex with GalNAc [Paenibacillus sp.],3SUR_A Crystal structure of beta-hexosaminidase from Paenibacillus sp. TS12 in complex with NAG-thiazoline. [Paenibacillus sp. TS12],3SUS_A Crystal structure of beta-hexosaminidase from Paenibacillus sp. TS12 in complex with Gal-NAG-thiazoline [Paenibacillus sp. TS12],3SUT_A Crystal structure of beta-hexosaminidase from Paenibacillus sp. TS12 in complex with PUGNAc [Paenibacillus sp. TS12],3SUU_A Crystal structure of beta-hexosaminidase from Paenibacillus sp. TS12 in complex with Gal-PUGNAc [Paenibacillus sp. TS12],3SUV_A Crystal structure of beta-hexosaminidase from Paenibacillus sp. TS12 in complex with NHAc-DNJ [Paenibacillus sp. TS12],3SUW_A Crystal structure of beta-hexosaminidase from Paenibacillus sp. TS12 in complex with NHAc-CAS [Paenibacillus sp. TS12]

Swiss-Prot Hits     

has no Swissprot hit.

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
1.000022	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000003480_01563.