CAZyme Information: MGYG000000467_00465

Basic Information

• Species: CAAGED01 sp900768505
• Lineage: Bacteria; Verrucomicrobiota; Lentisphaeria; Victivallales; Victivallaceae; CAAGED01; CAAGED01 sp900768505
• CAZyme ID: MGYG000000467_00465
• CAZy Family: GH20
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
483	MGYG000000467_6|CGC1	55183.15	6.2325

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000467	2445290	MAG	Fiji	Oceania

• Gene Location: Start: 31230; End: 32681 Strand: +

Full Sequence      

MRIENMIIPRPAEIIEQNGVVCHLGKINWIEGAGVCKSGVKCINDALIAIGANPLPSHLS
KMNLGTRQRISFNVNAENLAPEEYVLNISNESIVIEGGDAAGVFYGAQSLVQMLAVCSEL
GGHDRYLPVCVIKDRPRFKYRGIMIDSARHFQKPEILLKLIDEMAKYKLNVLHWHLVDRQ
SWRLPLACAPELLKNVPRSRAYVFGAYTKEDIQRVVEYAENRYIQVIPEIEMPGHSAAVF
YTHPELACPVSPTPYEDDFWEFCIGNDEVEIFLTKILQECVELFPNSKYIHIGGDEASDA
HWRNCPRCQKKMSSLGFKEPRELEQYFMARMEQVVNNLGRQAISWGIPHGDGENFTGRMV
IQNWLRNDINSYLNGSHQVINSFHVNNYFDYPAGDSEPVVDYQRRNYEFDPAAGVTPEKI
SLVLGGEGCIWSEQIPQWRVLPRAIPRMRALAEILWSHPEHKDFDNFLLRERLLTGSGLY
RYC

Enzyme Prediction     

No EC number prediction in MGYG000000467_00465.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH20	133	458	2.3e-88	0.973293768545994

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06563	GH20_chitobiase-like	1.55e-113	138	470	1	356	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-105	138	457	1	344	Glycosyl hydrolase family 20, catalytic domain. This domain has a TIM barrel fold.
cd06562	GH20_HexA_HexB-like	2.08e-79	138	474	1	345	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	5.30e-72	79	470	203	627	N-acetyl-beta-hexosaminidase [Carbohydrate transport and metabolism].
cd02742	GH20_hexosaminidase	1.56e-70	140	457	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
AFH50886.1	5.07e-83	75	470	89	484
QKJ99561.1	3.93e-82	82	470	106	500
QGA23908.1	2.59e-79	2	475	24	521
QNL37442.1	6.33e-79	80	470	101	510
QCQ33705.1	2.09e-78	81	470	109	520

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
7CBN_A	2.28e-68	79	473	75	496	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	3.35e-67	7	470	31	521	BT0459[Bacteroides thetaiotaomicron],6Q63_B BT0459 [Bacteroides thetaiotaomicron],6Q63_C BT0459 [Bacteroides thetaiotaomicron]
3RCN_A	1.82e-59	79	481	75	505	CrystalStructure of Beta-N-Acetylhexosaminidase from Arthrobacter aurescens [Paenarthrobacter aurescens TC1]
4PYS_A	1.78e-56	79	467	75	473	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]
6EZR_A	3.12e-54	84	470	211	622	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
B2UQG6	1.60e-67	79	473	94	515	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	3.45e-63	7	470	37	517	Beta-hexosaminidase OS=Porphyromonas gingivalis (strain ATCC BAA-308 / W83) OX=242619 GN=nahA PE=3 SV=2
B2UP57	1.54e-51	79	467	55	458	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
P96155	2.09e-48	84	452	210	601	Beta-hexosaminidase OS=Vibrio furnissii OX=29494 GN=exoI PE=1 SV=1
P07686	5.73e-45	82	466	147	524	Beta-hexosaminidase subunit beta OS=Homo sapiens OX=9606 GN=HEXB PE=1 SV=4

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
1.000063	0.000003	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000467_00465.