CAZyme Information: MGYG000000575_02005

Basic Information

• Species: UBA11452 sp003526375
• Lineage: Bacteria; Verrucomicrobiota; Lentisphaeria; Victivallales; UBA1829; UBA11452; UBA11452 sp003526375
• CAZyme ID: MGYG000000575_02005
• CAZy Family: GH20
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
496		57343.09	6.9773

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000575	4988607	MAG	Madagascar	Africa

• Gene Location: Start: 9823; End: 11313 Strand: -

Full Sequence      

MDSHEIKILTDRLIPVPKEIKFRDGREYPIAGKCKVAIHAAETGEISEKAEKLFKDYWNA
EAEITLKQDASAKKLGTDAYKIKVAEKQLSITVKGMAGLLNAFKTLRQLAEVQRGTEKVT
GYFLVQCEINDAPAMEFRGIHLCIFPETPLWDIEKQIRLAAYHKFNYAVIETWGVFPFDS
HPEFCWADRKISKTELKKLILLGRELGITLIPQFNLLGHAAAARSMTGKHAVLDYNPSLQ
PLFEPEGWTWCLSNPEVRRIQTDLVMEMYEFYDCPPFFHIGCDEADNIGTCRDCRKHVLK
DLVRDHIVYYHDLFKKHGARIIMWHDMLLQRGDERWKGYIVCGLPEHKLDRLYRELPKDI
VIADWQYGYKAKEDDPEPTWPTTKFFKKEKFDVLVCPWINEQGTKSLGEFAGKEKLMGML
ETTWHIYHGVHYPYVHATAAYAAWNPAVNPMTSLATRLSVAMHMRQIGWDMDVVDYEKTG
WNQYQVDPGHHPHPVS

Enzyme Prediction     

No EC number prediction in MGYG000000575_02005.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH20	149	397	1.9e-24	0.6735905044510386

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06565	GH20_GcnA-like	5.27e-26	155	397	21	237	Glycosyl hydrolase family 20 (GH20) catalytic domain of N-acetyl-beta-D-glucosaminidase (GcnA, also known as BhsA) and related proteins. GcnA is an exoglucosidase which cleaves N-acetyl-beta-D-galactosamine (NAG) and N-acetyl-beta-D-galactosamine residues from 4-methylumbelliferylated (4MU) substrates, as well as cleaving NAG from chito-oligosaccharides (i.e. NAG polymers). In contrast, sulfated forms of the substrate are unable to be cleaved and act instead as mild competitive inhibitors. Additionally, the enzyme is known to be poisoned by several first-row transition metals as well as by mercury. GcnA forms a homodimer with subunits comprised of three domains, an N-terminal zincin-like domain, this central catalytic GH20 domain, and a C-terminal alpha helical domain. 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.
cd06564	GH20_DspB_LnbB-like	1.57e-11	188	373	76	230	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.
cd02742	GH20_hexosaminidase	1.92e-10	192	328	70	194	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.
pfam00728	Glyco_hydro_20	2.30e-10	136	329	2	224	Glycosyl hydrolase family 20, catalytic domain. This domain has a TIM barrel fold.
pfam02838	Glyco_hydro_20b	2.96e-08	12	117	3	115	Glycosyl hydrolase family 20, domain 2. This domain has a zincin-like fold.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
BBD46391.1	1.45e-144	8	492	55	529
ASV74378.1	2.36e-58	121	424	235	534
QDT72359.1	1.12e-23	153	424	54	331
AKA36241.1	3.40e-21	142	424	31	325
QUR50380.1	4.85e-21	117	402	2	299

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
7CBN_A	1.95e-15	1	327	1	360	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]
4PYS_A	1.61e-12	3	425	1	463	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	1.89e-11	75	381	206	542	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]
7DUP_A	8.76e-11	13	328	6	373	ChainA, Beta-N-acetylhexosaminidase [Bacteroides thetaiotaomicron],7DVA_A Chain A, Beta-N-acetylhexosaminidase [Bacteroides thetaiotaomicron],7DVA_B Chain B, Beta-N-acetylhexosaminidase [Bacteroides thetaiotaomicron]
6EZT_A	1.76e-10	75	381	203	539	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
B2UQG6	1.40e-13	14	327	33	379	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
Q9HGI3	3.73e-09	83	368	136	425	Beta-hexosaminidase OS=Emericella nidulans OX=162425 GN=nagA PE=1 SV=1
P96155	8.68e-09	10	381	138	539	Beta-hexosaminidase OS=Vibrio furnissii OX=29494 GN=exoI PE=1 SV=1
D4AUH6	1.99e-08	76	348	155	434	Beta-hexosaminidase ARB_07893 OS=Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) OX=663331 GN=ARB_07893 PE=1 SV=1
B2UP57	3.75e-07	64	295	44	295	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

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 MGYG000000575_02005.