CAZyme Information: MGYG000003443_00932

Basic Information

• Species: UBA1067 sp900767325
• Lineage: Bacteria; Verrucomicrobiota; Kiritimatiellae; RFP12; UBA1067; UBA1067; UBA1067 sp900767325
• CAZyme ID: MGYG000003443_00932
• CAZy Family: GH20
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
607	MGYG000003443_85|CGC1	69419.6	8.2787

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003443	1101788	MAG	Fiji	Oceania

• Gene Location: Start: 3572; End: 5395 Strand: -

Full Sequence      

MLKSLLLLAVAAVTAPLGADCLDELMPRPMSVYRGSDHLLKERVSPGAYILTIRNGEAKI
KARDEEGKRYAKATLWQLKRLAEGKKLPDCIIQDWPRFKYRGLLLDCGRNFQELSSLKDI
IDQLARYKYNVFHWHIVDNYGWRLESKKYPQLQRKEAFSRNVGKFYTQAEFKELVAYAKK
RGVTIIPELDMPGHTLAFRKAFDFKTLATEEAKKILGELIDELCSLVPAEDMPIIHLGTD
EAREPGEKVPQTHLDHWAGRVKANGRKLMGWSPGLRLPGQDMKQLWMGAVDPRGDKCPYL
DSQRSYYINHVDAEELLPIAAYQKPCRWGDESEQLGAIACIWHDDAIGDNEDMVRMSSGY
AAIVLLSDAFWRGREKDDADLIARLPFPDDPRFELAVDLERRTLAQRDKVLKDLRHPFTY
VAQTGMRWRMTDETGVEIARDIAHATVYPKHFWFDSGYVKRNEGTVTLETWIVSPREIDC
GAWIGMTGFSRSDGRSRDAPTPKLGQWNKHDATIALNGKPIEPPKWTHPGVGGNPKEQPL
VDEDYWYRPPTKIHLVKGVNHVKMTLPKKGGWKWIGTFVPIEGESDHPHEVEGLRYFSHL
PKKRGEM

Enzyme Prediction     

No EC number prediction in MGYG000003443_00932.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH20	93	351	2e-57	0.9169139465875371

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd02742	GH20_hexosaminidase	9.88e-55	100	356	1	289	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	6.64e-50	98	271	1	224	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	9.57e-49	98	275	1	223	Glycosyl hydrolase family 20, catalytic domain. This domain has a TIM barrel fold.
COG3525	Chb	7.75e-48	47	275	206	490	N-acetyl-beta-hexosaminidase [Carbohydrate transport and metabolism].
cd06568	GH20_SpHex_like	2.35e-40	98	286	1	211	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
AEM69598.1	1.34e-127	48	596	113	684
BBE20173.1	2.51e-124	48	596	80	654
QCX38608.1	1.89e-122	40	596	95	675
AHW60354.1	7.56e-119	48	600	39	618
ASO05495.1	3.46e-118	48	600	107	682

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6EZR_A	9.42e-38	47	271	209	487	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	1.02e-36	47	271	206	484	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]
7DUP_A	1.03e-32	40	241	72	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]
7DVB_A	4.62e-32	40	241	72	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]
4PYS_A	2.84e-31	60	286	91	361	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
P96155	7.96e-38	47	271	208	484	Beta-hexosaminidase OS=Vibrio furnissii OX=29494 GN=exoI PE=1 SV=1
B2UP57	4.49e-30	48	250	59	289	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
B2UQG6	1.88e-29	32	242	80	328	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
Q7WUL4	6.28e-26	17	292	43	351	Beta-N-acetylhexosaminidase OS=Cellulomonas fimi OX=1708 GN=hex20 PE=1 SV=1
P49008	6.21e-25	27	271	93	384	Beta-hexosaminidase OS=Porphyromonas gingivalis (strain ATCC BAA-308 / W83) OX=242619 GN=nahA PE=3 SV=2

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
0.000319	0.999069	0.000182	0.000152	0.000138	0.000131

TMHMM  Annotations     

There is no transmembrane helices in MGYG000003443_00932.