CAZyme Information: MGYG000003461_01296

Basic Information

• Species: Prevotella sp900553595
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Prevotella; Prevotella sp900553595
• CAZyme ID: MGYG000003461_01296
• CAZy Family: GH20
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
672	MGYG000003461_388|CGC1	75933.98	6.8428

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003461	2310521	MAG	Fiji	Oceania

• Gene Location: Start: 4037; End: 6055 Strand: +

Full Sequence      

MTTKSVPTLFLTAGLSLLSCGALAQGMLPKPQSFTARKGAFDVNAVAFKVVNEAGDDARN
IYSAACFAKASDNAGRVVRFVRLENASSTEAYRLHITPDTLLVSAASADGFRYAWQTVEQ
LKNKKGAVPACDIDDAPAYRWRSLMIDVSRHFQPISFLKKQIDVMSQYKFNRLHLHLTDA
AGWRMEIKRYPRLTNLAAWRPERTWKEWGKNGSKYAKEGTEGAYGGYYTQEQLRDLVSYA
AERGITIVPEIEMPGHSAEVLTAYPELSCTHEPYKQMDFCPGSVATYDFLENVLKEVMDV
FPSKYIHVGGDEADKASWPSCPLCQEKMRELGCDKDGLQAHLIAHFGKFLTEHGRQLVGW
DEVIAGNLAKNTTVMVWRGLEKAHEAIEHGYDVVLSPGAYCYLDAYQDAPDSQLEAIGGF
LPLEKVYSYIPGEDLPEAERRRITGVQANLWTEYIPTPEHAEYMLYPRALAIAEIGWNGT
EKKDYPEFRQRALKQIEHLRRQGVNTFDLAHERGERPESKKPIKHKALGCKVIFNHRYSD
KYKAQGDQTLVDGQRGGWTYGDQKWQGYIDGDYCLDVTLDLGKRQSIKSVSAVFMQAYGA
WVFFPEEFKVSVSDDGKNFTEVYTTTSEVNRDIQSGFRTLEWKGAKQTRYIRVQGKTTMD
GGWLFTDEIVVK

Enzyme Prediction     

No EC number prediction in MGYG000003461_01296.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH20	134	479	2.5e-115	0.973293768545994

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06563	GH20_chitobiase-like	0.0	139	492	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	2.67e-147	139	479	1	345	Glycosyl hydrolase family 20, catalytic domain. This domain has a TIM barrel fold.
COG3525	Chb	5.38e-114	90	499	206	634	N-acetyl-beta-hexosaminidase [Carbohydrate transport and metabolism].
cd06568	GH20_SpHex_like	2.99e-96	139	491	1	328	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.
cd06570	GH20_chitobiase-like_1	3.42e-80	139	491	1	310	A functionally uncharacterized subgroup of the Glycosyl hydrolase family 20 (GH20) catalytic domain found in proteins similar to the chitobiase of Serratia marcescens, a beta-N-1,4-acetylhexosaminidase 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 subgroup 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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
VDS02715.1	2.62e-236	8	672	5	686
QJR73620.1	2.60e-233	14	672	13	684
AII70172.1	2.60e-233	14	672	13	684
QJR54346.1	2.60e-233	14	672	13	684
AII64491.1	2.60e-233	14	672	13	684

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6Q63_A	4.62e-126	90	622	106	712	BT0459[Bacteroides thetaiotaomicron],6Q63_B BT0459 [Bacteroides thetaiotaomicron],6Q63_C BT0459 [Bacteroides thetaiotaomicron]
7CBN_A	3.35e-97	84	528	71	524	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]
6EZR_A	4.92e-89	24	505	139	636	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	6.69e-88	24	505	136	633	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	5.13e-83	27	497	6	511	ChainA, Beta-N-acetylhexosaminidase [Bacteroides thetaiotaomicron],7DVA_A Chain A, Beta-N-acetylhexosaminidase [Bacteroides thetaiotaomicron],7DVA_B Chain B, Beta-N-acetylhexosaminidase [Bacteroides thetaiotaomicron]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P49008	5.94e-104	90	505	111	531	Beta-hexosaminidase OS=Porphyromonas gingivalis (strain ATCC BAA-308 / W83) OX=242619 GN=nahA PE=3 SV=2
B2UQG6	2.49e-96	84	528	90	543	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
P96155	9.68e-82	91	476	209	604	Beta-hexosaminidase OS=Vibrio furnissii OX=29494 GN=exoI PE=1 SV=1
B2UP57	2.38e-77	89	517	57	485	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
Q7WUL4	1.17e-54	90	494	82	465	Beta-N-acetylhexosaminidase OS=Cellulomonas fimi OX=1708 GN=hex20 PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as LIPO

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.000564	0.427374	0.571382	0.000305	0.000196	0.000152

TMHMM  Annotations     

start	end
7	29