CAZyme Information: MGYG000000170_01387

Basic Information

• Species: Alistipes_A sp900240235
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Rikenellaceae; Alistipes_A; Alistipes_A sp900240235
• CAZyme ID: MGYG000000170_01387
• CAZy Family: GH20
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
829	MGYG000000170_4|CGC1	94145.82	6.8023

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000170	3119069	Isolate	China	Asia

• Gene Location: Start: 42548; End: 45037 Strand: +

Full Sequence      

MKSSLSLLFVLLGLFCHGQNLIPRPERADKREGEFLVAKQTEIYSPAFPDLFDYLNDHIE
RVCGYRLAAGGHRRSIQQISIEKHEGGLSEEGYLLDISPSRITIRANDRGGAFYALQTLF
QLMPVSVYRPDAAQHAETFAIPCFHIEDAPRFAYRGVMLDVSRNFSDKAAVMRYIDWIAR
HKLNTLHWHLTDDNGWRVEIKKYPELTSRGAWRGPGEVLPPSYGSGNERYGGFYTQQDVR
EIVDYAAFRNVEIIPEIDLPGHSQTLTSVYPETFCRTSGSVTYKPEEMRETLCAGREENF
EMLRDILQELAGLFPSKYIHIGGDEVSVRYWRNCPRCRALMTEKKMKTPAELRGYFVHRL
EDLVHSVGKTCAAWNEAVQARNLRPATLIYGWENVDVCRQAAAAGQPVVMMPASYCYIDM
KQHPWDRGHTWAGRVDVRRVYDFEPADFLSAERLERVRGVEAAQWAELLNEPERFAEYQG
YPRLCALAEVGWTQPGQRDWNDFYRRLTSGHLERLGAMGIRFRMFPPQTEYRSGVVTVTP
EIAGVEIRYTTDLSEPDESSALYTEPLRTDRPERYRFRAFGCGGYSTAVFPVAELFRAEL
APAEQRVFRVPLKDYVTRDGLWLLSFTQRRDNAMIVRLEVSGPDTAYTIIRNGQKINPLR
DLRLYADSANRTADLLVTLKNNSSKREELTLNLRPSPYIEPAVSVTSSLTCSGKFPIRNS
ADYQFSSYVRTVSPCKAGDYILFAFDEPVDCEAIDVRTGLPDVTRYIVTDGTAACSADGK
TFGEEIPLKPDGSVVLRPSAPVRAVRISIRGGNGETILGWQDLRVVPRL

Enzyme Prediction     

No EC number prediction in MGYG000000170_01387.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH20	147	494	4.6e-108	0.973293768545994

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06563	GH20_chitobiase-like	4.25e-167	152	507	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	1.30e-127	152	494	1	345	Glycosyl hydrolase family 20, catalytic domain. This domain has a TIM barrel fold.
COG3525	Chb	1.27e-123	21	566	136	688	N-acetyl-beta-hexosaminidase [Carbohydrate transport and metabolism].
cd06568	GH20_SpHex_like	1.35e-98	152	507	1	329	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.
cd06569	GH20_Sm-chitobiase-like	4.47e-84	148	507	1	445	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. 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
QGA24588.1	0.0	1	829	1	829
BCG55301.1	0.0	17	829	22	833
AYN06483.1	1.63e-212	1	827	1	834
ABQ07807.1	2.62e-208	1	827	1	834
AOC95872.1	9.07e-206	1	827	1	833

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6EZR_A	2.81e-102	17	523	138	638	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	3.80e-101	17	523	135	635	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	1.09e-89	21	507	6	506	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	5.78e-89	21	507	6	506	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]
6Q63_A	1.22e-86	91	602	106	623	BT0459[Bacteroides thetaiotaomicron],6Q63_B BT0459 [Bacteroides thetaiotaomicron],6Q63_C BT0459 [Bacteroides thetaiotaomicron]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P96155	4.24e-90	20	491	140	604	Beta-hexosaminidase OS=Vibrio furnissii OX=29494 GN=exoI PE=1 SV=1
P49008	5.20e-88	18	589	34	607	Beta-hexosaminidase OS=Porphyromonas gingivalis (strain ATCC BAA-308 / W83) OX=242619 GN=nahA PE=3 SV=2
B2UP57	3.57e-77	88	508	55	463	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	1.06e-73	85	523	91	530	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	1.53e-62	21	526	6	481	Beta-N-acetylhexosaminidase OS=Cellulomonas fimi OX=1708 GN=hex20 PE=1 SV=1

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
0.000227	0.999196	0.000155	0.000146	0.000135	0.000128

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000170_01387.