dbCAN-seq: a database of CAZyme sequence and annotation

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CAZyme Information: MGYG000003905_01334

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Basic Information help

Species

Lineage

Bacteria; Bacteroidota; Bacteroidia; Flavobacteriales; UBA1820; UBA1820;

CAZyme ID

MGYG000003905_01334

CAZy Family

GH20

CAZyme Description

N,N'-diacetylchitobiase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
849	MGYG000003905_18\|CGC1	95033.27	5.0796

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003905	1618825	MAG	China	Asia

Gene Location

Start: 488; End: 3037 Strand: -

Full Sequence Download help

Enzyme Prediction help

EC	3.2.1.52	2.4.1.-

CAZyme Signature Domains help

Family	Start	End	Evalue	family coverage
GH20	314	735	8e-94	0.9703264094955489

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06569	GH20_Sm-chitobiase-like	0.0	314	755	1	437	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.
cd06563	GH20_chitobiase-like	6.16e-108	318	739	1	350	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	1.66e-101	318	735	1	345	Glycosyl hydrolase family 20, catalytic domain. This domain has a TIM barrel fold.
COG3525	Chb	7.38e-94	265	817	205	707	N-acetyl-beta-hexosaminidase [Carbohydrate transport and metabolism].
cd06568	GH20_SpHex_like	6.14e-62	318	740	1	323	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 help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QNL38883.1	1.67e-232	17	843	20	830
QGT71689.1	1.07e-230	17	843	20	830
QUU00208.1	2.00e-230	13	844	17	829
QUT80345.1	4.27e-230	17	843	20	830
CBK66445.1	4.61e-230	15	843	31	843

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1QBA_A	1.05e-100	49	811	41	823	BACTERIALCHITOBIASE, GLYCOSYL HYDROLASE FAMILY 20 [Serratia marcescens],1QBB_A BACTERIAL CHITOBIASE COMPLEXED WITH CHITOBIOSE (DINAG) [Serratia marcescens]
1C7T_A	1.06e-98	49	811	41	823	ChainA, BETA-N-ACETYLHEXOSAMINIDASE [Serratia marcescens]
1C7S_A	5.53e-98	49	811	41	823	ChainA, BETA-N-ACETYLHEXOSAMINIDASE [Serratia marcescens]
6EZR_A	6.52e-71	268	779	211	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	8.04e-70	268	779	208	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]

Swiss-Prot Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q04786	5.23e-109	41	809	34	809	Beta-hexosaminidase OS=Vibrio vulnificus OX=672 GN=hex PE=3 SV=1
P13670	1.83e-101	49	809	66	846	N,N'-diacetylchitobiase OS=Vibrio harveyi OX=669 GN=chb PE=1 SV=1
Q54468	3.74e-99	49	811	68	850	Chitobiase OS=Serratia marcescens OX=615 GN=chb PE=1 SV=1
P49007	6.88e-85	47	773	54	762	Beta-hexosaminidase B OS=Pseudoalteromonas piscicida OX=43662 GN=nag096 PE=3 SV=1
P96155	3.14e-61	214	734	160	606	Beta-hexosaminidase OS=Vibrio furnissii OX=29494 GN=exoI PE=1 SV=1

SignalP and Lipop Annotations help

This protein is predicted as LIPO

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.000000	0.000000	1.000069	0.000000	0.000000	0.000000

TMHMM Annotations help

There is no transmembrane helices in MGYG000003905_01334.