dbCAN-seq: a database of CAZyme sequence and annotation

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CAZyme Information: MGYG000003018_01975

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Basic Information help

Species

Alistipes_A sp900549685

Lineage

Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Rikenellaceae; Alistipes_A; Alistipes_A sp900549685

CAZyme ID

MGYG000003018_01975

CAZy Family

GH20

CAZyme Description

hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
703		79451.75	5.4438

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003018	2600623	MAG	China	Asia

Gene Location

Start: 153; End: 2264 Strand: +

Full Sequence Download help

Enzyme Prediction help

No EC number prediction in MGYG000003018_01975.

CAZyme Signature Domains help

Family	Start	End	Evalue	family coverage
GH20	181	476	4.7e-35	0.9525222551928784

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06565	GH20_GcnA-like	2.37e-67	190	475	10	301	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.
cd02742	GH20_hexosaminidase	1.29e-24	195	415	14	237	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.
pfam02838	Glyco_hydro_20b	2.78e-23	32	175	1	123	Glycosyl hydrolase family 20, domain 2. This domain has a zincin-like fold.
COG3525	Chb	1.72e-17	127	367	206	490	N-acetyl-beta-hexosaminidase [Carbohydrate transport and metabolism].
pfam00728	Glyco_hydro_20	1.75e-14	195	416	16	265	Glycosyl hydrolase family 20, catalytic domain. This domain has a TIM barrel fold.

CAZyme Hits help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QGA23073.1	0.0	3	700	2	698
QNI31352.1	3.95e-123	25	667	25	668
AHG90566.1	1.19e-122	21	694	15	693
QNI34778.1	7.87e-118	16	694	7	680
SDF25835.1	4.91e-112	98	694	84	693

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4C7D_A	5.61e-21	35	371	9	340	Structureand activity of the GH20 beta-N-acetylhexosaminidase from Streptomyces coelicolor A3(2) [Streptomyces coelicolor],4C7D_B Structure and activity of the GH20 beta-N-acetylhexosaminidase from Streptomyces coelicolor A3(2) [Streptomyces coelicolor],4C7F_A Structure and activity of the GH20 beta-N-acetylhexosaminidase from Streptomyces coelicolor A3(2) [Streptomyces coelicolor],4C7F_B Structure and activity of the GH20 beta-N-acetylhexosaminidase from Streptomyces coelicolor A3(2) [Streptomyces coelicolor]
4C7G_A	1.32e-20	35	371	9	340	Structureand activity of the GH20 beta-N-acetylhexosaminidase from Streptomyces coelicolor A3(2) [Streptomyces coelicolor]
1HP4_A	1.96e-20	35	371	27	358	ChainA, Beta-n-acetylhexosaminidase [Streptomyces plicatus],1HP5_A Chain A, Beta-n-acetylhexosaminidase [Streptomyces plicatus],1JAK_A Chain A, Beta-N-acetylhexosaminidase [Streptomyces plicatus],1M01_A Chain A, Beta-N-acetylhexosaminidase [Streptomyces plicatus],5FCZ_A Chain A, B-N-acetylhexosaminidase [Streptomyces plicatus],5FD0_A Chain A, B-N-acetylhexosaminidase [Streptomyces plicatus]
1M04_A	8.12e-20	35	371	27	358	ChainA, Beta-N-acetylhexosaminidase [Streptomyces plicatus]
7BWG_A	1.19e-19	26	422	10	406	AGlycoside Hydrolase Family 20 beta-N-Acetylglucosaminidase [Microbacterium sp. HJ5],7BWG_B A Glycoside Hydrolase Family 20 beta-N-Acetylglucosaminidase [Microbacterium sp. HJ5]

Swiss-Prot Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P96155	1.85e-22	28	424	134	534	Beta-hexosaminidase OS=Vibrio furnissii OX=29494 GN=exoI PE=1 SV=1
Q3U4H6	2.09e-17	190	472	17	321	Hexosaminidase D OS=Mus musculus OX=10090 GN=Hexd PE=1 SV=1
P49008	2.47e-17	27	366	29	387	Beta-hexosaminidase OS=Porphyromonas gingivalis (strain ATCC BAA-308 / W83) OX=242619 GN=nahA PE=3 SV=2
Q8WVB3	1.35e-13	190	472	17	321	Hexosaminidase D OS=Homo sapiens OX=9606 GN=HEXD PE=1 SV=3
A6QNR0	5.85e-13	190	451	9	290	Hexosaminidase D OS=Bos taurus OX=9913 GN=HEXD PE=2 SV=2

SignalP and Lipop Annotations help

This protein is predicted as SP

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.000271	0.999073	0.000178	0.000164	0.000150	0.000137

TMHMM Annotations help

There is no transmembrane helices in MGYG000003018_01975.