dbCAN-seq: a database of CAZyme sequence and annotation

Basic Information help

Species

Lineage

Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Tannerellaceae; Parabacteroides;

CAZyme ID

MGYG000001735_00011

CAZy Family

GH20

CAZyme Description

hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
526	MGYG000001735_1\|CGC1	61236.36	7.9522

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001735	5309957	MAG	Sweden	Europe

Gene Location

Start: 16290; End: 17870 Strand: -

Enzyme Prediction help

No EC number prediction in MGYG000001735_00011.

CAZyme Signature Domains help

Family	Start	End	Evalue	family coverage
GH20	36	316	1.7e-36	0.8902077151335311

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06565	GH20_GcnA-like	3.78e-85	43	320	1	280	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	1.09e-22	45	317	3	277	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.
cd06564	GH20_DspB_LnbB-like	5.14e-18	43	268	2	235	Glycosyl hydrolase family 20 (GH20) catalytic domain of dispersin B (DspB), lacto-N-biosidase (LnbB) and related proteins. Dispersin B is a soluble beta-N-acetylglucosamidase found in bacteria that hydrolyzes the beta-1,6-linkages of PGA (poly-beta-(1,6)-N-acetylglucosamine), a major component of the extracellular polysaccharide matrix. Lacto-N-biosidase hydrolyzes lacto-N-biose (LNB) type I oligosaccharides at the nonreducing terminus to produce lacto-N-biose as part of the GNB/LNB (galacto-N-biose/lacto-N-biose I) degradation pathway. The lacto-N-biosidase from Bifidobacterium bifidum has this GH20 domain, a carbohydrate binding module 32, and a bacterial immunoglobulin-like domain 2, as well as a YSIRK signal peptide and a G5 membrane anchor at the N and C termini, respectively. 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	1.24e-16	85	320	61	306	Glycosyl hydrolase family 20, catalytic domain. This domain has a TIM barrel fold.
cd06563	GH20_chitobiase-like	4.40e-16	84	254	70	245	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.

CAZyme Hits help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AVM54072.1	2.08e-228	33	523	19	507
QRX64341.1	2.73e-206	19	518	15	510
ALJ60693.1	1.63e-204	18	523	12	512
QUT88323.1	4.63e-204	18	523	12	512
ALJ06766.1	6.12e-203	27	523	2	498

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6JE8_A	7.27e-08	37	316	86	434	crystalstructure of a beta-N-acetylhexosaminidase [Akkermansia muciniphila ATCC BAA-835],6JEA_A crystal structure of a beta-N-acetylhexosaminidase [Akkermansia muciniphila ATCC BAA-835],6JEB_A crystal structure of a beta-N-acetylhexosaminidase [Akkermansia muciniphila ATCC BAA-835]
1NOU_A	3.11e-07	31	293	141	415	Nativehuman lysosomal beta-hexosaminidase isoform B [Homo sapiens],1NOU_B Native human lysosomal beta-hexosaminidase isoform B [Homo sapiens],1NOW_A Human lysosomal beta-hexosaminidase isoform B in complex with (2R,3R,4S,5R)-2-Acetamido-3,4-Dihydroxy-5-Hydroxymethyl-Piperidinium Chloride (GalNAc-isofagomine) [Homo sapiens],1NOW_B Human lysosomal beta-hexosaminidase isoform B in complex with (2R,3R,4S,5R)-2-Acetamido-3,4-Dihydroxy-5-Hydroxymethyl-Piperidinium Chloride (GalNAc-isofagomine) [Homo sapiens],2GJX_B Crystallographic structure of human beta-Hexosaminidase A [Homo sapiens],2GJX_C Crystallographic structure of human beta-Hexosaminidase A [Homo sapiens],2GJX_F Crystallographic structure of human beta-Hexosaminidase A [Homo sapiens],2GJX_G Crystallographic structure of human beta-Hexosaminidase A [Homo sapiens]
1O7A_A	3.14e-07	31	293	149	423	Humanbeta-Hexosaminidase B [Homo sapiens],1O7A_B Human beta-Hexosaminidase B [Homo sapiens],1O7A_C Human beta-Hexosaminidase B [Homo sapiens],1O7A_D Human beta-Hexosaminidase B [Homo sapiens],1O7A_E Human beta-Hexosaminidase B [Homo sapiens],1O7A_F Human beta-Hexosaminidase B [Homo sapiens]
3LMY_A	3.30e-07	31	293	190	464	TheCrystal Structure of beta-hexosaminidase B in complex with Pyrimethamine [Homo sapiens],3LMY_B The Crystal Structure of beta-hexosaminidase B in complex with Pyrimethamine [Homo sapiens]
5BRO_A	2.20e-06	31	293	148	422	Crystalstructure of modified HexB (modB) [Homo sapiens]

Swiss-Prot Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
A6QNR0	1.45e-29	47	338	5	305	Hexosaminidase D OS=Bos taurus OX=9913 GN=HEXD PE=2 SV=2
Q3U4H6	3.07e-23	41	338	7	313	Hexosaminidase D OS=Mus musculus OX=10090 GN=Hexd PE=1 SV=1
Q8WVB3	5.80e-22	41	316	7	298	Hexosaminidase D OS=Homo sapiens OX=9606 GN=HEXD PE=1 SV=3
B2UP57	4.14e-07	37	316	107	455	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
P07686	1.80e-06	31	293	190	464	Beta-hexosaminidase subunit beta OS=Homo sapiens OX=9606 GN=HEXB PE=1 SV=4

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
0.007102	0.733093	0.258875	0.000413	0.000253	0.000240

TMHMM Annotations download full data without filtering help

start	end
12	31

You are here: Home > Sequence: MGYG000001735_00011