dbCAN-seq: a database of CAZyme sequence and annotation

Basic Information help

Species

Lineage

Bacteria; Firmicutes_A; Clostridia; Oscillospirales; UBA644; ;

CAZyme ID

MGYG000002695_00181

CAZy Family

GH20

CAZyme Description

hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
624	MGYG000002695_1\|CGC2	72449.88	4.837

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002695	1947536	MAG	Canada	North America

Gene Location

Start: 200098; End: 201972 Strand: +

Enzyme Prediction help

No EC number prediction in MGYG000002695_00181.

CAZyme Signature Domains help

Family	Start	End	Evalue	family coverage
GH20	128	371	5.5e-47	0.7388724035608308

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06565	GH20_GcnA-like	9.42e-81	131	429	1	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.
pfam00728	Glyco_hydro_20	1.14e-30	130	367	2	263	Glycosyl hydrolase family 20, catalytic domain. This domain has a TIM barrel fold.
cd02742	GH20_hexosaminidase	6.79e-24	131	428	1	297	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.
cd06570	GH20_chitobiase-like_1	4.33e-21	132	339	4	223	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.
cd06563	GH20_chitobiase-like	4.66e-20	130	366	2	262	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
QJD87484.1	9.53e-102	3	587	8	608
AIQ50869.1	2.92e-100	3	587	9	615
QSF45803.1	1.77e-99	3	587	9	615
QNK59368.1	1.81e-98	62	457	66	470
AYQ72904.1	1.18e-96	1	458	7	476

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1NOU_A	4.97e-14	41	319	44	359	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	5.09e-14	41	319	52	367	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]
2GK1_I	5.17e-14	79	359	26	324	X-raycrystal structure of NGT-bound HexA [Homo sapiens],2GK1_J X-ray crystal structure of NGT-bound HexA [Homo sapiens],2GK1_K X-ray crystal structure of NGT-bound HexA [Homo sapiens],2GK1_L X-ray crystal structure of NGT-bound HexA [Homo sapiens]
3LMY_A	5.62e-14	41	319	93	408	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]
2GJX_A	6.59e-14	79	359	92	390	Crystallographicstructure of human beta-Hexosaminidase A [Homo sapiens],2GJX_D Crystallographic structure of human beta-Hexosaminidase A [Homo sapiens],2GJX_E Crystallographic structure of human beta-Hexosaminidase A [Homo sapiens],2GJX_H Crystallographic structure of human beta-Hexosaminidase A [Homo sapiens]

Swiss-Prot Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
E9DFH0	2.44e-17	64	420	103	487	Beta-hexosaminidase 1 OS=Coccidioides posadasii (strain RMSCC 757 / Silveira) OX=443226 GN=HEX1 PE=1 SV=1
P43077	1.52e-15	44	470	80	546	Beta-hexosaminidase OS=Candida albicans OX=5476 GN=HEX1 PE=1 SV=1
Q54SC9	2.39e-14	56	322	82	368	Beta-hexosaminidase subunit A2 OS=Dictyostelium discoideum OX=44689 GN=hexa2 PE=3 SV=1
P07686	3.08e-13	41	319	93	408	Beta-hexosaminidase subunit beta OS=Homo sapiens OX=9606 GN=HEXB PE=1 SV=4
P06865	3.83e-13	79	359	114	412	Beta-hexosaminidase subunit alpha OS=Homo sapiens OX=9606 GN=HEXA PE=1 SV=2

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
1.000041	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM Annotations help

There is no transmembrane helices in MGYG000002695_00181.

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