dbCAN-seq: a database of CAZyme sequence and annotation

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CAZyme Information: MGYG000002414_04447

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Basic Information help

Species

Paenibacillus odorifer

Lineage

Bacteria; Firmicutes; Bacilli; Paenibacillales; Paenibacillaceae; Paenibacillus; Paenibacillus odorifer

CAZyme ID

MGYG000002414_04447

CAZy Family

GH20

CAZyme Description

hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
601	MGYG000002414_1\|CGC89	70123.89	5.8597

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002414	6802552	Isolate	South Korea	Asia

Gene Location

Start: 4999588; End: 5001393 Strand: -

Full Sequence Download help

Enzyme Prediction help

No EC number prediction in MGYG000002414_04447.

CAZyme Signature Domains help

Family	Start	End	Evalue	family coverage
GH20	141	356	1e-33	0.6617210682492581

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06565	GH20_GcnA-like	8.36e-62	159	420	16	276	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	8.00e-22	141	365	1	226	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.
COG3525	Chb	5.67e-15	73	348	184	509	N-acetyl-beta-hexosaminidase [Carbohydrate transport and metabolism].
pfam02838	Glyco_hydro_20b	2.39e-12	3	135	3	123	Glycosyl hydrolase family 20, domain 2. This domain has a zincin-like fold.
pfam00728	Glyco_hydro_20	6.48e-12	181	348	47	239	Glycosyl hydrolase family 20, catalytic domain. This domain has a TIM barrel fold.

CAZyme Hits help

Hit ID	Query Start	Query End	Hit Start	Hit End
AWV35100.1	1	601	1	601
AIQ75797.1	1	601	1	601
QOS80451.1	1	596	1	647
AIQ58793.1	1	601	1	610
QUL52138.1	1	601	1	612

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4C7D_A	2.54e-14	90	382	80	381	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]
1HP4_A	4.70e-14	90	382	98	399	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]
4C7G_A	5.91e-14	90	382	80	381	Structureand activity of the GH20 beta-N-acetylhexosaminidase from Streptomyces coelicolor A3(2) [Streptomyces coelicolor]
1M04_A	1.92e-13	90	382	98	399	ChainA, Beta-N-acetylhexosaminidase [Streptomyces plicatus]
1M03_A	4.45e-13	90	382	98	399	ChainA, Beta-N-acetylhexosaminidase [Streptomyces plicatus]

Swiss-Prot Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
A6QNR0	3.15e-33	141	458	1	334	Hexosaminidase D OS=Bos taurus OX=9913 GN=HEXD PE=2 SV=2
Q3U4H6	1.08e-28	141	420	9	298	Hexosaminidase D OS=Mus musculus OX=10090 GN=Hexd PE=1 SV=1
Q8WVB3	3.08e-26	141	420	9	298	Hexosaminidase D OS=Homo sapiens OX=9606 GN=HEXD PE=1 SV=3
B2UPR7	7.91e-09	74	330	164	448	Beta-hexosaminidase Amuc_2136 OS=Akkermansia muciniphila (strain ATCC BAA-835 / DSM 22959 / JCM 33894 / BCRC 81048 / CCUG 64013 / CIP 107961 / Muc) OX=349741 GN=Amuc_2136 PE=1 SV=1
P49008	2.41e-08	88	329	109	389	Beta-hexosaminidase OS=Porphyromonas gingivalis (strain ATCC BAA-308 / W83) OX=242619 GN=nahA PE=3 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
1.000073	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM Annotations help

There is no transmembrane helices in MGYG000002414_04447.