CAZyme Information: MGYG000000437_01415

Basic Information

• Species: Alistipes sp001941065
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Rikenellaceae; Alistipes; Alistipes sp001941065
• CAZyme ID: MGYG000000437_01415
• CAZy Family: GH20
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
518		58907.4	6.074

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000437	3341375	MAG	Sweden	Europe

• Gene Location: Start: 8993; End: 10549 Strand: -

Full Sequence      

MKHCFLTVAAALLTLSTGIGTCAARTGDFPVRAFHLDFRTEVMTLDAMKRLVDRISERGI
NTLVMEWEATFPFDKHATLSNASAFTREEVISFVDYCSGRGVEVIPLQNCFGHCEYILQH
ERYRALREDPKDPSQVCPLKIAEATACFSELFAEVAALHPSKYFHIGADETYLLGLCGNC
RAVADREGKSRLFVDYVKAMCDIVHDLGKTPVMWADIILKYPEALDELPDELIFVDWNYG
WEPDRFGKLANLFSRGVKLWGAPALRSGPDNIYLTQWKKHFDNLAVFVEYAREHDYGGMI
ETSWSTSGTYGYWFDNGYEILSMQPVRLVYPMSAFRILEAACCEAFVTDAPFEPEAFVRR
YARTELGLDDAGADVLWRYFSMPQETVAVSDSGAKDASGRDLHEVIDECVRMRDELARLK
PRKGAEEVAHYLLMLDIRINYLRFKAVEARYQSASFGRSGIPGLVSGLKTLLAEARILDR
RFARLNASYLKAHEIEYINTMRSVKMKSLYERLTNNTR

Enzyme Prediction     

No EC number prediction in MGYG000000437_01415.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH20	25	259	1.5e-38	0.7181008902077152

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06565	GH20_GcnA-like	4.71e-81	31	308	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	1.34e-22	32	305	2	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.
pfam00728	Glyco_hydro_20	2.29e-19	29	251	1	252	Glycosyl hydrolase family 20, catalytic domain. This domain has a TIM barrel fold.
cd06564	GH20_DspB_LnbB-like	1.54e-18	30	243	1	227	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.
cd06563	GH20_chitobiase-like	3.50e-14	29	243	1	246	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     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QUT88323.1	2.99e-205	1	514	1	511
ALJ60693.1	4.24e-205	1	514	1	511
QIU93919.1	4.83e-192	23	518	29	516
AVM54072.1	1.38e-167	28	511	26	503
AYN69240.1	4.66e-163	28	513	16	497

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4C7D_A	9.76e-08	26	214	136	332	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	2.31e-07	26	296	154	426	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]
7PUL_A	2.79e-06	81	259	88	269	ChainA, Beta-N-acetylhexosaminidase [Enterococcus faecalis]
6JE8_A	6.19e-06	85	214	165	307	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
A6QNR0	1.55e-23	31	304	1	290	Hexosaminidase D OS=Bos taurus OX=9913 GN=HEXD PE=2 SV=2
Q3U4H6	2.50e-19	29	249	7	235	Hexosaminidase D OS=Mus musculus OX=10090 GN=Hexd PE=1 SV=1
Q8WVB3	1.89e-18	29	304	7	298	Hexosaminidase D OS=Homo sapiens OX=9606 GN=HEXD PE=1 SV=3

SignalP and Lipop Annotations

This protein is predicted as LIPO

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.005627	0.427992	0.565008	0.000701	0.000325	0.000336

TMHMM  Annotations     

start	end
5	27