CAZyme Information: MGYG000003701_03868

Basic Information

• Species: Parabacteroides sp003480915
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Tannerellaceae; Parabacteroides; Parabacteroides sp003480915
• CAZyme ID: MGYG000003701_03868
• CAZy Family: GH20
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
778	MGYG000003701_10|CGC4	87560.84	5.498

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003701	6084075	Isolate	China	Asia

• Gene Location: Start: 251668; End: 254004 Strand: +

Full Sequence      

MITQQISQMTKDKLLLITFLVWLVTGCTNPAPVGINIIPQPEQQIPAKGYFTFNESTTIQ
IENQEQEPVARLLADLFTTSAGFNPIINANSSQTATITFSTNTALAEENYKLEITPSHIS
IEAADNRGFFYAVQSIRQLLPPAIESKTPAEGIQWNIPAVSLQDGPRFPYRGLLLDVSRC
FIPKENVIKIIDYMSMLKLNKLHLHLVDDNGWRLEIKKYPRLTEVGAWRVEREKDFSQRK
NAKAGEPTPVGGFYTQEDMKEIIAYAGTRQVEIIPEIEMPAHTNSALAAFPELACPVVKD
PIRVIPGMGGHGAEIVYCAGNDKVFSFLQDVLDEVMTLFPSRYINLGGDEASKRYWKICP
LCQARMKAEGFTDIEELQGYFMGRMAGYVKSKGREVIGWDELTNSKIPDDAIILGWQGLG
TAGYKAGQMGHRFIMTPARVLYLIRYQGPQWFEPRTYFGNNTLENVYKYEPVQPEWDPEV
AKKLIGVQGCMWTEFCSSADDVEYLLFPRLAAVGEIAWSGKDRKDWPGFLKRLDILTQHY
DYLGVNYARSMFNLDHLVTGSNDTLKVALTCIRPDMEVRYTTDGSEPQAASTLYQDSLIV
TGDLTIKAATFMNGEQKGKTLTLPLHWNKATARPVTNGNEQSYRLTNGLRGSDKQSDFEW
SGWYGKDASFTIDLGKTASFDKVTIGCMTNYGMGAHLPKQIILSVSDDNQTFTRIAERSF
TPEQIFREGIRIEDQLFDNLKASGRYLKVDLQNPGKCPEDHTRPGQGSWVYIDEVIIK

Enzyme Prediction     

No EC number prediction in MGYG000003701_03868.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH20	163	520	1.3e-109	0.973293768545994

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06563	GH20_chitobiase-like	3.59e-171	168	533	1	357	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.
pfam00728	Glyco_hydro_20	1.31e-140	168	520	1	345	Glycosyl hydrolase family 20, catalytic domain. This domain has a TIM barrel fold.
COG3525	Chb	7.46e-104	35	646	127	732	N-acetyl-beta-hexosaminidase [Carbohydrate transport and metabolism].
cd06568	GH20_SpHex_like	7.02e-81	168	533	1	329	A subgroup of the Glycosyl hydrolase family 20 (GH20) catalytic domain found in proteins similar to the N-acetylhexosaminidase from Streptomyces plicatus (SpHex). SpHex catalyzes the hydrolysis of N-acetyl-beta-hexosaminides. An Asp residue within the active site plays a critical role in substrate-assisted catalysis by orienting the 2-acetamido group and stabilizing the transition state. 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. Proteins belonging to this subgroup lack the C-terminal PKD (polycystic kidney disease I)-like domain found in the chitobiases.
cd06562	GH20_HexA_HexB-like	1.89e-68	168	533	1	337	Beta-N-acetylhexosaminidases 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. The hexA and hexB genes encode the alpha- and beta-subunits of the two major beta-N-acetylhexosaminidase isoenzymes, N-acetyl-beta-D-hexosaminidase A (HexA) and beta-N-acetylhexosaminidase B (HexB). Both the alpha and the beta catalytic subunits have a TIM-barrel fold and belong to the glycosyl hydrolase family 20 (GH20). The HexA enzyme is a heterodimer containing one alpha and one beta subunit while the HexB enzyme is a homodimer containing two beta-subunits. Hexosaminidase mutations cause an inability to properly hydrolyze certain sphingolipids which accumulate in lysosomes within the brain, resulting in the lipid storage disorders Tay-Sachs and Sandhoff. Mutations in the alpha subunit cause in a deficiency in the HexA enzyme and result in Tay-Sachs, mutations in the beta-subunit cause in a deficiency in both HexA and HexB enzymes and result in Sandhoff disease. In both disorders GM(2) gangliosides accumulate in lysosomes. 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
QUT71945.1	0.0	9	778	1	776
QNL38602.1	0.0	14	778	7	774
ALJ41001.1	0.0	9	778	1	776
AAO76734.1	0.0	14	778	7	776
QMW88597.1	0.0	9	778	1	776

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6Q63_A	1.82e-129	23	777	16	773	BT0459[Bacteroides thetaiotaomicron],6Q63_B BT0459 [Bacteroides thetaiotaomicron],6Q63_C BT0459 [Bacteroides thetaiotaomicron]
7DUP_A	3.09e-100	35	556	4	529	ChainA, Beta-N-acetylhexosaminidase [Bacteroides thetaiotaomicron],7DVA_A Chain A, Beta-N-acetylhexosaminidase [Bacteroides thetaiotaomicron],7DVA_B Chain B, Beta-N-acetylhexosaminidase [Bacteroides thetaiotaomicron]
7DVB_A	1.67e-99	35	556	4	529	ChainA, Beta-N-acetylhexosaminidase [Bacteroides thetaiotaomicron],7DVB_B Chain B, Beta-N-acetylhexosaminidase [Bacteroides thetaiotaomicron],7DVB_C Chain C, Beta-N-acetylhexosaminidase [Bacteroides thetaiotaomicron],7DVB_D Chain D, Beta-N-acetylhexosaminidase [Bacteroides thetaiotaomicron]
3RCN_A	3.99e-94	104	533	74	498	CrystalStructure of Beta-N-Acetylhexosaminidase from Arthrobacter aurescens [Paenarthrobacter aurescens TC1]
7CBN_A	2.06e-91	65	549	39	512	Crystalstructure of beta-N-acetylhexosaminidase Am0868 from Akkermansia muciniphila [Akkermansia muciniphila ATCC BAA-835],7CBO_A Crystal structure of beta-N-acetylhexosaminidase Am0868 from Akkermansia muciniphila in complex with GlcNAc [Akkermansia muciniphila ATCC BAA-835]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P49008	1.55e-123	34	610	34	599	Beta-hexosaminidase OS=Porphyromonas gingivalis (strain ATCC BAA-308 / W83) OX=242619 GN=nahA PE=3 SV=2
B2UQG6	5.55e-91	28	549	23	531	Beta-hexosaminidase Amuc_0868 OS=Akkermansia muciniphila (strain ATCC BAA-835 / DSM 22959 / JCM 33894 / BCRC 81048 / CCUG 64013 / CIP 107961 / Muc) OX=349741 GN=Amuc_0868 PE=1 SV=1
P96155	6.97e-79	35	524	139	608	Beta-hexosaminidase OS=Vibrio furnissii OX=29494 GN=exoI PE=1 SV=1
B2UP57	1.76e-60	105	533	55	462	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
Q7WUL4	2.48e-50	35	550	4	480	Beta-N-acetylhexosaminidase OS=Cellulomonas fimi OX=1708 GN=hex20 PE=1 SV=1

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
0.000070	0.000601	0.999334	0.000015	0.000004	0.000002

TMHMM  Annotations     

start	end
13	35