CAZyme Information: MGYG000002584_01370

Basic Information

• Species: Akkermansia sp900545155
• Lineage: Bacteria; Verrucomicrobiota; Verrucomicrobiae; Verrucomicrobiales; Akkermansiaceae; Akkermansia; Akkermansia sp900545155
• CAZyme ID: MGYG000002584_01370
• CAZy Family: GH20
• CAZyme Description: Beta-hexosaminidase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
506	MGYG000002584_10|CGC4	57045.39	7.9306

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002584	3044716	MAG	China	Asia

• Gene Location: Start: 66032; End: 67552 Strand: +

Full Sequence      

MSPFFPALTALFSLAFGQGITASAAPDFTERPAYIIPEPREIITDDGLLKKPFPIKNVID
KSLDPEAYELIITPREAFVKSSTPAGRLYGHSTLDQLISQFGDKGIPCGTIKDSPRYPWR
GLMLDPARHFIPVSDIRKFIDVMAYYKFNRLHLHLTDDQGWRLPVPGYPRLKTIASHREE
TNGDGKPHGGMYTKQELKDLVRYAAAKNVEIIPEVDAPGHNVALAAAYPEFICFPNPNLK
VFTSNGVTKELVCPGNPDIWRFYTAVIKELKDIFPSRYIHLGGDEAPEDNWMKCPKCAAW
RKAAGIAEPKDGDNNAMKTAARQEMIQFFSRLTDIVNKAGKEPLFWYEQPIASYPKGSTV
YTWRLGLTPDTVARTRKEGLKLIFSPGEHCYLDYPQLPGDWPKKEPAGGWMPTTTLEQTY
KLDPGRGLTEEDAAHIVGVEATMWGECIPDINKAFYMAYPRALALSEAGWSPADVRSWER
FQGKLDQHRNIMQKKWNISLERPAKK

Enzyme Prediction     

No EC number prediction in MGYG000002584_01370.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH20	112	472	1.9e-102	0.973293768545994

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06563	GH20_chitobiase-like	2.21e-156	117	485	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	6.32e-131	117	472	1	345	Glycosyl hydrolase family 20, catalytic domain. This domain has a TIM barrel fold.
cd06568	GH20_SpHex_like	2.33e-102	117	485	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.
COG3525	Chb	4.81e-85	63	496	203	641	N-acetyl-beta-hexosaminidase [Carbohydrate transport and metabolism].
cd06562	GH20_HexA_HexB-like	5.10e-72	117	492	1	344	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
QWP03669.1	6.61e-215	24	506	18	493
QWP27460.1	6.61e-215	24	506	18	493
QWP68878.1	6.61e-215	24	506	18	493
QWP61543.1	6.61e-215	24	506	18	493
QWP64076.1	6.61e-215	24	506	18	493

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6JE8_A	1.34e-180	35	502	6	458	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]
7CBN_A	6.00e-88	60	487	72	498	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]
6Q63_A	2.35e-87	64	485	104	522	BT0459[Bacteroides thetaiotaomicron],6Q63_B BT0459 [Bacteroides thetaiotaomicron],6Q63_C BT0459 [Bacteroides thetaiotaomicron]
7DUP_A	5.11e-80	59	497	72	519	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	2.78e-79	59	497	72	519	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
B2UP57	2.93e-180	19	502	10	479	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
B2UQG6	4.38e-87	60	487	91	517	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
P49008	9.56e-76	63	486	108	519	Beta-hexosaminidase OS=Porphyromonas gingivalis (strain ATCC BAA-308 / W83) OX=242619 GN=nahA PE=3 SV=2
P96155	8.67e-73	62	469	204	604	Beta-hexosaminidase OS=Vibrio furnissii OX=29494 GN=exoI PE=1 SV=1
Q7WUL4	1.70e-59	66	488	82	466	Beta-N-acetylhexosaminidase OS=Cellulomonas fimi OX=1708 GN=hex20 PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.000488	0.998757	0.000182	0.000201	0.000167	0.000154

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002584_01370.