CAZyme Information: MGYG000004329_01161

Basic Information

• Species: Prevotellamassilia sp900539625
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Prevotellamassilia; Prevotellamassilia sp900539625
• CAZyme ID: MGYG000004329_01161
• CAZy Family: GH20
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1171		129579.89	5.8416

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000004329	2571737	MAG	Israel	Asia

• Gene Location: Start: 13476; End: 16991 Strand: +

Full Sequence      

MKKTLLLCFFCLLAISQLWAAEKPKVSVGDDVTWYLVQMSNGKGVLTAQGDGEEVLTGIP
MGRDAQFWKIEGSATTGYTLTSRSGLTLYTTTTKQEGMFKAGKTPNANKYFVWQTTTNAN
YSGDFVISPKANLGVYMNQWGGAGTGKKLGLWNDRSDANQPLTFVSEEDFEKMGKMLSLV
PYPASVTKGDGSLSLSKIDGIVATGDAPLRYASEFASQAKRTLGIDLQVNPASAACAISM
VADKTLEHEAYRLNINASGVEIASADSTGFFYGLQTLKQLLPAAIYGKKLQKNDGWTLPY
VEIVDKPNLGHRGFMLDVARHFFSKTEVMRVLDVMASYKMNRFHWHLTDDQGWRIEIPEY
PRLTEVGSVRAGSFSNAGGASKFFDDTEYGRGMWYSLNDLREIVAYAKDRNIEIIPEIDL
PGHMVAAVAAYPELSCDPSKSYSVRIDGGISKDVLNIGKDEVVDFLKCVLGHVAEVFPYQ
YIHLGGDECPTGQWANNADCLRRVKEKGLSGVNELQSWLVEELGLYLKEKYGKDIVVWDE
LLSHWNADNKVKPVIMAWNNINMSSKAADKGFKSIVVPYQSLYLDMMQVPMAQRDINEKY
QGGWGDNWVNSVETVYNVNPVASLSGREDFCLGVQGNMWTETCNDSVELEYQLFPRLLAL
SETGWLPAAKKNWVGFYMRLQTQRSVLDEMGVTYATHYFEKPEQTAAQKAVEEAEEIIAA
AGDYVGLPAADKKTAMTEALSDLKGDMENADKLAALTASVGQYKKADITMPEEGKYYQIL
SASTYYKAKYEGSSLYASDNNVRFHYTKQYEPEEIWQFEAVTGGYKVKNVITGKALTMPA
GNAENMTLTANGSVMKIALATKASGQYTYIPAVLNIFSGGKYLTADCTGYAKSGADAALC
YQGTWRIVEVKDFTFMLKHLVEKCETILHNAKPGEMGEPTEAALSLLSDEIIAPAKALIG
KGAVSRSEYDKFLTLYAQFVAMPRTSVLDALDEGYYYNLRNAYFTNYLAMASTSNTVQPR
TMSNNTDAYQWRIRKNADGTVSIFSKVGDKPAYPASDAETKNILLGKEYSWKLNQHTCDE
GKTGIRIISASGAYSWYVNASSWANNVILKPIAWGASIWTFEKLNISTSINNVNTSSAAP
SNVYYDLQGRQLHQPVQHGVYINGNGEKVIR

Enzyme Prediction     

EC	3.2.1.52

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH20	310	665	4.3e-106	0.9495548961424333

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06563	GH20_chitobiase-like	2.51e-153	310	680	2	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	1.71e-129	310	665	2	343	Glycosyl hydrolase family 20, catalytic domain. This domain has a TIM barrel fold.
COG3525	Chb	7.81e-98	157	687	119	637	N-acetyl-beta-hexosaminidase [Carbohydrate transport and metabolism].
cd06568	GH20_SpHex_like	4.97e-83	310	680	2	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	7.23e-75	310	684	2	341	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
QFQ12497.1	1.45e-229	178	909	35	713
QFQ12789.1	1.45e-206	15	980	13	954
BBL09404.1	2.83e-115	177	699	24	540
BBL01546.1	2.83e-115	177	699	24	540
BBL12197.1	2.83e-115	177	699	24	540

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
7DUP_A	2.68e-114	177	697	4	523	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	1.41e-113	177	697	4	523	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]
6Q63_A	2.02e-92	210	700	65	542	BT0459[Bacteroides thetaiotaomicron],6Q63_B BT0459 [Bacteroides thetaiotaomicron],6Q63_C BT0459 [Bacteroides thetaiotaomicron]
3RCN_A	3.98e-91	179	694	10	513	CrystalStructure of Beta-N-Acetylhexosaminidase from Arthrobacter aurescens [Paenarthrobacter aurescens TC1]
7CBN_A	3.62e-77	180	694	14	510	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	8.97e-99	175	702	33	540	Beta-hexosaminidase OS=Porphyromonas gingivalis (strain ATCC BAA-308 / W83) OX=242619 GN=nahA PE=3 SV=2
B2UQG6	2.62e-76	180	694	33	529	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	5.11e-67	177	664	139	604	Beta-hexosaminidase OS=Vibrio furnissii OX=29494 GN=exoI PE=1 SV=1
B2UP57	2.71e-62	245	687	54	469	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
Q04786	5.41e-54	179	669	200	721	Beta-hexosaminidase OS=Vibrio vulnificus OX=672 GN=hex PE=3 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
0.000234	0.999146	0.000169	0.000158	0.000146	0.000136

TMHMM  Annotations     

There is no transmembrane helices in MGYG000004329_01161.