CAZyme Information: MGYG000002412_00359

Basic Information

• Species: Prevotellamassilia timonensis
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Prevotellamassilia; Prevotellamassilia timonensis
• CAZyme ID: MGYG000002412_00359
• CAZy Family: GH20
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1173		128904.83	5.4512

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002412	3472293	Isolate	not provided	not provided

• Gene Location: Start: 56034; End: 59555 Strand: +

Full Sequence      

MKLRLLTLLTLVMTVLHLNAAPVEPQVSSGNQVHWYVLKFLNQNNVLEAKGDGAEVKTAG
FKGNKNQLWKIEGNATTGYTLTCKNGMKLYTTTTAKEGKFMAGNTPNENTHFVWQATTNT
TYADGWVLSPKANTLVYMNQWGGAGAGKSLGLWNDKASADQPLAFVKAEDLLGEAENMLP
LIPYPANLTRNEGTFNLKQLTAITTPAGDEAVARYAQEFATQLEKTSGIKVLVNPTTAAT
SLVMTKDATLAHEAYKLTVNEAGINIAAADSTGFFYAIQTLKQLMPHAIYYRNSASTAID
WTVPCVEIADQPQLGHRGYMLDVARHFFSKTEVKRILDIMATYKMNRFHWHLTDDQGWRI
DIPEYPKLAQVGAVRKGSFVNAGGSSKFFDDTEYGRGMYYTLDDLREIVAYAKSLNIEII
PEIDLPGHMVAAVAAYPEFSCDPTKKYEVRIDGGISKDVLNIGKDETIDFLKCVLGHMAE
IFPYKYIHLGGDECPTDQWSHNADCLKRVKDEGLAGVNELQSWLVEKLGLYLKEKYNKDI
ICWDELLAHWKSDNTVKPVIMAWNHINKSKEAADKGFKSIVVPYQSLYLDMMQVPLSEVD
VNEKYQGGWGDNWVNSVETVYGVNPVASLSGKEDFCLGVQGNMWTETCNDSVEVEYQLLP
RMLALSETGWLPAAKKDFASFYMRLQKNRDILDAKGLTYATHYFDEPDLTEQEAAVAEAA
SLLENAKPGKVGYPSQTEYDKLSSAYAPFIADNGATGDVAALKAAIAAYKTAAVTMPVEG
KTYKLVSASTYYKAKYVGSTAYVDGSQIRFHYTPQVEPEELWQFTAKDGGYVMTNALTGK
QVVMPANNNANITLADAGTTLTIAQATVASGKYSYVAGALNIGTNGKYLSADCTGLVKAG
TNTALCYQGTWYLEEVTDFTAQLNGLVKKANRIVAESNPGAMGEPTEEAIALLSNDLIAP
ATAAVAAGSVSEAAYKQYQEVYAQYLAMPRVSPISGIDESYYYYIRNAFFDTYYAEAQAD
GTIAPRTKGEGDSFLWQFVKKGDKVSIISKLTGKPAYIDTEADGTNLKTGSPYEWGLNEY
TCDEGKTGIQIITANGEFSWYTNPNAWKNNVILKPKTYGAAIWTFEVSNVATGVHATTAP
AIVPTSYYDLQGRRVSQPSHGVYVTNTGRKVIK

Enzyme Prediction     

EC	3.2.1.52

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH20	315	670	3.1e-105	0.9495548961424333

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06563	GH20_chitobiase-like	2.30e-154	315	685	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	4.94e-125	315	670	2	343	Glycosyl hydrolase family 20, catalytic domain. This domain has a TIM barrel fold.
COG3525	Chb	1.10e-91	159	699	103	642	N-acetyl-beta-hexosaminidase [Carbohydrate transport and metabolism].
cd06568	GH20_SpHex_like	9.17e-82	315	685	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	6.72e-72	315	696	2	348	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	3.08e-232	244	915	75	713
QFQ12789.1	1.68e-193	8	998	8	972
QUT70076.1	5.50e-125	179	702	24	543
QMW86727.1	2.18e-123	171	702	12	543
AAO79499.1	2.18e-123	171	702	12	543

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
7DUP_A	1.07e-124	179	702	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	5.69e-124	179	702	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	5.23e-97	181	705	31	542	BT0459[Bacteroides thetaiotaomicron],6Q63_B BT0459 [Bacteroides thetaiotaomicron],6Q63_C BT0459 [Bacteroides thetaiotaomicron]
3RCN_A	5.44e-80	247	699	72	513	CrystalStructure of Beta-N-Acetylhexosaminidase from Arthrobacter aurescens [Paenarthrobacter aurescens TC1]
7CBN_A	4.58e-76	242	699	67	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	1.69e-97	174	746	30	581	Beta-hexosaminidase OS=Porphyromonas gingivalis (strain ATCC BAA-308 / W83) OX=242619 GN=nahA PE=3 SV=2
B2UQG6	1.76e-75	174	699	28	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	1.27e-62	179	669	139	604	Beta-hexosaminidase OS=Vibrio furnissii OX=29494 GN=exoI PE=1 SV=1
B2UP57	9.32e-62	249	692	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	3.12e-52	165	746	185	778	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
0.000184	0.999234	0.000141	0.000153	0.000132	0.000130

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002412_00359.