CAZyme Information: MGYG000002984_00499

Basic Information

• Species: UBA737 sp900554525
• Lineage: Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Acutalibacteraceae; UBA737; UBA737 sp900554525
• CAZyme ID: MGYG000002984_00499
• CAZy Family: GH20
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
930	MGYG000002984_39|CGC1	103753.89	4.3135

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002984	1653947	MAG	United States	North America

• Gene Location: Start: 347; End: 3139 Strand: +

Full Sequence      

MKNNMFFRKCMSAFMALLFAAAMVFVPGKLPVSATAGPNLISNPGFEELTDGFPSDWTVW
NPNSDPEKYTYEYGEGLGRTGGGVHISHKENDGYVILQQENIPVTSNTDYLFEYWFKAEN
VIANGRIQVCIRQFTETGDADNSYLWTDTYNQWGNTNGFAKVSIPFTTSANAVKLRAEIY
VNVAGGGSGDWYFDDVSLHTPDPNPIRNSDFEEASGNVPAAWSFSNGEDENITWERDASG
GRNGSAAVHINRAVKSSKASYIYTPDIKVKPGTKYVLEYWFKSQNVTNLGNLTVMLKQKQ
SNGNDSLEKCYYYLDNYEQYGDTDWKKVTIPFTTASDAARVDLYFHFVGDSTGRYGSTGE
YWIDDVSIRTKAEYDADTEQYAGMTEVNVTPTVKGMPNGYYEAVRLNCALISENNVFADA
VNVFKNYVKSVHNMEISEGEGGIRLILDDSLASDTYKLICDENGLTVKASSTEGINYALS
TVLQIMKPNSAGGLDFPICDITDYPDSNFRGVMSGVDLTDVPGYVKIPISRMLDYIDLCY
LNKINYLHIDFNQYSLHALPSDVFPDLPTEGHYTKEEIATLTAYAKERGITIIPAINAPG
HSSEFLIKYPEVFGSYTEFDEAIGADIGIVDCSEEAFAGLKKVYEEVCEMFPDSPYIHLG
GDEAPTTLWHHSEKTKAYAAEHGFTDENGNIDIQALYTEFMRRTTDMILEMGRTPIVWEG
FPASGNDKISKDVIVMEWECAYNMPQDLINSGFEFVNVSWQPLYIAGTDGASWDYREILK
WNIYNWQHFYEASAAFGGMTIEPNDLVIGAEMPIWIYNSADDQTYTELAERLPALAQKTW
NIRGNFSFNEFAHSLELNSAMLKKMNAADRSEEPALQGDVNGDGAVDIKDLIRLKKITAG
ISPEVPAADMNLDSVVNAKDIALLKKTLMQ

Enzyme Prediction     

No EC number prediction in MGYG000002984_00499.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH20	528	841	2.5e-55	0.9109792284866469

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06563	GH20_chitobiase-like	1.83e-52	527	852	15	354	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	8.04e-45	527	840	15	343	Glycosyl hydrolase family 20, catalytic domain. This domain has a TIM barrel fold.
cd06564	GH20_DspB_LnbB-like	1.23e-36	510	840	3	324	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.
cd02742	GH20_hexosaminidase	2.21e-35	527	840	13	302	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.
cd06562	GH20_HexA_HexB-like	3.39e-33	527	815	15	297	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
SOE23912.1	9.23e-71	375	878	18	506
AUP78698.1	2.98e-66	366	856	16	490
QHI70394.1	1.12e-63	404	857	233	670
QHI70392.1	1.69e-61	436	877	86	523
CAZ95083.1	1.22e-53	437	865	89	511

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
7CBN_A	1.31e-37	433	815	57	455	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]
3RCN_A	5.40e-33	440	867	64	508	CrystalStructure of Beta-N-Acetylhexosaminidase from Arthrobacter aurescens [Paenarthrobacter aurescens TC1]
6JE8_A	4.92e-28	450	877	33	467	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]
6EZR_A	5.22e-28	416	856	166	624	Crystalstructure of GH20 Exo beta-N-Acetylglucosaminidase from Vibrio harveyi [Vibrio harveyi],6EZR_B Crystal structure of GH20 Exo beta-N-Acetylglucosaminidase from Vibrio harveyi [Vibrio harveyi],6EZS_A Crystal structure of GH20 Exo beta-N-Acetylglucosaminidase from Vibrio harveyi in complex with N-acetylglucosamine [Vibrio harveyi],6EZS_B Crystal structure of GH20 Exo beta-N-Acetylglucosaminidase from Vibrio harveyi in complex with N-acetylglucosamine [Vibrio harveyi],6K35_A Crystal structure of GH20 exo beta-N-acetylglucosaminidase from Vibrio harveyi in complex with NAG-thiazoline [Vibrio harveyi],6K35_B Crystal structure of GH20 exo beta-N-acetylglucosaminidase from Vibrio harveyi in complex with NAG-thiazoline [Vibrio harveyi]
6EZT_A	4.92e-27	416	856	163	621	Crystalstructure of GH20 Exo beta-N-Acetylglucosaminidase D437A inactive mutant from Vibrio harveyi [Vibrio harveyi],6EZT_B Crystal structure of GH20 Exo beta-N-Acetylglucosaminidase D437A inactive mutant from Vibrio harveyi [Vibrio harveyi]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
B2UQG6	8.31e-37	433	815	76	474	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
B2UP57	1.48e-27	450	881	54	492	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
P96155	1.11e-23	439	773	193	543	Beta-hexosaminidase OS=Vibrio furnissii OX=29494 GN=exoI PE=1 SV=1
P49008	6.19e-21	451	856	108	519	Beta-hexosaminidase OS=Porphyromonas gingivalis (strain ATCC BAA-308 / W83) OX=242619 GN=nahA PE=3 SV=2
P49614	2.02e-20	452	841	119	489	Beta-hexosaminidase subunit beta OS=Felis catus OX=9685 GN=HEXB PE=2 SV=2

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
0.000393	0.998902	0.000192	0.000197	0.000147	0.000133

TMHMM  Annotations     

start	end
13	35