CAZyme Information: MGYG000003317_01250

Basic Information

• Species: Lentilactobacillus buchneri
• Lineage: Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; Lentilactobacillus; Lentilactobacillus buchneri
• CAZyme ID: MGYG000003317_01250
• CAZy Family: GH20
• CAZyme Description: Beta-N-acetylhexosaminidase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
381	MGYG000003317_96|CGC1	43312.93	9.6785

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003317	2478253	MAG	Russia	Europe

• Gene Location: Start: 23339; End: 24484 Strand: -

Full Sequence      

MVHKSWLLLPLTVLLMGCSAHKTTTAQTTSSTASEQDGRHNGVTLDVARRHYQVGTLQKF
IQLVGDHNGRFIQLHLSDDRNFAIENDYVGQSLKNAQKVDGVWHNKKTHQFFYSKAEIKY
LVNDAEQHHVTLIPEIDTPAHVTALVKLMKANGKAQLADQVSWYSKSYRDEIHLNQTGID
FTKKLDDEVGALFAGQANPRFHLGGDEFSDKLTSNAAYVKYLNATSANVEKMGFTPEAWN
DGFLNSSLSKLNKNIQVTYWNWTADQTGKLAAQRQKYWASMPKLINRGFKVFNYNDYYLY
FNLSKTNMSKKNVTYMIKDMKQYWKPTLWHNDVDTKLKSKRGIVGSSVSLWADSAGSVND
QQVYAASEQFIKTFLALAESR

Enzyme Prediction     

No EC number prediction in MGYG000003317_01250.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH20	40	379	3.6e-45	0.9376854599406528

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06564	GH20_DspB_LnbB-like	7.60e-57	40	374	2	319	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	3.07e-41	40	357	1	282	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.
pfam00728	Glyco_hydro_20	1.03e-24	40	352	3	318	Glycosyl hydrolase family 20, catalytic domain. This domain has a TIM barrel fold.
cd06568	GH20_SpHex_like	6.78e-18	40	276	3	227	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.
cd06569	GH20_Sm-chitobiase-like	2.09e-17	40	351	7	389	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. 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
AFR99311.1	4.31e-279	1	381	1	381
QUX06558.1	4.31e-279	1	381	1	381
APR07016.1	1.36e-215	1	381	1	379
QOP51663.1	7.29e-211	9	381	1	370
QOJ86140.1	7.29e-211	9	381	1	370

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1YHT_A	2.23e-56	39	375	17	354	Crystalstructure analysis of Dispersin B [Aggregatibacter actinomycetemcomitans]
6EZR_A	1.30e-13	39	253	264	479	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]
7PUL_A	6.59e-13	45	314	15	303	ChainA, Beta-N-acetylhexosaminidase [Enterococcus faecalis]
6EZT_A	1.29e-12	39	253	261	476	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]
4AZI_A	1.67e-12	35	353	5	331	Differentialinhibition of the tandem GH20 catalytic modules in the pneumococcal exo-beta-D-N-acetylglucosaminidase, StrH [Streptococcus pneumoniae TIGR4],4AZI_B Differential inhibition of the tandem GH20 catalytic modules in the pneumococcal exo-beta-D-N-acetylglucosaminidase, StrH [Streptococcus pneumoniae TIGR4]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
B2UPR7	1.02e-11	42	300	236	490	Beta-hexosaminidase Amuc_2136 OS=Akkermansia muciniphila (strain ATCC BAA-835 / DSM 22959 / JCM 33894 / BCRC 81048 / CCUG 64013 / CIP 107961 / Muc) OX=349741 GN=Amuc_2136 PE=1 SV=1
P49610	5.02e-11	30	354	177	520	Beta-N-acetylhexosaminidase OS=Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4) OX=170187 GN=strH PE=1 SV=2
Q86M34	7.85e-08	42	261	191	418	Beta-hexosaminidase subunit beta OS=Entamoeba histolytica OX=5759 GN=HEXB PE=1 SV=1
P49010	5.83e-07	40	240	213	403	Chitooligosaccharidolytic beta-N-acetylglucosaminidase OS=Bombyx mori OX=7091 PE=1 SV=1
P43077	3.08e-06	39	261	167	389	Beta-hexosaminidase OS=Candida albicans OX=5476 GN=HEX1 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
0.000000	0.000000	1.000057	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000003317_01250.