CAZyme Information: MGYG000001333.1_01746

Basic Information

• Species: Lentilactobacillus hilgardii
• Lineage: Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; Lentilactobacillus; Lentilactobacillus hilgardii
• CAZyme ID: MGYG000001333.1_01746
• CAZy Family: GH20
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
378	MGYG000001333.1_106|CGC3	43105.04	10.2191

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001333.1	3077266	Isolate	not provided	not provided

• Gene Location: Start: 152734; End: 153870 Strand: -

Full Sequence      

MHKRWLLLMPLVILLMGCSLTTKTTQKSTQSQYGRFNGVTLDVSRHHYRVATLVKFIKLV
STNHGQFIQLHLSDDKDFAIENQVVGQTRDRAVEQGGIWRNKKTHQAFYSRQQIHFLVNN
AKKYNVTLIPEIDTPAHVTGLVNTLKAAGQSKLVKALSWHSDSYGDELHLSKASIKFVEK
VDTEVAADFAGQKDARFHLGGDEFTDKLTKNSAYINYLNATSATIQKLGFIPEAWNDGFL
NSSLTALNHHIQVTYWNWTADQYGKLGAARRKAWSSMPNLIRHHFKVFNYNDYYLYFNIS
KKNLSKSNVSYMSSDMKRYWKPTLWHNDDATHLKSLKGIVGSSVSFWADSAGNVSDQQIY
QAGKSFIKNFLVLTRKSL

Enzyme Prediction     

No EC number prediction in MGYG000001333.1_01746.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH20	35	355	4.5e-40	0.8961424332344213

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06564	GH20_DspB_LnbB-like	1.92e-40	37	370	3	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	1.89e-35	38	353	3	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.
COG3525	Chb	2.55e-19	38	261	265	515	N-acetyl-beta-hexosaminidase [Carbohydrate transport and metabolism].
pfam00728	Glyco_hydro_20	4.43e-19	38	270	5	253	Glycosyl hydrolase family 20, catalytic domain. This domain has a TIM barrel fold.
cd06563	GH20_chitobiase-like	1.64e-18	38	203	5	175	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QIR10640.1	1.39e-278	1	378	1	378
QHB53470.1	9.43e-275	9	378	1	370
QEU39826.1	5.23e-272	9	378	1	370
APR07016.1	1.80e-182	2	373	3	375
AMV63908.1	1.32e-179	36	377	17	358

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1YHT_A	7.59e-52	23	368	13	351	Crystalstructure analysis of Dispersin B [Aggregatibacter actinomycetemcomitans]
7PUL_A	2.97e-07	41	256	15	247	ChainA, Beta-N-acetylhexosaminidase [Enterococcus faecalis]
1HP4_A	6.98e-07	41	236	164	351	ChainA, Beta-n-acetylhexosaminidase [Streptomyces plicatus],1HP5_A Chain A, Beta-n-acetylhexosaminidase [Streptomyces plicatus],1JAK_A Chain A, Beta-N-acetylhexosaminidase [Streptomyces plicatus],1M01_A Chain A, Beta-N-acetylhexosaminidase [Streptomyces plicatus],5FCZ_A Chain A, B-N-acetylhexosaminidase [Streptomyces plicatus],5FD0_A Chain A, B-N-acetylhexosaminidase [Streptomyces plicatus]
1QBA_A	1.50e-06	36	203	313	513	BACTERIALCHITOBIASE, GLYCOSYL HYDROLASE FAMILY 20 [Serratia marcescens],1QBB_A BACTERIAL CHITOBIASE COMPLEXED WITH CHITOBIOSE (DINAG) [Serratia marcescens]
1M04_A	2.86e-06	41	236	164	351	ChainA, Beta-N-acetylhexosaminidase [Streptomyces plicatus]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q54468	8.26e-06	36	203	340	540	Chitobiase OS=Serratia marcescens OX=615 GN=chb 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	1.000034	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001333.1_01746.