CAZyme Information: MGYG000002894_00784

Basic Information

• Species: Winkia sp002849225
• Lineage: Bacteria; Actinobacteriota; Actinomycetia; Actinomycetales; Actinomycetaceae; Winkia; Winkia sp002849225
• CAZyme ID: MGYG000002894_00784
• CAZy Family: GH20
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
422	MGYG000002894_13|CGC1	47350.64	6.0939

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002894	2092236	MAG	United States	North America

• Gene Location: Start: 32390; End: 33658 Strand: +

Full Sequence      

MSDNPLNLEVPARQGGPEKGYLVRRVPADPTTPGSPQVGKHSFEVVARTDVQRLAGQVQV
ALEQAADQVVTVGVHEAPIGHRSLHLDAGRHYFSPSHIKQILHLMAWCRLNVLDLHISDT
HGYRVASALHPEIVSKHHLSKDEIEQIVAYAAELGIEVVPSFDMPGHLHKVLGPNQWAGL
RDDCGQLIPGALNILDPQAKELVWDLMDEVVQMFSATSFTVGADEFLEYGTRVDSLERQA
VAQFGPGAHGNDVWIDFANQCVQRLAEQGIAVNLFNDGVHVDAKVFPDKRANIFYWTRWG
AHMAPPQRFAELGYKLHNWDGESLYFILREEGNCKIPTFQSVWRDFDPYVFPDKAGAVRL
RPDGANFSVWCDQPETMTSDQIIAKLIDPLFAFGQLLWPLGRRRDEAQTRKLLSQLHTFQ
NQ

Enzyme Prediction     

No EC number prediction in MGYG000002894_00784.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH20	79	398	3.3e-55	0.9525222551928784

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06564	GH20_DspB_LnbB-like	1.77e-39	81	398	2	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.
pfam00728	Glyco_hydro_20	8.73e-36	80	398	2	343	Glycosyl hydrolase family 20, catalytic domain. This domain has a TIM barrel fold.
COG3525	Chb	2.40e-29	71	392	252	606	N-acetyl-beta-hexosaminidase [Carbohydrate transport and metabolism].
cd02742	GH20_hexosaminidase	3.81e-27	81	398	1	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	6.52e-27	80	225	2	159	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
QWW19992.1	1.00e-111	43	414	43	413
VEH83843.1	3.52e-64	74	398	74	405
AYV35170.1	4.95e-64	74	398	74	405
AWU40899.1	1.93e-63	74	398	74	405
QDE02058.1	1.93e-63	74	398	74	405

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4H04_A	1.81e-20	38	402	116	478	Lacto-N-biosidasefrom Bifidobacterium bifidum [Bifidobacterium bifidum JCM 1254],4H04_B Lacto-N-biosidase from Bifidobacterium bifidum [Bifidobacterium bifidum JCM 1254],4JAW_A Crystal Structure of Lacto-N-Biosidase from Bifidobacterium bifidum complexed with LNB-thiazoline [Bifidobacterium bifidum JCM 1254],4JAW_B Crystal Structure of Lacto-N-Biosidase from Bifidobacterium bifidum complexed with LNB-thiazoline [Bifidobacterium bifidum JCM 1254],5BXP_A LNBase in complex with LNB-LOGNAc [Bifidobacterium bifidum JCM 1254],5BXP_B LNBase in complex with LNB-LOGNAc [Bifidobacterium bifidum JCM 1254],5BXR_A LNBase in complex with LNB-NHAcDNJ [Bifidobacterium bifidum JCM 1254],5BXR_B LNBase in complex with LNB-NHAcDNJ [Bifidobacterium bifidum JCM 1254],5BXS_A LNBase in complex with LNB-NHAcCAS [Bifidobacterium bifidum JCM 1254],5BXS_B LNBase in complex with LNB-NHAcCAS [Bifidobacterium bifidum JCM 1254],5BXT_A LNBase in complex with LNB-NHAcAUS [Bifidobacterium bifidum JCM 1254],5BXT_B LNBase in complex with LNB-NHAcAUS [Bifidobacterium bifidum JCM 1254]
1YHT_A	2.61e-15	84	382	21	342	Crystalstructure analysis of Dispersin B [Aggregatibacter actinomycetemcomitans]
3RCN_A	5.05e-14	69	410	127	497	CrystalStructure of Beta-N-Acetylhexosaminidase from Arthrobacter aurescens [Paenarthrobacter aurescens TC1]
4AZ7_A	3.83e-13	86	387	12	354	Differentialinhibition of the tandem GH20 catalytic modules in the pneumococcal exo-beta-D-N-acetylglucosaminidase, StrH [Streptococcus pneumoniae TIGR4]
2YL6_A	3.84e-13	86	387	12	354	Inhibitionof the pneumococcal virulence factor StrH and molecular insights into N-glycan recognition and hydrolysis [Streptococcus pneumoniae TIGR4],4AZ5_A 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
Q9HGI3	7.33e-15	72	225	177	349	Beta-hexosaminidase OS=Emericella nidulans OX=162425 GN=nagA PE=1 SV=1
Q619W7	6.71e-14	1	229	68	326	Beta-hexosaminidase A OS=Caenorhabditis briggsae OX=6238 GN=hex-1 PE=3 SV=2
Q22492	2.12e-13	68	229	158	329	Beta-hexosaminidase A OS=Caenorhabditis elegans OX=6239 GN=hex-1 PE=1 SV=1
P43077	5.05e-13	81	228	168	327	Beta-hexosaminidase OS=Candida albicans OX=5476 GN=HEX1 PE=1 SV=1
P49610	3.10e-12	61	387	169	534	Beta-N-acetylhexosaminidase OS=Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4) OX=170187 GN=strH PE=1 SV=2

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
1.000032	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002894_00784.