CAZyme Information: MGYG000002898_00512

Basic Information

• Species: Haemophilus_D pittmaniae
• Lineage: Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Pasteurellaceae; Haemophilus_D; Haemophilus_D pittmaniae
• CAZyme ID: MGYG000002898_00512
• CAZy Family: GH20
• CAZyme Description: Beta-N-acetylhexosaminidase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
381	MGYG000002898_3|CGC1	42929.67	5.7065

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002898	2077686	MAG	United States	North America

• Gene Location: Start: 14918; End: 16063 Strand: +

Full Sequence      

MKKSFLLLLGALISFNGRAEISSPIENSQAVVQTHPKESGLMLDIARHFYPPEVIKSFID
TLSEAGGTFLHLHFSDDENYALESELLNQRVDGAIQKNGIYINPLTQKPFLSYQQIKDIK
DYAKLKGIEIIPELDSPAHMRGIFRLLQNAKGKDYVQSVASPQVSDEINMTNPQSIAFIQ
DLLDEVINVFANSSRHIHIGGDEFGYDINNNEEFIGYANTLTEFLRQKGLKARMWNDGLI
KKNLDKLDPSIEITYWSFDGDKQDQQEVKRLRSARAALPDLLTKGFKVLNYNSYYLYLTP
ESATAFPKDAEFAKNDLLKNWDLGVWDGENKQNKVANSENLIGAALSIWGENAKALKSEN
IQKDSKPLLKAVIQKTNLASQ

Enzyme Prediction     

EC	3.2.1.-

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH20	40	357	1.4e-58	0.887240356083086

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd02742	GH20_hexosaminidase	3.12e-93	40	377	3	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.
cd06564	GH20_DspB_LnbB-like	7.39e-92	37	377	1	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	2.14e-38	40	351	5	319	Glycosyl hydrolase family 20, catalytic domain. This domain has a TIM barrel fold.
cd06563	GH20_chitobiase-like	6.62e-37	40	351	5	318	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.
cd06562	GH20_HexA_HexB-like	3.93e-30	40	351	5	299	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
SNV82802.1	2.14e-279	1	381	1	381
AKU64311.1	6.36e-173	27	377	9	360
SQI99528.1	1.66e-172	6	377	14	387
VEF41785.1	1.66e-172	1	377	4	387
AKS64193.1	1.18e-167	42	377	1	337

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1YHT_A	3.40e-165	27	377	7	358	Crystalstructure analysis of Dispersin B [Aggregatibacter actinomycetemcomitans]
4AZ7_A	1.62e-21	37	303	6	296	Differentialinhibition of the tandem GH20 catalytic modules in the pneumococcal exo-beta-D-N-acetylglucosaminidase, StrH [Streptococcus pneumoniae TIGR4]
4AZB_A	1.64e-21	37	303	6	296	Differentialinhibition of the tandem GH20 catalytic modules in the pneumococcal exo-beta-D-N-acetylglucosaminidase, StrH [Streptococcus pneumoniae TIGR4]
2YL6_A	1.64e-21	37	303	6	296	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]
4AZ6_A	1.65e-21	37	303	8	298	Differentialinhibition 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
P49610	1.04e-20	26	303	175	476	Beta-N-acetylhexosaminidase OS=Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4) OX=170187 GN=strH PE=1 SV=2
P13723	4.02e-18	21	351	134	445	Beta-hexosaminidase subunit A1 OS=Dictyostelium discoideum OX=44689 GN=hexa1 PE=1 SV=1
Q54SC9	5.50e-18	40	356	167	458	Beta-hexosaminidase subunit A2 OS=Dictyostelium discoideum OX=44689 GN=hexa2 PE=3 SV=1
P96155	8.83e-16	37	203	261	435	Beta-hexosaminidase OS=Vibrio furnissii OX=29494 GN=exoI PE=1 SV=1
P43077	1.13e-14	37	351	167	482	Beta-hexosaminidase OS=Candida albicans OX=5476 GN=HEX1 PE=1 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
0.000429	0.998506	0.000539	0.000196	0.000178	0.000157

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002898_00512.