CAZyme Information: CDH58006.1

Basic Information

• Species: Lichtheimia corymbifera
• Lineage: Mucoromycota; Mucoromycetes; ; Lichtheimiaceae; Lichtheimia; Lichtheimia corymbifera
• CAZyme ID: CDH58006.1
• CAZy Family: GT22
• CAZyme Description: beta-hexosaminidase subunit beta

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
616	CBTN010000051|CGC2	70315.98	4.7475

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_LcorymbiferaJMRCFSU9682	12379	1263082	97	12282

• Gene Location: location=CBTN010000051:220718-223209(-)

Full Sequence      

MKISRAALVATTLFPSISWALQGAFLWPIPQFIDSGDTDVVLNITSFKFNAPDIPVLKDA
INRYTDLVRSEQWMPVQVPKQPMIRTTMATSHLSQLDIIVDNPSAELDHGVDESYTLDIQ
EFEGRLRAATVWGALRGLETFSQLVKARPPKEAPILDYSEDDATNTTMQLYIPETPIHIE
DAPVYSHRGLMLDTSRNYFPVSDILRTIDGMAYNKMNVFHWHITDSQSFPLRLDGVPELA
QQAAYVLNNRRLVYSKKDVKRVVEYARSRGIRVIPEIDMPAHTGSWANSHPDLITCNGKF
FLDPSNEWSERLAAEPTTGQLNPVLEETYHLVEKVISEVASLFPDNWYHGGGDEPIYKCW
EQDHRVQEYMSKYNATGDQLLHMFLNKEVQFIQNSGKKAILWEDSVTDNQLPISKDVVLQ
VWNKPVQEAAKKGYKVIASHANFWYLDCGHGGWTGNDDSYDEQEQPKVPESLAEELDRHQ
LTDNYRPSNWGGSGGDWCSPFKTWQRIYSYDMAYNLTKQEADNVLGGEVALWAEQTDSTA
LDVRLWPRTAAAAEVLWSGRYNTENEKRDLSDAMSRMFDWRYRLVQRGIQAEALQPLWCG
KNPSMCDSTFPEDLEK

Enzyme Prediction     

EC	3.2.1.52:9

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH20	179	559	4.2e-99	0.9762611275964391

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
119332	GH20_HexA_HexB-like	3.65e-163	185	588	1	348	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.
395590	Glyco_hydro_20	6.24e-130	185	559	1	345	Glycosyl hydrolase family 20, catalytic domain. This domain has a TIM barrel fold.
119333	GH20_chitobiase-like	2.38e-81	185	577	1	357	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.
119338	GH20_chitobiase-like_1	3.46e-77	188	577	4	311	A functionally uncharacterized subgroup of the Glycosyl hydrolase family 20 (GH20) catalytic domain found in proteins similar to the chitobiase of Serratia marcescens, a beta-N-1,4-acetylhexosaminidase 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 subgroup 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.
119331	GH20_hexosaminidase	9.03e-68	187	558	1	303	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CDS09580.1|GH20	0.0	1	616	1	616
CDS07988.1|GH20	3.18e-298	18	612	18	625
AKU79211.1|GH20	4.35e-298	8	614	7	638
BBN00792.1|GH20	4.18e-173	20	610	89	663
CAB4091242.1|GH20	9.73e-166	3	610	9	574

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5OAR_B	1.93e-122	89	607	1	490	Crystal structure of native beta-N-acetylhexosaminidase isolated from Aspergillus oryzae [Aspergillus oryzae],5OAR_D Crystal structure of native beta-N-acetylhexosaminidase isolated from Aspergillus oryzae [Aspergillus oryzae]
2GJX_A	4.93e-89	26	599	1	500	Crystallographic structure of human beta-Hexosaminidase A [Homo sapiens],2GJX_D Crystallographic structure of human beta-Hexosaminidase A [Homo sapiens],2GJX_E Crystallographic structure of human beta-Hexosaminidase A [Homo sapiens],2GJX_H Crystallographic structure of human beta-Hexosaminidase A [Homo sapiens]
5BRO_A	1.35e-86	15	600	4	507	Crystal structure of modified HexB (modB) [Homo sapiens]
3NSM_A	1.59e-86	26	608	43	572	Crystal Structure of insect beta-N-acetyl-D-hexosaminidase OfHex1 from Ostrinia furnacalis [Ostrinia furnacalis],3NSN_A Crystal Structure of insect beta-N-acetyl-D-hexosaminidase OfHex1 complexed with TMG-chitotriomycin [Ostrinia furnacalis],3OZO_A Crystal Structure of insect beta-N-acetyl-D-hexosaminidase OfHex1 complexed with NGT [Ostrinia furnacalis],3OZP_A Crystal Structure of insect beta-N-acetyl-D-hexosaminidase OfHex1 complexed with PUGNAc [Ostrinia furnacalis]
3S6T_A	1.72e-86	26	608	46	575	Crystal Structure of insect beta-N-acetyl-D-hexosaminidase OfHex1 V327G complexed with PUGNAc [Ostrinia furnacalis]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q9SYK0|HEXO2_ARATH	4.61e-162	11	608	19	572	Beta-hexosaminidase 2 OS=Arabidopsis thaliana OX=3702 GN=HEXO2 PE=1 SV=1
sp|E9DFH0|HEX1_COCPS	1.92e-126	1	614	1	593	Beta-hexosaminidase 1 OS=Coccidioides posadasii (strain RMSCC 757 / Silveira) OX=443226 GN=HEX1 PE=1 SV=1
sp|Q8J2T0|HEXA_ASPOZ	1.33e-121	1	607	1	591	Beta-hexosaminidase OS=Aspergillus oryzae OX=5062 GN=nagA PE=1 SV=1
sp|Q9HGI3|HEXA_EMEND	1.45e-121	53	614	53	601	Beta-hexosaminidase OS=Emericella nidulans OX=162425 GN=nagA PE=1 SV=1
sp|D4AYT4|HEX2_ARTBC	5.46e-111	48	607	60	606	Probable beta-hexosaminidase ARB_01353 OS=Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) OX=663331 GN=ARB_01353 PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000651	0.999315	CS pos: 20-21. Pr: 0.9675

TMHMM  Annotations     

Start	End
7	29