CAZyme Information: EGD98482.1

Basic Information

• Species: Trichophyton tonsurans
• Lineage: Ascomycota; Eurotiomycetes; ; Arthrodermataceae; Trichophyton; Trichophyton tonsurans
• CAZyme ID: EGD98482.1
• CAZy Family: GT15
• CAZyme Description: chitobiase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
548	GG698511|CGC3	62021.38	6.1082

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_TtonsuransCBS112818	8625	647933	104	8521

• Gene Location: location=GG698511:176630-178447(+)

Full Sequence      

MWWIWVAGILGLFGRHPWGSAEQPVAEPLPNVEQFVEDAIKRTKDAILNSKFVPWKFYPR
HQKFEPLVDGQHPTIEKVIINETSKTSEERSPRNYVNGDEKYEIRISEDGEVQISSRSPI
GTIRALQTFQQLFYSHSHSKSYTPFAPVSISDSPKWRHRGLNLDISRNVIRPEEAKRTID
AMASVKLNRLHVHAADSQSWPLDIPSIPELAAKASYHPSQVWSSSELEAVQLYGLERGVS
VFLEIDLPGHTAAVGHAFPDLVVAYHMDQWETYAAEPPSGQIKLNSSAVYQFLDRLMADL
IPRVSPLTEYFHTGGDEFNLNTYLLELNLGSNDRRVLTPFLKKMITHVHSSLRGSGVTPI
VWEELVLDWDLNLPSHKAEGETGGVIVQAWRNSSAVKHVLQKGYQTIFGTGDAWYLDCGV
GTFLNPRPGSKAVQDPYLDWCAPTKNWKHMYIYNPLKDIPVELQSLLVGGETHMWSELVD
PVNMDQMIWPRTAAAAEVLWTGPRSPDNIQDASYRLAEWRERVVIDAGIRAAMVQMTYCL
MRESGCEL

Enzyme Prediction     

EC	3.2.1.52:9

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH20	151	502	8.6e-77	0.973293768545994

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
119332	GH20_HexA_HexB-like	2.94e-133	156	525	1	346	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	1.60e-87	158	502	3	345	Glycosyl hydrolase family 20, catalytic domain. This domain has a TIM barrel fold.
119333	GH20_chitobiase-like	1.43e-45	158	503	3	345	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.
119336	GH20_SpHex_like	1.11e-44	158	507	3	321	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.
119338	GH20_chitobiase-like_1	1.13e-43	159	516	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ABU87865.1|GH20	6.63e-261	30	548	84	603
QSS57609.1|GH20	2.31e-256	13	548	68	602
QSS67367.1|GH20	2.31e-256	13	548	68	602
QSS66188.1|GH20	4.64e-256	13	548	68	602
AAL14649.1|GH20	5.01e-213	13	484	69	539

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3WMB_A	1.43e-65	99	546	126	570	Crystal structure of insect beta-N-acetyl-D-hexosaminidase OfHex1 complexed with naphthalimide derivative Q1 [Ostrinia furnacalis],3WMC_A Crystal structure of insect beta-N-acetyl-D-hexosaminidase OfHex1 complexed with naphthalimide derivative Q2 [Ostrinia furnacalis]
5Y1B_A	1.62e-65	99	546	126	570	Crystal Structure of insect beta-N-acetyl-D-hexosaminidase OfHex1 complexed with a berberine derivative (SYSU-00679) [Ostrinia furnacalis]
3NSM_A	2.79e-65	99	546	126	570	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	2.97e-65	99	546	129	573	Crystal Structure of insect beta-N-acetyl-D-hexosaminidase OfHex1 V327G complexed with PUGNAc [Ostrinia furnacalis]
5Y0V_A	2.31e-64	99	546	126	570	Crystal Structure of insect beta-N-acetyl-D-hexosaminidase OfHex1 complexed with berberine [Ostrinia furnacalis]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|D4AUH6|HEX1_ARTBC	0.0	15	548	72	605	Beta-hexosaminidase ARB_07893 OS=Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) OX=663331 GN=ARB_07893 PE=1 SV=1
sp|Q9SYK0|HEXO2_ARATH	3.60e-72	60	547	76	571	Beta-hexosaminidase 2 OS=Arabidopsis thaliana OX=3702 GN=HEXO2 PE=1 SV=1
sp|Q06GJ0|HEXC_OSTFU	2.25e-64	99	546	148	592	Chitooligosaccharidolytic beta-N-acetylglucosaminidase OS=Ostrinia furnacalis OX=93504 PE=1 SV=1
sp|Q8WSF3|FDL_DROME	2.90e-64	96	546	213	659	Probable beta-hexosaminidase fdl OS=Drosophila melanogaster OX=7227 GN=fdl PE=1 SV=1
sp|P43077|HEX1_CANAX	8.68e-63	36	548	58	555	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	CS Position
0.000275	0.999719	CS pos: 21-22. Pr: 0.9494

TMHMM  Annotations     

There is no transmembrane helices in EGD98482.1.