CAZyme Information: EXJ72626.1

Basic Information

• Species: Cladophialophora psammophila
• Lineage: Ascomycota; Eurotiomycetes; ; Herpotrichiellaceae; Cladophialophora; Cladophialophora psammophila
• CAZyme ID: EXJ72626.1
• CAZy Family: GH65
• CAZyme Description: Beta-hexosaminidase [Source:UniProtKB/TrEMBL;Acc:W9X6S4]

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
614	AMGX01000005|CGC7	69276.45	5.7779

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_CpsammophilaCBS110553	13421	1182543	0	13421

• Gene Location: location=AMGX01000005:336857-338875(-)

Full Sequence      

MLPQHLLILVSIAPCLAIWPQPAEIRTGHRVLWLDPALHATLRCEEKTIDVYGTANSQGS
HLAGVLNGAFGFTQGLMDKLQFAFVTRNSSDQPCFSERSIVQNAVREAIQSIQQSNFVPW
KLYKRHSTFEPDPHAARRYISTLHIQQKSCPASEPLSPESYFGGDESYLIDIDDDGITSI
KANGSIGTIRGLQTLEQLFFAHSTKSGSYTPFAPLRIADRARWRHRGLSIDIARNPFESQ
DLLRTIDAMAMAKLNRLHIHATDSQSWPLEIPSLPDLARKGAYQPHLVWSANNLREIQMH
GAAKGVSVFIEIDMPGHTASVTYAYPDLVAAFNELDWSTFAAEPLSGQLKLNSSDVHRFV
ATVLDDLLSRTSPYTSLYHVGGDELNRAAYLLDETVQSDDPGVLQPLLQKFIDSVIEASI
RHGMQPVVWEEMLLDWNLTLPSAMDSAPSRQTLVQVWRNSERIEEVLKRGHRAIFGDYHF
WYLDCKYLPYNTSGGYSSKLEKPYLDYCNPYHNWRQMYTYNPLANISADLQEGIEGGEVL
MWSEQTDSSDLDSKLWPRAAAAAEVLWAGVRQEAMLEDATRRLGEWRERGVMDLRMRMSP
VTMTWCLMEGGCNL

Enzyme Prediction     

EC	3.2.1.52:9

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH20	218	568	6.4e-78	0.9703264094955489

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
119332	GH20_HexA_HexB-like	7.04e-123	223	591	1	345	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	5.83e-92	225	569	3	345	Glycosyl hydrolase family 20, catalytic domain. This domain has a TIM barrel fold.
119333	GH20_chitobiase-like	6.88e-46	225	567	3	342	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	1.55e-40	225	583	3	329	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	2.45e-38	226	583	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	6.38e-189	17	614	19	603
QSS66188.1|GH20	4.79e-183	6	614	8	602
QSS67367.1|GH20	2.72e-182	1	614	1	602
QSS57609.1|GH20	1.09e-181	1	614	1	602
CBX95932.1|GH20	2.34e-162	17	614	17	613

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3WMB_A	2.25e-59	116	612	63	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	2.52e-59	116	612	63	570	Crystal Structure of insect beta-N-acetyl-D-hexosaminidase OfHex1 complexed with a berberine derivative (SYSU-00679) [Ostrinia furnacalis]
3NSM_A	8.28e-59	116	612	63	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	8.77e-59	116	612	66	573	Crystal Structure of insect beta-N-acetyl-D-hexosaminidase OfHex1 V327G complexed with PUGNAc [Ostrinia furnacalis]
5Y0V_A	3.42e-58	116	612	63	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	5.35e-183	17	614	18	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	2.92e-76	161	613	111	571	Beta-hexosaminidase 2 OS=Arabidopsis thaliana OX=3702 GN=HEXO2 PE=1 SV=1
sp|P43077|HEX1_CANAX	1.85e-59	141	614	93	555	Beta-hexosaminidase OS=Candida albicans OX=5476 GN=HEX1 PE=1 SV=1
sp|Q06GJ0|HEXC_OSTFU	6.44e-58	116	612	85	592	Chitooligosaccharidolytic beta-N-acetylglucosaminidase OS=Ostrinia furnacalis OX=93504 PE=1 SV=1
sp|Q8WSF3|FDL_DROME	9.92e-57	124	611	170	657	Probable beta-hexosaminidase fdl OS=Drosophila melanogaster OX=7227 GN=fdl PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000270	0.999702	CS pos: 17-18. Pr: 0.9764

TMHMM  Annotations     

There is no transmembrane helices in EXJ72626.1.