CAZyme Information: ETI28026.1

Basic Information

• Species: Cladophialophora carrionii
• Lineage: Ascomycota; Eurotiomycetes; ; Herpotrichiellaceae; Cladophialophora; Cladophialophora carrionii
• CAZyme ID: ETI28026.1
• CAZy Family: GT20
• CAZyme Description: Beta-hexosaminidase [Source:UniProtKB/TrEMBL;Acc:V9DN01]

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
631		71153.61	6.2609

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_CcarrioniiCBS160.54	10428	1279043	55	10373

• Gene Location: location=KB822697:1305326-1307265(+)

Full Sequence      

MLPRTLLGVLSILVSPCLAIWPQPAEIKTGTRVLWLDTALQATLKCDNGEDRGHDQDYVL
YSNHLTQHLKGMSRYAQGFVDRLPFAFPGKSRNGEVDFSESSIVEDAVRDTIKSIHRSKF
VPWKLHKRNATFEPDRSAPRQYISRLKIQQRHCPPPERFRPSSFFGGDESYEILITNETA
FITSNSSIGTIRGLQSFQQLFFAHSALSGTYTPFVPVKIADRPEWRHRGLSIDIARNPFE
PQDLLRTIDGMAMAKMSRLHVHATDSQSWPIEIPSLPELAQKGAYHPGLVWTARSLREVQ
MYGASKGVSVYLEIDVPGHTASIAHAYPELIAAYNELDWSTFAAEPLSGQLKLNLSAVDT
FIYTLLDDILPRTRQYTSLYHVGGDEVNLAAYKLDETVKSDNPEVLQPLLQRLIDHVVGT
SIQFGLQPIVWEEMLLDWNLTLPSAGPNDPTTQTLVQVWRNSERIDEVLKRGHRAIFGDY
HHWYLDCGYGVFLDPYASGKSPPGVPYNTSGGFSSRLKKPYLDYCAPFHNWRHMYTYDPV
AGIARELQDSIEGGEVLMWSEQTDSQDLDSKLWPRVAAAAEVLWSGTRNESMLEAATSRL
GEWRERAVVDLGIRSSPVTMTWCLMEGGCNL

Enzyme Prediction     

EC	3.2.1.52:9

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH20	220	586	6.6e-75	0.973293768545994

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
119332	GH20_HexA_HexB-like	1.37e-130	225	608	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	8.31e-95	227	586	3	345	Glycosyl hydrolase family 20, catalytic domain. This domain has a TIM barrel fold.
119333	GH20_chitobiase-like	1.21e-49	224	586	2	344	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	1.23e-46	227	589	3	319	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	8.11e-46	228	585	4	297	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
QSS67367.1|GH20	7.13e-195	14	631	12	602
QSS57609.1|GH20	1.43e-194	14	631	12	602
QSS66188.1|GH20	2.87e-194	13	631	11	602
ABU87865.1|GH20	4.20e-194	19	631	19	603
CBX95932.1|GH20	3.70e-174	4	631	2	613

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3WMB_A	5.42e-56	168	629	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	6.04e-56	168	629	126	570	Crystal Structure of insect beta-N-acetyl-D-hexosaminidase OfHex1 complexed with a berberine derivative (SYSU-00679) [Ostrinia furnacalis]
3NSM_A	1.03e-55	168	629	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	1.09e-55	168	629	129	573	Crystal Structure of insect beta-N-acetyl-D-hexosaminidase OfHex1 V327G complexed with PUGNAc [Ostrinia furnacalis]
5Y0V_A	7.99e-55	168	629	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	5.71e-187	19	631	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	5.19e-80	166	630	113	571	Beta-hexosaminidase 2 OS=Arabidopsis thaliana OX=3702 GN=HEXO2 PE=1 SV=1
sp|P43077|HEX1_CANAX	6.33e-56	103	631	57	555	Beta-hexosaminidase OS=Candida albicans OX=5476 GN=HEX1 PE=1 SV=1
sp|P49010|HEXC_BOMMO	3.10e-55	168	628	150	592	Chitooligosaccharidolytic beta-N-acetylglucosaminidase OS=Bombyx mori OX=7091 PE=1 SV=1
sp|Q06GJ0|HEXC_OSTFU	7.87e-55	168	629	148	592	Chitooligosaccharidolytic beta-N-acetylglucosaminidase OS=Ostrinia furnacalis OX=93504 PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000219	0.999718	CS pos: 19-20. Pr: 0.9771

TMHMM  Annotations     

There is no transmembrane helices in ETI28026.1.