CAZyme Information: ASPNIDRAFT2_1159353-t41_1-p1

Basic Information

• Species: Aspergillus niger
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus niger
• CAZyme ID: ASPNIDRAFT2_1159353-t41_1-p1
• CAZy Family: GH31
• CAZyme Description: Glycoside Hydrolase Family 20 protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
512	ACJE01000015.1|CGC9	57087.05	4.5239

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AnigerATCC1015	11910	380704	6	11904

• Gene Location: location=ACJE01000015.1:631138-632942(-)

Full Sequence      

MLLPRLWLACLTLLVAGVAAVKFNPLPAPRNINWASSGPKQLAGFVSLRASQNTSDFILA
NGWDRAWDSIVSLQWVPAATEGPVPSFQPFPTGTAGVARRSSQALPSLQFVDHGVDESYT
LEVTESATSVVIEAPTVWGALHAFTTLQQLVISDGQGGLLIEQPVKIQDAPLYPYRGIML
DSGRNFISVNKIYEQLDGIWRPAWTPGGPNDYALHTAVEPPPGQMDIIYNGTYDVVRPVY
NELSNIFPDNWSHVGADEIQPNCFNFSSYVTDWFAQDPSRTYNDLAQYWVDHAVPIFQNH
SASRRLVMWEDIVLSTEHAYDVPTNIVMQTWNSGLDYINQLTAKGYDVIVSSADFMYLDC
GMGGFLTNDPRYDVMSNPDASTANFNYGGNGGSWCAPYKTWQRIYDYDFTQNLTVTQAQH
IVGAEAPLWSEQVDDVTVSSQFWPRAAALAELVWSGNRDENGRKRTTLMTQRILNFREYL
VANGVQAQALVPKYCVQRPHTCDLYLNQSAIQ

Enzyme Prediction     

EC	3.2.1.52:13

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH20	215	456	6.1e-44	0.6231454005934718

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
119332	GH20_HexA_HexB-like	1.07e-82	173	484	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	2.71e-68	173	456	1	345	Glycosyl hydrolase family 20, catalytic domain. This domain has a TIM barrel fold.
373334	Glycohydro_20b2	1.51e-32	25	150	1	133	beta-acetyl hexosaminidase like.
119333	GH20_chitobiase-like	8.40e-28	173	465	1	356	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	1.57e-19	173	465	1	328	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CAK40161.1|GH20	0.0	1	512	1	604
BCS10909.1|GH20	0.0	1	512	1	601
BCR98575.1|GH20	0.0	1	512	1	601
CAK44595.1|GH20	0.0	1	512	1	584
BCR98607.1|GH20	0.0	1	512	1	602

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5OAR_B	1.22e-229	111	512	19	499	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]
3NSM_A	6.46e-45	115	502	125	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	1.75e-44	115	502	128	573	Crystal Structure of insect beta-N-acetyl-D-hexosaminidase OfHex1 V327G complexed with PUGNAc [Ostrinia furnacalis]
3WMB_A	2.32e-44	115	502	125	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	2.51e-44	115	502	125	570	Crystal Structure of insect beta-N-acetyl-D-hexosaminidase OfHex1 complexed with a berberine derivative (SYSU-00679) [Ostrinia furnacalis]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q8J2T0|HEXA_ASPOZ	1.16e-270	15	512	13	600	Beta-hexosaminidase OS=Aspergillus oryzae OX=5062 GN=nagA PE=1 SV=1
sp|Q9HGI3|HEXA_EMEND	2.34e-242	9	511	8	602	Beta-hexosaminidase OS=Emericella nidulans OX=162425 GN=nagA PE=1 SV=1
sp|E9DFH0|HEX1_COCPS	1.59e-196	14	511	13	594	Beta-hexosaminidase 1 OS=Coccidioides posadasii (strain RMSCC 757 / Silveira) OX=443226 GN=HEX1 PE=1 SV=1
sp|D4AYT4|HEX2_ARTBC	4.82e-175	17	511	29	614	Probable beta-hexosaminidase ARB_01353 OS=Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) OX=663331 GN=ARB_01353 PE=1 SV=1
sp|P43077|HEX1_CANAX	2.82e-118	18	507	20	558	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
0.000249	0.999713	CS pos: 20-21. Pr: 0.9756

TMHMM  Annotations     

There is no transmembrane helices in ASPNIDRAFT2_1159353-t41_1-p1.