CAZyme Information: AKAW_09893-t41_1-p1

Basic Information

• Species: Aspergillus luchuensis
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus luchuensis
• CAZyme ID: AKAW_09893-t41_1-p1
• CAZy Family: GT2
• CAZyme Description: beta-hexosaminidase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
709	DF126484|CGC2	78704.10	5.8344

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AluchuensisIFO4308	11755	1033177	267	11488

• Gene Location: location=DF126484:87642-89865(+)

Full Sequence      

MRWRALGTVGLILDFTICGFSRLVTVPTIPFADNNSTYALSQLTKIVVDARHASTVDTQG
QTLIPPTLKEFAATFQEDLRSSLGIDLPLVTSNTSSDHAIFLTLSNNTDFRDVAGRFTAE
AYALLIDNHGIAISGASPLGVWWGTRSLIQAAVVSKHNLPQGSAIDAPGWGTRGVMLDAG
RHYYPPDFLIEMCSYLSFFKQNVFHLHLSDNLYNNVDLYSTQESLDLYAAFRPWSDDPAL
SGLNKRANESYTRSQFDHIQRQCARRGVTIIPEIEAPGHALAIVQWRPELGLTDLSMLNI
SHPDTIPTMKTIWKIFLPWFHSKTVHLGADEYSSSYVSDYTDFVNDMHTYIAEQSNKNTR
IWGTFTPSQGANVSKAVTIQHWEFYEDNPYFDYIKNNYSVLNSDDAFYIVGKWSGSYPQF
LNKTRVFHGDPANNGPYAPNIFSTTNATDNPPRDNPYVLGHIAALWNDYGPNATTYLEAY
YSWRDVLPALADKQWGGDILEDEYDDVFDTLHAVIPGQNLDRHVPSKTDLILHYNFANIT
GTTVPDLSGNNYHATCNHSCPINTSNSTIRFTETCTLTTPIQSKGRDYTLSFSVYPSTSH
PSPLFSGRDSTLLNGNGSISNITLVSGGNPYTLNYSLPVGKWSDVSLIGKGNKTFLSVDG
GKKMEFLARLGVNGEYSVWAPIAIEAPVQRIGEGFVGMMGEVKLWGSAK

Enzyme Prediction     

No EC number prediction in AKAW_09893-t41_1-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH20	166	496	2.7e-55	0.9673590504451038

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
119334	GH20_DspB_LnbB-like	1.66e-113	172	497	2	326	Glycosyl hydrolase family 20 (GH20) catalytic domain of dispersin B (DspB), lacto-N-biosidase (LnbB) and related proteins. Dispersin B is a soluble beta-N-acetylglucosamidase found in bacteria that hydrolyzes the beta-1,6-linkages of PGA (poly-beta-(1,6)-N-acetylglucosamine), a major component of the extracellular polysaccharide matrix. Lacto-N-biosidase hydrolyzes lacto-N-biose (LNB) type I oligosaccharides at the nonreducing terminus to produce lacto-N-biose as part of the GNB/LNB (galacto-N-biose/lacto-N-biose I) degradation pathway. The lacto-N-biosidase from Bifidobacterium bifidum has this GH20 domain, a carbohydrate binding module 32, and a bacterial immunoglobulin-like domain 2, as well as a YSIRK signal peptide and a G5 membrane anchor at the N and C termini, respectively. 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	1.95e-34	173	496	2	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.
395590	Glyco_hydro_20	3.38e-29	173	495	4	343	Glycosyl hydrolase family 20, catalytic domain. This domain has a TIM barrel fold.
226056	Chb	7.07e-22	118	589	204	703	N-acetyl-beta-hexosaminidase [Carbohydrate transport and metabolism].
119332	GH20_HexA_HexB-like	1.39e-21	173	333	4	161	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
BCR95441.1|GH20	0.0	1	709	1	709
CAK43562.1|GH20	0.0	1	709	1	709
UDD59134.1|GH20	0.0	1	708	1	707
QMW41071.1|GH20	0.0	1	708	1	707
QRD85258.1|GH20	0.0	1	708	1	707

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6JQF_A	2.46e-36	69	496	118	547	Crystallization analysis of a beta-N-acetylhexosaminidase (Am2136) from Akkermansia muciniphila [Akkermansia muciniphila ATCC BAA-835]
4H04_A	1.59e-21	21	430	32	419	Lacto-N-biosidase from Bifidobacterium bifidum [Bifidobacterium bifidum JCM 1254],4H04_B Lacto-N-biosidase from Bifidobacterium bifidum [Bifidobacterium bifidum JCM 1254],4JAW_A Crystal Structure of Lacto-N-Biosidase from Bifidobacterium bifidum complexed with LNB-thiazoline [Bifidobacterium bifidum JCM 1254],4JAW_B Crystal Structure of Lacto-N-Biosidase from Bifidobacterium bifidum complexed with LNB-thiazoline [Bifidobacterium bifidum JCM 1254],5BXP_A LNBase in complex with LNB-LOGNAc [Bifidobacterium bifidum JCM 1254],5BXP_B LNBase in complex with LNB-LOGNAc [Bifidobacterium bifidum JCM 1254],5BXR_A LNBase in complex with LNB-NHAcDNJ [Bifidobacterium bifidum JCM 1254],5BXR_B LNBase in complex with LNB-NHAcDNJ [Bifidobacterium bifidum JCM 1254],5BXS_A LNBase in complex with LNB-NHAcCAS [Bifidobacterium bifidum JCM 1254],5BXS_B LNBase in complex with LNB-NHAcCAS [Bifidobacterium bifidum JCM 1254],5BXT_A LNBase in complex with LNB-NHAcAUS [Bifidobacterium bifidum JCM 1254],5BXT_B LNBase in complex with LNB-NHAcAUS [Bifidobacterium bifidum JCM 1254]
3GH4_A	1.66e-19	79	431	87	447	Crystal structure of beta-hexosaminidase from Paenibacillus sp. TS12 [Paenibacillus sp.],3GH5_A Crystal structure of beta-hexosaminidase from Paenibacillus sp. TS12 in complex with GlcNAc [Paenibacillus sp.],3GH7_A Crystal structure of beta-hexosaminidase from Paenibacillus sp. TS12 in complex with GalNAc [Paenibacillus sp.],3SUR_A Crystal structure of beta-hexosaminidase from Paenibacillus sp. TS12 in complex with NAG-thiazoline. [Paenibacillus sp. TS12],3SUS_A Crystal structure of beta-hexosaminidase from Paenibacillus sp. TS12 in complex with Gal-NAG-thiazoline [Paenibacillus sp. TS12],3SUT_A Crystal structure of beta-hexosaminidase from Paenibacillus sp. TS12 in complex with PUGNAc [Paenibacillus sp. TS12],3SUU_A Crystal structure of beta-hexosaminidase from Paenibacillus sp. TS12 in complex with Gal-PUGNAc [Paenibacillus sp. TS12],3SUV_A Crystal structure of beta-hexosaminidase from Paenibacillus sp. TS12 in complex with NHAc-DNJ [Paenibacillus sp. TS12],3SUW_A Crystal structure of beta-hexosaminidase from Paenibacillus sp. TS12 in complex with NHAc-CAS [Paenibacillus sp. TS12]
7BWG_A	4.00e-19	113	468	80	452	A Glycoside Hydrolase Family 20 beta-N-Acetylglucosaminidase [Microbacterium sp. HJ5],7BWG_B A Glycoside Hydrolase Family 20 beta-N-Acetylglucosaminidase [Microbacterium sp. HJ5]
7CBN_A	1.61e-17	120	505	78	491	Crystal structure of beta-N-acetylhexosaminidase Am0868 from Akkermansia muciniphila [Akkermansia muciniphila ATCC BAA-835],7CBO_A Crystal structure of beta-N-acetylhexosaminidase Am0868 from Akkermansia muciniphila in complex with GlcNAc [Akkermansia muciniphila ATCC BAA-835]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|B2UPR7|H2136_AKKM8	3.11e-38	69	496	140	569	Beta-hexosaminidase Amuc_2136 OS=Akkermansia muciniphila (strain ATCC BAA-835 / DSM 22959 / JCM 33894 / BCRC 81048 / CCUG 64013 / CIP 107961 / Muc) OX=349741 GN=Amuc_2136 PE=1 SV=1
sp|P96155|HEX1_VIBFU	2.16e-19	121	331	209	435	Beta-hexosaminidase OS=Vibrio furnissii OX=29494 GN=exoI PE=1 SV=1
sp|P49008|HEXA_PORGI	2.52e-17	68	291	66	283	Beta-hexosaminidase OS=Porphyromonas gingivalis (strain ATCC BAA-308 / W83) OX=242619 GN=nahA PE=3 SV=2
sp|B2UQG6|H0868_AKKM8	8.59e-17	120	505	97	510	Beta-hexosaminidase Amuc_0868 OS=Akkermansia muciniphila (strain ATCC BAA-835 / DSM 22959 / JCM 33894 / BCRC 81048 / CCUG 64013 / CIP 107961 / Muc) OX=349741 GN=Amuc_0868 PE=1 SV=1
sp|P43077|HEX1_CANAX	3.42e-15	120	498	112	508	Beta-hexosaminidase OS=Candida albicans OX=5476 GN=HEX1 PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
0.782223	0.217774

TMHMM  Annotations     

There is no transmembrane helices in AKAW_09893-t41_1-p1.