CAZyme Information: KLU86646.1

Basic Information

• Species: Magnaporthiopsis poae
• Lineage: Ascomycota; Sordariomycetes; ; Magnaporthaceae; Magnaporthiopsis; Magnaporthiopsis poae
• CAZyme ID: KLU86646.1
• CAZy Family: GH16
• CAZyme Description: Beta-N-acetylhexosaminidase [Source:UniProtKB/TrEMBL;Acc:A0A0C4DZZ5]

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
764		83588.03	6.2723

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_MpoaeATCC64411	12363	644358	200	12163

• Gene Location: location=GL876969:2723444-2725971(+)

Full Sequence      

MGRLHIQCPAEVGACSPWGFRSNIRVQDHHRSPCPHQGYTHGARPTSAMRANGILKLATA
ISAACAAVFPGIPTVPFERDGSAVLDFSSLSAIVVDEVHAASRDTRGLTLIPPTLRDFAE
TFAGDVGSVLGQNVSVVTGTAAAPGAIFLTLGDARDYLDVAGRETSEGYTLETTAEGIVI
RGASPLGVWWGTRTTLQQALVGNGSLPLGRALDSPGWGSRGMMLDVARHYYPADFLIEMC
SYMSFWKQNTFHLHLSDNLWNNARIYSFERQMELYAAFRLDSDDPAVRGLNKRRNESYSR
DVFDEIQTKCAARGVTIVPEIETPGHALVISQWKPQIGMSSDYSLLNISHPETVPTVKAI
WRVFLPWIQSKVVSIGADEYRDETLSPAALAKEYIRFADELNDFIVNESGKKVRLWGTFG
SAVAGKFNTSISVQHWAPWEGNPVFDWVKHGYGVMNSGDRVYIVGKWSQSYPQELNQQFI
FHGSPDRSAFAPNIFDPNNATNNSPRNEPKIEGHIAPLWNDYGPNATTVLEAYWSWRDGL
PALADKQWGGALTETEYPALFARLQPHVPGQNLERRIPSKGSTVLEYDFAATARRYESRI
EDTSGNDYHAATTCARTSEGVVLTSSCSIRTPLSSKGRDYTLSFSVKPTSSAKGPILTGS
DSALWFGNGTVDAVMLFSGESVYALNYTFPVGQWTNASLVGKGTRTYLRVEGAAAVPPVE
FLTVIGWNGERFVWERMAVEAPLQTIGGGGFEGIIGSMKLVDGA

Enzyme Prediction     

No EC number prediction in KLU86646.1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH20	216	549	1.6e-49	0.9584569732937686

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
119334	GH20_DspB_LnbB-like	1.62e-110	220	550	3	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	1.48e-30	220	535	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	4.35e-25	220	548	4	343	Glycosyl hydrolase family 20, catalytic domain. This domain has a TIM barrel fold.
119333	GH20_chitobiase-like	1.84e-24	216	564	2	357	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.
226056	Chb	9.46e-23	165	565	204	636	N-acetyl-beta-hexosaminidase [Carbohydrate transport and metabolism].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QBZ56968.1|GH20	0.0	55	762	5	718
UQC84237.1|GH20	0.0	70	764	21	712
UPL02709.1|GH20	0.0	54	764	5	709
QKX53893.1|GH20	8.89e-278	71	761	27	728
UJO23164.1|GH20	1.43e-266	71	764	23	719

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6JQF_A	1.08e-34	116	551	118	549	Crystallization analysis of a beta-N-acetylhexosaminidase (Am2136) from Akkermansia muciniphila [Akkermansia muciniphila ATCC BAA-835]
3GH4_A	4.08e-17	115	436	76	393	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	3.73e-15	125	337	50	249	A Glycoside Hydrolase Family 20 beta-N-Acetylglucosaminidase [Microbacterium sp. HJ5],7BWG_B A Glycoside Hydrolase Family 20 beta-N-Acetylglucosaminidase [Microbacterium sp. HJ5]
6EZR_A	4.84e-15	169	417	211	481	Crystal structure of GH20 Exo beta-N-Acetylglucosaminidase from Vibrio harveyi [Vibrio harveyi],6EZR_B Crystal structure of GH20 Exo beta-N-Acetylglucosaminidase from Vibrio harveyi [Vibrio harveyi],6EZS_A Crystal structure of GH20 Exo beta-N-Acetylglucosaminidase from Vibrio harveyi in complex with N-acetylglucosamine [Vibrio harveyi],6EZS_B Crystal structure of GH20 Exo beta-N-Acetylglucosaminidase from Vibrio harveyi in complex with N-acetylglucosamine [Vibrio harveyi],6K35_A Crystal structure of GH20 exo beta-N-acetylglucosaminidase from Vibrio harveyi in complex with NAG-thiazoline [Vibrio harveyi],6K35_B Crystal structure of GH20 exo beta-N-acetylglucosaminidase from Vibrio harveyi in complex with NAG-thiazoline [Vibrio harveyi]
6JE8_A	9.14e-15	166	393	36	272	crystal structure of a beta-N-acetylhexosaminidase [Akkermansia muciniphila ATCC BAA-835],6JEA_A crystal structure of a beta-N-acetylhexosaminidase [Akkermansia muciniphila ATCC BAA-835],6JEB_A crystal structure of a beta-N-acetylhexosaminidase [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	4.69e-37	116	551	140	571	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	1.44e-15	169	417	210	478	Beta-hexosaminidase OS=Vibrio furnissii OX=29494 GN=exoI PE=1 SV=1
sp|B2UP57|H2018_AKKM8	5.18e-14	166	393	57	293	Beta-hexosaminidase Amuc_2018 OS=Akkermansia muciniphila (strain ATCC BAA-835 / DSM 22959 / JCM 33894 / BCRC 81048 / CCUG 64013 / CIP 107961 / Muc) OX=349741 GN=Amuc_2018 PE=1 SV=1
sp|P43077|HEX1_CANAX	8.40e-14	166	550	111	507	Beta-hexosaminidase OS=Candida albicans OX=5476 GN=HEX1 PE=1 SV=1
sp|P49008|HEXA_PORGI	1.99e-13	115	436	66	401	Beta-hexosaminidase OS=Porphyromonas gingivalis (strain ATCC BAA-308 / W83) OX=242619 GN=nahA PE=3 SV=2

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
0.998288	0.001711

TMHMM  Annotations     

There is no transmembrane helices in KLU86646.1.