CAZyme Information: PHYBL_143275T0-p1

Basic Information

• Species: Phycomyces blakesleeanus
• Lineage: Mucoromycota; Mucoromycetes; ; Phycomycetaceae; Phycomyces; Phycomyces blakesleeanus
• CAZyme ID: PHYBL_143275T0-p1
• CAZy Family: GH25
• CAZyme Description: Beta-N-acetylhexosaminidase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
613	PblaNRRL1555-_SC06|CGC2	69709.65	5.5095

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_PblakesleeanusNRRL1555	16528	763407	0	16528

• Gene Location: location=PblaNRRL1555-_SC06:1782808-1785537(+)

Full Sequence      

MKRSLLTLTLLSVAFGQPVFLWPKPQSIQWGDVQLNLGRSFNIRGPDIAVLEDAMRRYTH
LIARERWDPVQVSDADNVNPVHASKHLNSLDIEIIDKEAALTFGTDESYTLHISPENTIG
TLKAQTVWGALRGLETFSQLVQAKYNDSEGEDEDEDEYAYEDDNDLGFQGLFIPQTPIII
NDEPRFSHRGLMLDTSRNYYPVKDLLRTLDAMAYNKMNVFHWHITDSQSFPLVLDSVPEL
AKKGAYRLHGKKLVYTKQDVRVIVKHAHSRGIRVIPEIDMPGHTGSWAKAFKQFISGIYP
LFSTCSDRFFLDPSNSWEKRYAAEPGSGQLNPILKGTYTLVKQVIDEVTALFPDEWYHGG
GDEPVYRCWEDAKSVRDYMARNNVTGLDLLNIFLEKELEIINSVTENHLAIPKDVVIQVW
KNPVKKAVKAGYKVIASSSNFWYLDCGHGQWSGNDTAVNEQSPPVIKKPLQKALEKYEGS
DNYNPSNWGGSGGDWCSPFKSWQRMYIYDITYGLSKEETKYVLGGECALWSEQSDETTLD
ARLWPRAAATAEVLWSGNYDEDGNKRSVDDAMPRMFDWRYRLLKRGIRAEPLQPLWCGSH
PHMCDAAFPAGYL

Enzyme Prediction     

EC	3.2.1.52:9

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH20	178	557	2.4e-88	0.9821958456973294

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
119332	GH20_HexA_HexB-like	2.63e-153	186	586	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	2.99e-123	186	557	1	345	Glycosyl hydrolase family 20, catalytic domain. This domain has a TIM barrel fold.
119333	GH20_chitobiase-like	5.32e-79	186	575	1	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.
119338	GH20_chitobiase-like_1	2.34e-69	186	556	1	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.
119331	GH20_hexosaminidase	3.25e-55	188	556	1	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AKU79211.1|GH20	2.52e-260	19	613	23	639
CDS09580.1|GH20	1.00e-258	17	609	22	611
CDS07988.1|GH20	1.35e-245	19	613	26	628
BBN00792.1|GH20	5.07e-165	19	608	93	663
BAG94727.1|GH20	1.28e-164	16	605	43	602

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5OAR_B	1.69e-116	83	605	1	490	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]
1NOU_A	3.35e-93	21	603	7	507	Native human lysosomal beta-hexosaminidase isoform B [Homo sapiens],1NOU_B Native human lysosomal beta-hexosaminidase isoform B [Homo sapiens],1NOW_A Human lysosomal beta-hexosaminidase isoform B in complex with (2R,3R,4S,5R)-2-Acetamido-3,4-Dihydroxy-5-Hydroxymethyl-Piperidinium Chloride (GalNAc-isofagomine) [Homo sapiens],1NOW_B Human lysosomal beta-hexosaminidase isoform B in complex with (2R,3R,4S,5R)-2-Acetamido-3,4-Dihydroxy-5-Hydroxymethyl-Piperidinium Chloride (GalNAc-isofagomine) [Homo sapiens],2GJX_B Crystallographic structure of human beta-Hexosaminidase A [Homo sapiens],2GJX_C Crystallographic structure of human beta-Hexosaminidase A [Homo sapiens],2GJX_F Crystallographic structure of human beta-Hexosaminidase A [Homo sapiens],2GJX_G Crystallographic structure of human beta-Hexosaminidase A [Homo sapiens]
1O7A_A	4.19e-93	21	603	15	515	Human beta-Hexosaminidase B [Homo sapiens],1O7A_B Human beta-Hexosaminidase B [Homo sapiens],1O7A_C Human beta-Hexosaminidase B [Homo sapiens],1O7A_D Human beta-Hexosaminidase B [Homo sapiens],1O7A_E Human beta-Hexosaminidase B [Homo sapiens],1O7A_F Human beta-Hexosaminidase B [Homo sapiens]
3LMY_A	1.28e-92	21	603	56	556	The Crystal Structure of beta-hexosaminidase B in complex with Pyrimethamine [Homo sapiens],3LMY_B The Crystal Structure of beta-hexosaminidase B in complex with Pyrimethamine [Homo sapiens]
5BRO_A	2.23e-92	21	603	14	514	Crystal structure of modified HexB (modB) [Homo sapiens]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q9SYK0|HEXO2_ARATH	2.80e-154	8	610	18	576	Beta-hexosaminidase 2 OS=Arabidopsis thaliana OX=3702 GN=HEXO2 PE=1 SV=1
sp|E9DFH0|HEX1_COCPS	7.70e-125	23	605	27	586	Beta-hexosaminidase 1 OS=Coccidioides posadasii (strain RMSCC 757 / Silveira) OX=443226 GN=HEX1 PE=1 SV=1
sp|Q8J2T0|HEXA_ASPOZ	3.96e-116	23	605	25	591	Beta-hexosaminidase OS=Aspergillus oryzae OX=5062 GN=nagA PE=1 SV=1
sp|Q9HGI3|HEXA_EMEND	4.47e-112	23	605	26	594	Beta-hexosaminidase OS=Emericella nidulans OX=162425 GN=nagA PE=1 SV=1
sp|P43077|HEX1_CANAX	1.31e-109	13	605	19	554	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
0.000353	0.999627	CS pos: 16-17. Pr: 0.9707

TMHMM  Annotations     

There is no transmembrane helices in PHYBL_143275T0-p1.