Basic Information | |
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Species | Panicum virgatum |
Cazyme ID | Pavirv00062645m |
Family | GH20 |
Protein Properties | Length: 446 Molecular Weight: 49139 Isoelectric Point: 6.9486 |
Chromosome | Chromosome/Scaffold: 002160 Start: 11132 End: 16425 |
Description | beta-hexosaminidase 3 |
View CDS |
External Links |
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CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
GH20 | 174 | 254 | 3.6e-29 |
MDVPRFHYRGLLIDTSRHYLPVPVIKSVIDSMTFSKLNVLHWHIVDEQSFPLQIPSYPKLWNGAYSYSERYTFDDAIDIVQ | |||
GH20 | 258 | 396 | 6.7e-32 |
HGMNESDAYRYFVLRAQKIAISHGYDIINWEETFNNFGDKLDRKTVVHNWLGSGVAQKVVTAGLRCIVSNQDKWYLDHLDATWEGFYMNEPLTNIYNPEQ QRLVLGGEVCMWGEHIDASDIQQTIWPRAAAAAERLWTP |
Full Sequence |
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Protein Sequence Length: 446 Download |
MAPAARLLLA LLAAAAAAVG PCAGAGAGAG RVDLWPMPAS VARGAQTLLV SRDLKLSTPG 60 SNYSDGRGIL REAFQRMLAV VELDHVVNGS YGGRGSPVLA GVRVVVRSPN DELNFGVDES 120 YKLSVPATGN PLYAQIEAQT VFGALHALET FSQLCKFDFN ARLIELHSAP WTIMDVPRFH 180 YRGLLIDTSR HYLPVPVIKS VIDSMTFSKL NVLHWHIVDE QSFPLQIPSY PKLWNGAYSY 240 SERYTFDDAI DIVQLIQHGM NESDAYRYFV LRAQKIAISH GYDIINWEET FNNFGDKLDR 300 KTVVHNWLGS GVAQKVVTAG LRCIVSNQDK WYLDHLDATW EGFYMNEPLT NIYNPEQQRL 360 VLGGEVCMWG EHIDASDIQQ TIWPRAAAAA ERLWTPIEKL AKDPGSVAAR LARFRCLLNQ 420 RGVAAAPLAG YGRSAPSEPG SCLRQ* |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
cd06563 | GH20_chitobiase-like | 4.0e-21 | 261 | 399 | 153 | + 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. | ||
pfam00728 | Glyco_hydro_20 | 1.0e-28 | 179 | 254 | 77 | + Glycosyl hydrolase family 20, catalytic domain. This domain has a TIM barrel fold. | ||
pfam00728 | Glyco_hydro_20 | 3.0e-32 | 255 | 396 | 159 | + Glycosyl hydrolase family 20, catalytic domain. This domain has a TIM barrel fold. | ||
cd06562 | GH20_HexA_HexB-like | 2.0e-38 | 179 | 254 | 77 | + 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. | ||
cd06562 | GH20_HexA_HexB-like | 1.0e-59 | 259 | 422 | 171 | + 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. |
Gene Ontology | |
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GO Term | Description |
GO:0004553 | hydrolase activity, hydrolyzing O-glycosyl compounds |
GO:0004563 | beta-N-acetylhexosaminidase activity |
GO:0005975 | carbohydrate metabolic process |
Annotations - NR Download unfiltered results here | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
GenBank | AAT77374.1 | 0 | 32 | 261 | 27 | 255 | putative beta-N-acetylhexosaminidase [Oryza sativa Japonica Group] |
GenBank | AAT77374.1 | 0 | 255 | 445 | 335 | 527 | putative beta-N-acetylhexosaminidase [Oryza sativa Japonica Group] |
RefSeq | NP_001055557.1 | 0 | 32 | 261 | 31 | 259 | Os05g0415700 [Oryza sativa (japonica cultivar-group)] |
RefSeq | NP_001055557.1 | 0 | 255 | 445 | 339 | 531 | Os05g0415700 [Oryza sativa (japonica cultivar-group)] |
RefSeq | XP_002514769.1 | 0 | 24 | 445 | 19 | 527 | beta-hexosaminidase, putative [Ricinus communis] |
Annotations - PDB Download unfiltered results here | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
PDB | 3lmy_B | 3e-34 | 11 | 254 | 36 | 276 | A Chain A, The Crystal Structure Of Beta-Hexosaminidase B In Complex With Pyrimethamine |
PDB | 3lmy_B | 1e-22 | 251 | 431 | 369 | 550 | A Chain A, The Crystal Structure Of Beta-Hexosaminidase B In Complex With Pyrimethamine |
PDB | 3lmy_A | 3e-34 | 11 | 254 | 36 | 276 | A Chain A, The Crystal Structure Of Beta-Hexosaminidase B In Complex With Pyrimethamine |
PDB | 3lmy_A | 1e-22 | 251 | 431 | 369 | 550 | A Chain A, The Crystal Structure Of Beta-Hexosaminidase B In Complex With Pyrimethamine |
PDB | 1o7a_F | 9e-34 | 17 | 254 | 1 | 235 | A Chain A, Human Beta-Hexosaminidase B |
Metabolic Pathways | |||
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Pathway Name | Reaction | EC | Protein Name |
chitin degradation II | RXN-12625 | EC-3.2.1.52 | β-L-N-acetylhexosaminidase |
chitin degradation II | RXN-12626 | EC-3.2.1.52 | β-L-N-acetylhexosaminidase |