Basic Information | |
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Species | Ricinus communis |
Cazyme ID | 47890.m000013 |
Family | GH20 |
Protein Properties | Length: 355 Molecular Weight: 38556.9 Isoelectric Point: 7.2606 |
Chromosome | Chromosome/Scaffold: 47890 Start: 7 End: 1071 |
Description | beta-hexosaminidase 2 |
View CDS |
External Links |
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NCBI Taxonomy |
Plaza |
CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
GH20 | 1 | 235 | 0 |
MPAHITSAIAAYPWLASRPNPPAAPASDWGILPDVINPNPRNIAFFETVLDQVMRLFPSKLIHIGGDEAMKDHWNANPAVRAQMQALGLEDAEGLQAWFM ARIAAYVAAHGRQAIGWDKSAPLPAEAVVMSWAGSEAAVAAIKAGHETILAPAPVFYINNRQSQSNDEPPGRRDIISWQRVYQADAPPAGLSDEERARVL GLHVALWTEYVRTTEQTDRMIWPRASVLAEIGWSS |
Full Sequence |
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Protein Sequence Length: 355 Download |
MPAHITSAIA AYPWLASRPN PPAAPASDWG ILPDVINPNP RNIAFFETVL DQVMRLFPSK 60 LIHIGGDEAM KDHWNANPAV RAQMQALGLE DAEGLQAWFM ARIAAYVAAH GRQAIGWDKS 120 APLPAEAVVM SWAGSEAAVA AIKAGHETIL APAPVFYINN RQSQSNDEPP GRRDIISWQR 180 VYQADAPPAG LSDEERARVL GLHVALWTEY VRTTEQTDRM IWPRASVLAE IGWSSAPREW 240 EAFAPRLLAE IKRQQSLGLS MDLTPLEPMG RFTAAGGGKV RAVLDQPAAL GTLRYTLDGS 300 APRSASPAYS EPLLLGGGTV LTVRAFADAE PLGSARNWRM SAALTRTLAR RRDGH 360 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
cd06562 | GH20_HexA_HexB-like | 2.0e-36 | 36 | 249 | 222 | + 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. | ||
cd06570 | GH20_chitobiase-like_1 | 8.0e-40 | 1 | 236 | 239 | + 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. | ||
COG3525 | Chb | 2.0e-49 | 1 | 341 | 356 | + N-acetyl-beta-hexosaminidase [Carbohydrate transport and metabolism] | ||
pfam00728 | Glyco_hydro_20 | 1.0e-53 | 1 | 234 | 244 | + Glycosyl hydrolase family 20, catalytic domain. This domain has a TIM barrel fold. | ||
cd06563 | GH20_chitobiase-like | 2.0e-88 | 1 | 247 | 250 | + 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. |
Gene Ontology | |
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GO Term | Description |
GO:0004553 | hydrolase activity, hydrolyzing O-glycosyl compounds |
Annotations - NR Download unfiltered results here | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
RefSeq | NP_419266.1 | 0 | 2 | 347 | 260 | 607 | beta-N-acetylhexosaminidase, putative [Caulobacter crescentus CB15] |
RefSeq | XP_002538791.1 | 0 | 1 | 355 | 1 | 355 | Beta-hexosaminidase precursor, putative [Ricinus communis] |
RefSeq | YP_001681928.1 | 0 | 1 | 347 | 280 | 629 | Beta-N-acetylhexosaminidase [Caulobacter sp. K31] |
RefSeq | YP_001914285.1 | 0 | 1 | 337 | 220 | 565 | beta-hexosaminidase [Xanthomonas oryzae pv. oryzae PXO99A] |
RefSeq | ZP_06123353.1 | 0 | 2 | 347 | 260 | 607 | Beta-N-acetylhexosaminidase [Caulobacter segnis ATCC 21756] |
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 | 3rcn_A | 2e-38 | 1 | 260 | 246 | 512 | A Chain A, Crystal Structure Of Beta-N-Acetylhexosaminidase From Arthrobacter Aurescens |
PDB | 3suw_A | 1e-19 | 1 | 266 | 278 | 524 | A Chain A, Crystal Structure Of Beta-N-Acetylhexosaminidase From Arthrobacter Aurescens |
PDB | 3suv_A | 1e-19 | 1 | 266 | 278 | 524 | A Chain A, Crystal Structure Of Beta-N-Acetylhexosaminidase From Arthrobacter Aurescens |
PDB | 3suu_A | 1e-19 | 1 | 266 | 278 | 524 | A Chain A, Crystal Structure Of Beta-N-Acetylhexosaminidase From Arthrobacter Aurescens |
PDB | 3sut_A | 1e-19 | 1 | 266 | 278 | 524 | A Chain A, Crystal Structure Of Beta-N-Acetylhexosaminidase From Arthrobacter Aurescens |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
FG601912 | 215 | 96 | 307 | 6e-20 |
GO978280 | 202 | 39 | 234 | 6e-18 |
ES755087 | 207 | 41 | 239 | 2e-16 |
JG187931 | 229 | 36 | 234 | 9e-16 |
DW119158 | 203 | 39 | 235 | 0.000000000000001 |
Sequence Alignments (This image is cropped. Click for full image.) |
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