| Basic Information | |
|---|---|
| Species | Sorghum bicolor |
| Cazyme ID | Sb01g042640.1 |
| Family | GH20 |
| Protein Properties | Length: 574 Molecular Weight: 62954.6 Isoelectric Point: 7.6548 |
| Chromosome | Chromosome/Scaffold: 1 Start: 65892971 End: 65895359 |
| Description | beta-hexosaminidase 2 |
| View CDS | |
| External Links |
|---|
| NCBI Taxonomy |
| Plaza |
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| GH20 | 230 | 523 | 0 |
| DVRRIVRFAESFGIRVIPEIDMPGHTGSWAAAYPEIVTCANKFWAPKAKPALAAEPCTGQLNPLNPKTYRVAQDVLRDLAALFPDPYLHAGADEVNTACW EDDPVVRGFLADGGSHDRLLELFVNATRPFLVHELNRTSVYWEDVLLGPKVSVGQTVLPRDTTVLQTWNNGAANTKRVVSAGYRVIVSSSSYYYLDCGHG GWVGNDSRYDVQEKEHDGMPLFNDPGGTGGSWCAPFKTWQRIYDYDILHGLTEDEARRVLGGEVALWSEQSDAAVLDSRLWPRASAAAETLWSG | |||
| Full Sequence |
|---|
| Protein Sequence Length: 574 Download |
| MAASPYFLLL LLFLFHPLAA LAPLAPSPSP SPSQPSPPRS QPPPPRVPQQ VQVWPKPVSI 60 SWPLPVYAPL SPSFSIRASP SHPSLRHAIA YYTRLIRTER HAPIMPPVNY TIAGVPIRLL 120 ALSVSDPDTK LGPGVDESYT LSVPPNSSSA DISAATPWGV IRGLETFSQL AWSSSAAAAG 180 GQPIVPSDLE ISDHPLFTHR GVLLDTARNY YPVGDILRTI RAMAANKLND VRRIVRFAES 240 FGIRVIPEID MPGHTGSWAA AYPEIVTCAN KFWAPKAKPA LAAEPCTGQL NPLNPKTYRV 300 AQDVLRDLAA LFPDPYLHAG ADEVNTACWE DDPVVRGFLA DGGSHDRLLE LFVNATRPFL 360 VHELNRTSVY WEDVLLGPKV SVGQTVLPRD TTVLQTWNNG AANTKRVVSA GYRVIVSSSS 420 YYYLDCGHGG WVGNDSRYDV QEKEHDGMPL FNDPGGTGGS WCAPFKTWQR IYDYDILHGL 480 TEDEARRVLG GEVALWSEQS DAAVLDSRLW PRASAAAETL WSGNKGSNGR KRYANATVRL 540 NEWRHRMVAR GIRAEPIQPL WCPMHPHMCN LSQ* 600 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| cd06570 | GH20_chitobiase-like_1 | 2.0e-35 | 197 | 416 | 261 | + 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. | ||
| cd02742 | GH20_hexosaminidase | 9.0e-38 | 199 | 522 | 367 | + 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. | ||
| cd06563 | GH20_chitobiase-like | 9.0e-50 | 197 | 528 | 389 | + 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 | 8.0e-86 | 197 | 524 | 366 | + Glycosyl hydrolase family 20, catalytic domain. This domain has a TIM barrel fold. | ||
| cd06562 | GH20_HexA_HexB-like | 4.0e-118 | 197 | 551 | 394 | + 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 | |
|---|---|
| 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 | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| GenBank | ACF87335.1 | 0 | 1 | 573 | 3 | 599 | unknown [Zea mays] |
| GenBank | EAZ03246.1 | 0 | 232 | 573 | 47 | 400 | hypothetical protein OsI_25394 [Oryza sativa Indica Group] |
| RefSeq | NP_001049401.1 | 0 | 37 | 573 | 30 | 605 | Os03g0219400 [Oryza sativa (japonica cultivar-group)] |
| RefSeq | NP_001146582.1 | 0 | 1 | 573 | 3 | 599 | hypothetical protein LOC100280178 [Zea mays] |
| RefSeq | XP_002465632.1 | 0 | 39 | 573 | 39 | 573 | hypothetical protein SORBIDRAFT_01g042640 [Sorghum bicolor] |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 3vtr_A | 0 | 135 | 569 | 125 | 570 | A Chain A, Crystal Structure Of Insect Beta-n-acetyl-d-hexosaminidase Ofhex1 E328a Complexed With Tmg-chitotriomycin |
| PDB | 3s6t_A | 0 | 135 | 569 | 128 | 573 | A Chain A, Crystal Structure Of Insect Beta-N-Acetyl-D-Hexosaminidase Ofhex1 V327g Complexed With Pugnac |
| PDB | 3ozp_A | 0 | 135 | 569 | 125 | 570 | A Chain A, Crystal Structure Of Insect Beta-N-Acetyl-D-Hexosaminidase Ofhex1 V327g Complexed With Pugnac |
| PDB | 3ozo_A | 0 | 135 | 569 | 125 | 570 | A Chain A, Crystal Structure Of Insect Beta-N-Acetyl-D-Hexosaminidase Ofhex1 V327g Complexed With Pugnac |
| PDB | 3nsn_A | 0 | 135 | 569 | 125 | 570 | A Chain A, Crystal Structure Of Insect Beta-N-Acetyl-D-Hexosaminidase Ofhex1 V327g Complexed With Pugnac |
| Metabolic Pathways | |||
|---|---|---|---|
| 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 |
