| Basic Information | |
|---|---|
| Species | Oryza sativa |
| Cazyme ID | LOC_Os07g38790.1 |
| Family | GH20 |
| Protein Properties | Length: 594 Molecular Weight: 64304.8 Isoelectric Point: 6.1996 |
| Chromosome | Chromosome/Scaffold: 7 Start: 23274099 End: 23276580 |
| Description | beta-hexosaminidase 2 |
| View CDS | |
| External Links |
|---|
| NCBI Taxonomy |
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| GH20 | 182 | 543 | 0 |
| EDRPLYPHRGLMLDTGRTYFPVADILRTIDAMAANKMNVFHWHITDSQSFPLELPSEPALAEKGSYGDGMRYTVDDVKLIVDFAMNRGVRVVPEIDTPGH TASWAGAYPELVSCAGEFWLPDASDWPSRLAAEPGAGQLNPLEPKTYQVMSNVINDVTSLFPDGFYHAGADEVTPGCWNADPSIQRYLARGGTLSRLLEK FVGAAHPLIVSRNRTAVYWEDVLLDQAVNVTASAIPPETTILQTWNNGGNNTRLIVRAGYRAIVSSASFYYLDCGHGDFAGNDSAYDDPRSDYGTSGGSW CGPYKTWQRVYDYDVAGGLTAEEARLVVGGEVAMWTEQVDAAVLDGRVWPRASAMAEALWSG | |||
| Full Sequence |
|---|
| Protein Sequence Length: 594 Download |
| MATKNGGFVA LLLLLSFLLS SPLPARCDAP LPVNVWPKPT SMSWAEPHMA VRVSSSFHVV 60 APSGNAHLLS AARRYAALLL AERYRPLVTP AVNVTAGGAG AGAAGRGAEL GYLTLAVSDL 120 HAPLQHGVDE SYALEILPAG AAATVTAATA WGAMRGLETF SQLAWWCGRE RAVLVAAGVR 180 VEDRPLYPHR GLMLDTGRTY FPVADILRTI DAMAANKMNV FHWHITDSQS FPLELPSEPA 240 LAEKGSYGDG MRYTVDDVKL IVDFAMNRGV RVVPEIDTPG HTASWAGAYP ELVSCAGEFW 300 LPDASDWPSR LAAEPGAGQL NPLEPKTYQV MSNVINDVTS LFPDGFYHAG ADEVTPGCWN 360 ADPSIQRYLA RGGTLSRLLE KFVGAAHPLI VSRNRTAVYW EDVLLDQAVN VTASAIPPET 420 TILQTWNNGG NNTRLIVRAG YRAIVSSASF YYLDCGHGDF AGNDSAYDDP RSDYGTSGGS 480 WCGPYKTWQR VYDYDVAGGL TAEEARLVVG GEVAMWTEQV DAAVLDGRVW PRASAMAEAL 540 WSGNRDATGR KRYAEATDRL TDWRHRMVGR GVRAEPIQPL WCRNRPGMCN LVR* 600 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| cd02742 | GH20_hexosaminidase | 4.0e-61 | 189 | 542 | 363 | + 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. | ||
| cd06570 | GH20_chitobiase-like_1 | 1.0e-71 | 187 | 542 | 358 | + 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. | ||
| cd06563 | GH20_chitobiase-like | 6.0e-78 | 187 | 560 | 394 | + 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-116 | 187 | 544 | 359 | + Glycosyl hydrolase family 20, catalytic domain. This domain has a TIM barrel fold. | ||
| cd06562 | GH20_HexA_HexB-like | 1.0e-157 | 187 | 571 | 387 | + 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:0005886 | plasma membrane |
| GO:0005975 | carbohydrate metabolic process |
| GO:0008152 | metabolic process |
| Annotations - NR Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| DDBJ | BAF21992.2 | 0 | 1 | 593 | 1 | 593 | Os07g0575500 [Oryza sativa Japonica Group] |
| GenBank | EEE67459.1 | 0 | 1 | 593 | 1 | 559 | hypothetical protein OsJ_24848 [Oryza sativa Japonica Group] |
| RefSeq | NP_001060078.1 | 0 | 1 | 593 | 1 | 593 | Os07g0575500 [Oryza sativa (japonica cultivar-group)] |
| RefSeq | NP_001147095.1 | 0 | 29 | 593 | 26 | 578 | beta-hexosaminidase [Zea mays] |
| RefSeq | XP_002463072.1 | 0 | 29 | 593 | 26 | 584 | hypothetical protein SORBIDRAFT_02g037280 [Sorghum bicolor] |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 3ozp_A | 0 | 35 | 589 | 43 | 570 | A Chain A, X-Ray Crystal Structure Of Tdp-Vancosaminyltransferase Gtfd As A Complex With Tdp And The Natural Substrate, Desvancosaminyl Vancomycin. |
| PDB | 3ozo_A | 0 | 35 | 589 | 43 | 570 | A Chain A, X-Ray Crystal Structure Of Tdp-Vancosaminyltransferase Gtfd As A Complex With Tdp And The Natural Substrate, Desvancosaminyl Vancomycin. |
| PDB | 3nsn_A | 0 | 35 | 589 | 43 | 570 | A Chain A, X-Ray Crystal Structure Of Tdp-Vancosaminyltransferase Gtfd As A Complex With Tdp And The Natural Substrate, Desvancosaminyl Vancomycin. |
| PDB | 3nsm_A | 0 | 35 | 589 | 43 | 570 | A Chain A, Crystal Structure Of Insect Beta-N-Acetyl-D-Hexosaminidase Ofhex1 From Ostrinia Furnacalis |
| PDB | 3s6t_A | 0 | 35 | 589 | 46 | 573 | 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 |
