| Basic Information | |
|---|---|
| Species | Sorghum bicolor |
| Cazyme ID | Sb02g037280.1 |
| Family | GH20 |
| Protein Properties | Length: 585 Molecular Weight: 63796.2 Isoelectric Point: 5.0296 |
| Chromosome | Chromosome/Scaffold: 2 Start: 71633329 End: 71635214 |
| 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 | 174 | 534 | 0 |
| EDRPLYPHRGLMLDTGRTYFPVSDILRTIDAMAANKMNVFHWHITDSQSFPIVLPSEPSLAEKGAYGEDMVYTVEDVKRIVEFAMSRGVRVVPEIDSPGH TASWAGAYPEAVTCAGKFWLPDGDWNNRLAAEPGAGQLNPLAPKTYEVITNVVNDLTSLFPDGFYHAGADEVTPGCWQADATIQADLERGGTLSQLLERY VSAVHPLVVSKNRTAVYWEDVLLDAAVNVSASLIPPATTILQSWNNGANNTKLIVQAGYRAIVSSASFYYLDCGHGDFVGNNSIYDDPNSDYDTDGGSWC GPYKTWQRVYDYDITYGLTAEEAQLVIGGEVAMWTEQVDTAVLDGRVWPRASAMAEALWSG | |||
| Full Sequence |
|---|
| Protein Sequence Length: 585 Download |
| MATLLLQLLF LLGWPVTLLT CAAAGASFPV NVWPKPTSMS WAEPHSAVPV SPSFHIVASS 60 GNPYLVSAAE RYAKLLFKET YRPIVRPAVN VTAGNALETL TLAVSDLAAP LQHGVDESYT 120 LEILPTGAAT VTAVTAWGAM RGLETFSQLS WRAGGRGRSR SRDLLLVAAG VRVEDRPLYP 180 HRGLMLDTGR TYFPVSDILR TIDAMAANKM NVFHWHITDS QSFPIVLPSE PSLAEKGAYG 240 EDMVYTVEDV KRIVEFAMSR GVRVVPEIDS PGHTASWAGA YPEAVTCAGK FWLPDGDWNN 300 RLAAEPGAGQ LNPLAPKTYE VITNVVNDLT SLFPDGFYHA GADEVTPGCW QADATIQADL 360 ERGGTLSQLL ERYVSAVHPL VVSKNRTAVY WEDVLLDAAV NVSASLIPPA TTILQSWNNG 420 ANNTKLIVQA GYRAIVSSAS FYYLDCGHGD FVGNNSIYDD PNSDYDTDGG SWCGPYKTWQ 480 RVYDYDITYG LTAEEAQLVI GGEVAMWTEQ VDTAVLDGRV WPRASAMAEA LWSGNRDASG 540 RKRYAEATDR LIDWRQRMVG RGIRAEPIQP LWCRTRPGMC NAVQ* 600 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| cd02742 | GH20_hexosaminidase | 1.0e-59 | 181 | 533 | 362 | + 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-67 | 179 | 533 | 357 | + 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 | 1.0e-76 | 179 | 534 | 376 | + 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-115 | 179 | 535 | 358 | + Glycosyl hydrolase family 20, catalytic domain. This domain has a TIM barrel fold. | ||
| cd06562 | GH20_HexA_HexB-like | 1.0e-158 | 179 | 562 | 386 | + 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 |
| DDBJ | BAF21992.2 | 0 | 22 | 584 | 25 | 593 | Os07g0575500 [Oryza sativa Japonica Group] |
| GenBank | EEE67459.1 | 0 | 22 | 584 | 25 | 559 | hypothetical protein OsJ_24848 [Oryza sativa Japonica Group] |
| RefSeq | NP_001060078.1 | 0 | 22 | 584 | 25 | 593 | Os07g0575500 [Oryza sativa (japonica cultivar-group)] |
| RefSeq | NP_001147095.1 | 0 | 21 | 584 | 21 | 578 | beta-hexosaminidase [Zea mays] |
| RefSeq | XP_002463072.1 | 0 | 1 | 584 | 1 | 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 | 32 | 580 | 43 | 570 | A Chain A, Crystal Structure Of Human Pofut2 |
| PDB | 3ozo_A | 0 | 32 | 580 | 43 | 570 | A Chain A, Crystal Structure Of Human Pofut2 |
| PDB | 3nsn_A | 0 | 32 | 580 | 43 | 570 | A Chain A, Crystal Structure Of Human Pofut2 |
| PDB | 3nsm_A | 0 | 32 | 580 | 43 | 570 | A Chain A, Crystal Structure Of Insect Beta-N-Acetyl-D-Hexosaminidase Ofhex1 From Ostrinia Furnacalis |
| PDB | 3s6t_A | 0 | 32 | 580 | 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 |
