Basic Information | |
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Species | Picea abies |
Cazyme ID | MA_92690g0010 |
Family | GH20 |
Protein Properties | Length: 479 Molecular Weight: 54657.8 Isoelectric Point: 7.5523 |
View CDS |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
GH20 | 297 | 429 | 3.5e-24 |
ETTILQTWNNDHNNTKRITAACYRAIVSSTDFYYLDCGHGGWLGNDSRYDKQISDAPGRPFNYNGGNGGSWCAPFKTWQRIYDYDISYGLSEEESKLVLG GEVALWSEQSDRTGMDGRIWPRASAMAETLWSG | |||
GH20 | 179 | 289 | 1.96182e-44 |
DYPLYPHRGLVLDTARNFYPLRDILRTIRAMSYNKLNVFHWHITDSQSFPLELNSEPALAINGSYSPEMRYSSKDVQRIVKFGRNHGVRVIPELDTPAHS ASWADAYPDIV |
Full Sequence |
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Protein Sequence Length: 479 Download |
MKILGSSRCV IIICLWVFFL SHFHSSAVVA VSQQEQYPWP KPISTVWGDA VSIPLSPTFK 60 IVSVNHIYLQ SSVSRYNRII RSEHWFPILS SSSYNTIDSS TISSLEKLDV FVRDLQADLQ 120 HGVDESYTLT VPAGGAVNLS AETPWGAMRG LETFSQLVHR YNATSVYPLV FQRQVKIFDY 180 PLYPHRGLVL DTARNFYPLR DILRTIRAMS YNKLNVFHWH ITDSQSFPLE LNSEPALAIN 240 GSYSPEMRYS SKDVQRIVKF GRNHGVRVIP ELDTPAHSAS WADAYPDIVT CAGMFWETTI 300 LQTWNNDHNN TKRITAACYR AIVSSTDFYY LDCGHGGWLG NDSRYDKQIS DAPGRPFNYN 360 GGNGGSWCAP FKTWQRIYDY DISYGLSEEE SKLVLGGEVA LWSEQSDRTG MDGRIWPRAS 420 AMAETLWSGN RDCDGKKRYA EAMDRLNQWR YRMVKRRIDA EPLQPLWCLK NPGMCTLDQ 480 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
pfam00728 | Glyco_hydro_20 | 7.0e-21 | 254 | 430 | 178 | + Glycosyl hydrolase family 20, catalytic domain. This domain has a TIM barrel fold. | ||
cd02742 | GH20_hexosaminidase | 2.0e-31 | 185 | 290 | 110 | + 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. | ||
pfam00728 | Glyco_hydro_20 | 4.0e-43 | 183 | 308 | 126 | + Glycosyl hydrolase family 20, catalytic domain. This domain has a TIM barrel fold. | ||
cd06562 | GH20_HexA_HexB-like | 2.0e-43 | 297 | 456 | 160 | + 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 | 9.0e-57 | 183 | 298 | 116 | + 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. |
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 | EAZ03246.1 | 3e-17 | 209 | 296 | 1 | 100 | hypothetical protein OsI_25394 [Oryza sativa Indica Group] |
GenBank | EAZ03246.1 | 0 | 297 | 479 | 217 | 400 | hypothetical protein OsI_25394 [Oryza sativa Indica Group] |
RefSeq | NP_001049401.1 | 0 | 297 | 479 | 422 | 605 | Os03g0219400 [Oryza sativa (japonica cultivar-group)] |
RefSeq | XP_002266897.1 | 0 | 17 | 296 | 12 | 280 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002266897.1 | 0 | 297 | 475 | 399 | 569 | PREDICTED: hypothetical protein [Vitis vinifera] |
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 | 2gk1_G | 4.99983e-42 | 125 | 334 | 92 | 298 | B Chain B, X-Ray Crystal Structure Of Ngt-Bound Hexa |
PDB | 2gk1_G | 0.0000000001 | 374 | 468 | 409 | 500 | B Chain B, X-Ray Crystal Structure Of Ngt-Bound Hexa |
PDB | 2gk1_E | 4.99983e-42 | 125 | 334 | 92 | 298 | B Chain B, X-Ray Crystal Structure Of Ngt-Bound Hexa |
PDB | 2gk1_E | 0.0000000001 | 374 | 468 | 409 | 500 | B Chain B, X-Ray Crystal Structure Of Ngt-Bound Hexa |
PDB | 2gk1_C | 4.99983e-42 | 125 | 334 | 92 | 298 | B Chain B, X-Ray Crystal Structure Of Ngt-Bound Hexa |