Basic Information | |
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Species | Selaginella moellendorffii |
Cazyme ID | 156990 |
Family | AA2 |
Protein Properties | Length: 349 Molecular Weight: 37802.1 Isoelectric Point: 8.9163 |
View CDS |
External Links |
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NCBI Taxonomy |
CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
AA2 | 91 | 333 | 0 |
KMHCNPIVIRLGWHDAGTYDKNISEWPKCGGANGSLRFPIELEHGANAGLINALKLLNPVKEKFTAVSYADLFQLASATAIEMAGGPRIPMRYGRVDTVG PEQCPKEGNLPSAGPPNPSEHLRKVFHRMGLDDKDIVALSGAHTLGRSRPERSGWGKKETKYTKDGPGAPGGQSWTVEWLKFDNSYFKDIKEKRDEDLLV LPTDAVLFEDPGFKEHAELYAKDQDAFFKDYAQAHAKLSELGA |
Full Sequence |
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Protein Sequence Length: 349 Download |
MAMASARSIV FSGALLCKSL PAVTARLSIA AAPHRRLSSS GLSLRAACSR RIRTFAMSGS 60 GAAAVESSQR IASQLDQLVG AREAIKEVIT KMHCNPIVIR LGWHDAGTYD KNISEWPKCG 120 GANGSLRFPI ELEHGANAGL INALKLLNPV KEKFTAVSYA DLFQLASATA IEMAGGPRIP 180 MRYGRVDTVG PEQCPKEGNL PSAGPPNPSE HLRKVFHRMG LDDKDIVALS GAHTLGRSRP 240 ERSGWGKKET KYTKDGPGAP GGQSWTVEWL KFDNSYFKDI KEKRDEDLLV LPTDAVLFED 300 PGFKEHAELY AKDQDAFFKD YAQAHAKLSE LGAKFDPPQG IRIDESTS* |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
cd00314 | plant_peroxidase_like | 3.0e-45 | 83 | 330 | 271 | + Heme-dependent peroxidases similar to plant peroxidases. Along with animal peroxidases, these enzymes belong to a group of peroxidases containing a heme prosthetic group (ferriprotoporphyrin IX), which catalyzes a multistep oxidative reaction involving hydrogen peroxide as the electron acceptor. The plant peroxidase-like superfamily is found in all three kingdoms of life and carries out a variety of biosynthetic and degradative functions. Several sub-families can be identified. Class I includes intracellular peroxidases present in fungi, plants, archaea and bacteria, called catalase-peroxidases, that can exhibit both catalase and broad-spectrum peroxidase activities depending on the steady-state concentration of hydrogen peroxide. Catalase-peroxidases are typically comprised of two homologous domains that probably arose via a single gene duplication event. Class II includes ligninase and other extracellular fungal peroxidases, while class III is comprised of classic extracellular plant peroxidases, like horseradish peroxidase. | ||
PLN02364 | PLN02364 | 5.0e-65 | 82 | 332 | 252 | + L-ascorbate peroxidase 1 | ||
PLN02879 | PLN02879 | 4.0e-72 | 82 | 332 | 251 | + L-ascorbate peroxidase | ||
PLN02608 | PLN02608 | 6.0e-96 | 72 | 338 | 269 | + L-ascorbate peroxidase | ||
cd00691 | ascorbate_peroxidase | 2.0e-136 | 72 | 336 | 269 | + Ascorbate peroxidases and cytochrome C peroxidases. Ascorbate peroxidases are a subgroup of heme-dependent peroxidases of the plant superfamily that share a heme prosthetic group and catalyze a multistep oxidative reaction involving hydrogen peroxide as the electron acceptor. Along with related catalase-peroxidases, ascorbate peroxidases belong to class I of the plant superfamily. Ascorbate peroxidases are found in the chloroplasts and/or cytosol of algae and plants, where they have been shown to control the concentration of lethal hydrogen peroxide molecules. The yeast cytochrome c peroxidase is a divergent member of the family; it forms a complex with cytochrome c to catalyze the reduction of hydrogen peroxide to water. |
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 | 1iyn_A | 0 | 72 | 346 | 2 | 276 | A Chain A, Crystal Structure Of Chloroplastic Ascorbate Peroxidase From Tobacco Plants And Structural Insights For Its Instability |
PDB | 2xj6_A | 0 | 81 | 332 | 18 | 245 | A Chain A, Crystal Structure Of Chloroplastic Ascorbate Peroxidase From Tobacco Plants And Structural Insights For Its Instability |
PDB | 2xih_A | 0 | 81 | 332 | 18 | 245 | A Chain A, Crystal Structure Of Chloroplastic Ascorbate Peroxidase From Tobacco Plants And Structural Insights For Its Instability |
PDB | 2xif_A | 0 | 81 | 332 | 18 | 245 | A Chain A, The Structure Of Ascorbate Peroxidase Compound Ii |
PDB | 2xi6_A | 0 | 81 | 332 | 18 | 245 | A Chain A, The Structure Of Ascorbate Peroxidase Compound Ii |
Metabolic Pathways | |||
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Pathway Name | Reaction | EC | Protein Name |
L-ascorbate degradation III | RXN-12440 | EC-1.11.1.11 | L-ascorbate peroxidase |
L-ascorbate degradation V | RXN-12440 | EC-1.11.1.11 | L-ascorbate peroxidase |