Basic Information | |
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Species | Selaginella moellendorffii |
Cazyme ID | 270176 |
Family | AA2 |
Protein Properties | Length: 251 Molecular Weight: 27564.4 Isoelectric Point: 5.8229 |
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 | 27 | 246 | 0 |
IAEKNCAPLMLRLAWHSAGTYDCQSKTGGPFGTMKLAEELGHTANNGLDIAVKLLQPIKDQFPILSYGDFYQLAGVVAVEVTGGPEIPFHPGRVDKPTCP MEGRLPDATKGADHLRDVFVKHMGLTDKDIVALSGGHTLGRAHKERSGFEGPWTHNPLQFDNSYFTILLSGEQEGILTLPTDKVLVEDPSFRPLVELYAK DEEAFFKDYTEAHLKLSELG |
Full Sequence |
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Protein Sequence Length: 251 Download |
MGKSYPAVSE EYKAAVEKAK RKLRGFIAEK NCAPLMLRLA WHSAGTYDCQ SKTGGPFGTM 60 KLAEELGHTA NNGLDIAVKL LQPIKDQFPI LSYGDFYQLA GVVAVEVTGG PEIPFHPGRV 120 DKPTCPMEGR LPDATKGADH LRDVFVKHMG LTDKDIVALS GGHTLGRAHK ERSGFEGPWT 180 HNPLQFDNSY FTILLSGEQE GILTLPTDKV LVEDPSFRPL VELYAKDEEA FFKDYTEAHL 240 KLSELGFAEE * |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
cd00314 | plant_peroxidase_like | 2.0e-55 | 17 | 244 | 256 | + 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. | ||
PLN02879 | PLN02879 | 1.0e-136 | 1 | 250 | 250 | + L-ascorbate peroxidase | ||
PLN02364 | PLN02364 | 4.0e-137 | 1 | 247 | 247 | + L-ascorbate peroxidase 1 | ||
PLN02608 | PLN02608 | 1.0e-144 | 6 | 247 | 242 | + L-ascorbate peroxidase | ||
cd00691 | ascorbate_peroxidase | 8.0e-151 | 5 | 250 | 254 | + 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 - NR Download unfiltered results here | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
GenBank | AAA86689.1 | 0 | 1 | 249 | 1 | 249 | ascorbate peroxidase [Nicotiana tabacum] |
GenBank | ABX79340.1 | 0 | 1 | 249 | 1 | 248 | cytosolic ascorbate peroxidase [Vitis vinifera] |
GenBank | ACB45429.3 | 0 | 1 | 249 | 1 | 249 | ascorbate peroxidase [Camellia sinensis] |
DDBJ | BAA12918.1 | 0 | 1 | 249 | 1 | 249 | cytosolic ascorbate peroxidase [Nicotiana tabacum] |
EMBL | CBI32625.1 | 0 | 1 | 249 | 1 | 248 | unnamed protein product [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 | 2xj6_A | 0 | 2 | 249 | 1 | 248 | A Chain A, The Structure Of Endoglucanase From Termite, Nasutitermes Takasagoensis, At Ph 2.5. |
PDB | 2xih_A | 0 | 2 | 249 | 1 | 248 | A Chain A, The Structure Of Endoglucanase From Termite, Nasutitermes Takasagoensis, At Ph 2.5. |
PDB | 2xif_A | 0 | 2 | 249 | 1 | 248 | A Chain A, The Structure Of Ascorbate Peroxidase Compound Ii |
PDB | 2xi6_A | 0 | 2 | 249 | 1 | 248 | A Chain A, The Structure Of Ascorbate Peroxidase Compound Ii |
PDB | 1apx_D | 0 | 2 | 249 | 1 | 248 | A Chain A, Crystal Structure Of Recombinant Ascorbate Peroxidase |
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 |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
FE436893 | 250 | 2 | 251 | 0 |
DN839337 | 251 | 1 | 251 | 0 |
FE468290 | 248 | 1 | 248 | 0 |
FE474871 | 246 | 1 | 246 | 0 |
FE480822 | 245 | 1 | 245 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
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