Basic Information | |
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Species | Physcomitrella patens |
Cazyme ID | Pp1s152_82V6.2 |
Family | AA2 |
Protein Properties | Length: 245 Molecular Weight: 26927.1 Isoelectric Point: 7.7955 |
Chromosome | Chromosome/Scaffold: 152 Start: 438048 End: 442618 |
Description | ascorbate peroxidase 1 |
View CDS |
External Links |
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NCBI Taxonomy |
Plaza |
CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
AA2 | 16 | 225 | 0 |
IEKARRKIRGMVAEKNCAPIILRLAWHGSGTYDQESKTGGPLGTIRFGQELAHGANAGLDIAVNLLQPIKEQFPELSYADFYTLAGVVAVEVTGGPTIPF HPGRKDHETCPVEGRLPDATKGLDHLRCVFTKQMGLTDKDIVVLSGAHTLGRCHKDRSGFEGAWTPNPLRFDNSYFQVLLEGEKDGLIMLPSDKALLDEP KTRELVELYA |
Full Sequence |
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Protein Sequence Length: 245 Download |
MAKSYPNVSE KYAALIEKAR RKIRGMVAEK NCAPIILRLA WHGSGTYDQE SKTGGPLGTI 60 RFGQELAHGA NAGLDIAVNL LQPIKEQFPE LSYADFYTLA GVVAVEVTGG PTIPFHPGRK 120 DHETCPVEGR LPDATKGLDH LRCVFTKQMG LTDKDIVVLS GAHTLGRCHK DRSGFEGAWT 180 PNPLRFDNSY FQVLLEGEKD GLIMLPSDKA LLDEPKTREL VELYAKVCAV FCLVVTWLCR 240 KKSE* |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
cd00314 | plant_peroxidase_like | 1.0e-49 | 24 | 231 | 235 | + 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 | 3.0e-115 | 3 | 225 | 223 | + L-ascorbate peroxidase | ||
PLN02364 | PLN02364 | 3.0e-121 | 1 | 225 | 225 | + L-ascorbate peroxidase 1 | ||
PLN02608 | PLN02608 | 4.0e-122 | 6 | 226 | 221 | + L-ascorbate peroxidase | ||
cd00691 | ascorbate_peroxidase | 2.0e-140 | 5 | 226 | 230 | + 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. |
Gene Ontology | |
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GO Term | Description |
GO:0004601 | peroxidase activity |
GO:0006979 | response to oxidative stress |
GO:0020037 | heme binding |
GO:0055114 | oxidation-reduction process |
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 | AAC08576.1 | 0 | 1 | 244 | 1 | 244 | ascorbate peroxidase [Zantedeschia aethiopica] |
GenBank | AAS19934.1 | 0 | 1 | 225 | 1 | 225 | ascorbate peroxidase [Rehmannia glutinosa] |
GenBank | ACV92696.1 | 0 | 1 | 231 | 1 | 231 | APX [Brassica rapa subsp. pekinensis] |
RefSeq | XP_001772538.1 | 0 | 1 | 226 | 1 | 226 | predicted protein [Physcomitrella patens subsp. patens] |
RefSeq | XP_001772540.1 | 0 | 25 | 226 | 1 | 202 | predicted protein [Physcomitrella patens subsp. patens] |
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 | 1apx_D | 0 | 3 | 231 | 2 | 230 | A Chain A, Crystal Structure Of Recombinant Ascorbate Peroxidase |
PDB | 1apx_C | 0 | 3 | 231 | 2 | 230 | A Chain A, Crystal Structure Of Recombinant Ascorbate Peroxidase |
PDB | 1apx_B | 0 | 3 | 231 | 2 | 230 | A Chain A, Crystal Structure Of Recombinant Ascorbate Peroxidase |
PDB | 1apx_A | 0 | 3 | 231 | 2 | 230 | A Chain A, Crystal Structure Of Recombinant Ascorbate Peroxidase |
PDB | 2xj6_A | 0 | 3 | 244 | 2 | 243 | A Chain A, Crystal Structure Of Recombinant Ascorbate Peroxidase |
Metabolic Pathways | |||
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Pathway Name | Reaction | EC | Protein Name |
ascorbate glutathione cycle | RXN-3521 | - | L-ascorbate peroxidase |
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 |
FC448009 | 226 | 1 | 226 | 0 |
FC394778 | 226 | 1 | 226 | 0 |
BJ946123 | 226 | 1 | 226 | 0 |
FC365977 | 226 | 1 | 226 | 0 |
FC389948 | 226 | 1 | 226 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
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