Basic Information | |
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Species | Linum usitatissimum |
Cazyme ID | Lus10025680 |
Family | AA2 |
Protein Properties | Length: 435 Molecular Weight: 47374.6 Isoelectric Point: 8.0225 |
Chromosome | Chromosome/Scaffold: 145 Start: 952914 End: 956409 |
Description | thylakoidal ascorbate peroxidase |
View CDS |
External Links |
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CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
AA2 | 114 | 357 | 0 |
KSKFCHPILVRLGWHDAGTYNKDIEEFPMRGGANGSLRFDIELKHGANAGLVNALSLLQPIKEKYSGVTYADLFQLASATAIEEAGGPKIPMKYGRVDVS APEECPEEGRLPDAGPPSPADHLRKVFYRMGLNDKEIVALSGAHTLGRSRPDRSGWGKPETKYTKDGPGAPGGQSWTAEWLKFDNSYFKDIKAQIDEDLL VLPTDAAIFEDPSFKVYAEKYAEDQDAFFKDYAEAHAKLSNLGS |
Full Sequence |
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Protein Sequence Length: 435 Download |
MAHCPSHLQL SKSPQHHSPP PPFQMASSTL STAAAATSSR LLLPSSSTTA RAHIRQHLST 60 SSTHGFSPLK CIRSSPLPPF RAFSNQRRPL SAVAAASDPA QLKSAREDIK EILKSKFCHP 120 ILVRLGWHDA GTYNKDIEEF PMRGGANGSL RFDIELKHGA NAGLVNALSL LQPIKEKYSG 180 VTYADLFQLA SATAIEEAGG PKIPMKYGRV DVSAPEECPE EGRLPDAGPP SPADHLRKVF 240 YRMGLNDKEI VALSGAHTLG RSRPDRSGWG KPETKYTKDG PGAPGGQSWT AEWLKFDNSY 300 FKDIKAQIDE DLLVLPTDAA IFEDPSFKVY AEKYAEDQDA FFKDYAEAHA KLSNLGSKFD 360 PPEGIVLDGV QGEKFVAANY SYGKREFSDS MKQKMRAEYE AIGGSPSKAL SSNYFLNIII 420 VISVLAVLTY LFGN* |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
pfam00141 | peroxidase | 3.0e-48 | 105 | 337 | 241 | + Peroxidase. | ||
PLN02879 | PLN02879 | 8.0e-66 | 102 | 356 | 255 | + L-ascorbate peroxidase | ||
PLN02364 | PLN02364 | 3.0e-66 | 102 | 356 | 256 | + L-ascorbate peroxidase 1 | ||
PLN02608 | PLN02608 | 2.0e-95 | 100 | 362 | 265 | + L-ascorbate peroxidase | ||
cd00691 | ascorbate_peroxidase | 3.0e-146 | 93 | 360 | 272 | + 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 | AAS55852.1 | 0 | 70 | 413 | 35 | 391 | chloroplast thylakoid-bound ascorbate peroxidase [Vigna unguiculata] |
GenBank | AAY89389.1 | 0 | 25 | 410 | 1 | 397 | thylakoid-bound ascorbate peroxidase 6 [Solanum lycopersicum] |
RefSeq | XP_002285865.1 | 0 | 90 | 413 | 82 | 413 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002300978.1 | 0 | 70 | 434 | 45 | 400 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002307442.1 | 0 | 95 | 412 | 1 | 318 | predicted protein [Populus trichocarpa] |
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 | 95 | 384 | 1 | 294 | A Chain A, Crystal Structure Of Chloroplastic Ascorbate Peroxidase From Tobacco Plants And Structural Insights For Its Instability |
PDB | 1apx_D | 0 | 102 | 356 | 15 | 245 | A Chain A, Crystal Structure Of Recombinant Ascorbate Peroxidase |
PDB | 1apx_C | 0 | 102 | 356 | 15 | 245 | A Chain A, Crystal Structure Of Recombinant Ascorbate Peroxidase |
PDB | 1apx_B | 0 | 102 | 356 | 15 | 245 | A Chain A, Crystal Structure Of Recombinant Ascorbate Peroxidase |
PDB | 1apx_A | 0 | 102 | 356 | 15 | 245 | A Chain A, Crystal Structure Of Recombinant Ascorbate Peroxidase |