| Basic Information | |
|---|---|
| Species | Thellungiella halophila |
| Cazyme ID | Thhalv10025686m |
| Family | AA2 |
| Protein Properties | Length: 331 Molecular Weight: 35811.9 Isoelectric Point: 8.9603 |
| Chromosome | Chromosome/Scaffold: 1 Start: 3287121 End: 3289113 |
| Description | ascorbate peroxidase 6 |
| View CDS | |
| External Links |
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| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| AA2 | 102 | 324 | 0 |
| MQNEIKKVVTKGKAAGVLRLVFHDAGTFELDDNTGGINGSIAYELERPENTGLKKSLKVLAKAKIKVDEIQPVSWADMISVAGSVAVSICGGPTIPVVLG RLDSTQPDPEDKLPPESLSASGLKECFKRKGFSTQELVALSGAHTLGSKGFGDPTVFDNAYYKILLAKPWTSASKMTSMVGLPSDHALVEDDECLRWVKR YAEDQDKFFQDFTNAYTKLVNSG | |||
| Full Sequence |
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| Protein Sequence Length: 331 Download |
| MTTTTTASLF ETSLSRCYSS SSSSSSFKFE SPAKTKTRLF SPATGNHVIR SVTACRIRCA 60 SDDPGSVFLS SRRKVVVLLS TMQLLSQSLP PNGNAAEIYQ LMQNEIKKVV TKGKAAGVLR 120 LVFHDAGTFE LDDNTGGING SIAYELERPE NTGLKKSLKV LAKAKIKVDE IQPVSWADMI 180 SVAGSVAVSI CGGPTIPVVL GRLDSTQPDP EDKLPPESLS ASGLKECFKR KGFSTQELVA 240 LSGAHTLGSK GFGDPTVFDN AYYKILLAKP WTSASKMTSM VGLPSDHALV EDDECLRWVK 300 RYAEDQDKFF QDFTNAYTKL VNSGAKWKML * 360 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| PLN02879 | PLN02879 | 1.0e-37 | 119 | 324 | 219 | + L-ascorbate peroxidase | ||
| pfam00141 | peroxidase | 3.0e-41 | 119 | 305 | 195 | + Peroxidase. | ||
| PLN02608 | PLN02608 | 2.0e-41 | 119 | 320 | 214 | + L-ascorbate peroxidase | ||
| cd00314 | plant_peroxidase_like | 5.0e-61 | 119 | 322 | 234 | + 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. | ||
| cd00691 | ascorbate_peroxidase | 2.0e-62 | 91 | 327 | 256 | + 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 | |
|---|---|
| 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 | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| GenBank | ACU18323.1 | 0 | 99 | 330 | 88 | 319 | unknown [Glycine max] |
| RefSeq | NP_194958.2 | 0 | 3 | 330 | 2 | 329 | APX6; L-ascorbate peroxidase/ heme binding / peroxidase [Arabidopsis thaliana] |
| RefSeq | XP_002282677.1 | 0 | 10 | 330 | 6 | 330 | PREDICTED: similar to APX6 (ASCORBATE PEROXIDASE 6); L-ascorbate peroxidase [Vitis vinifera] |
| RefSeq | XP_002309628.1 | 0 | 28 | 330 | 27 | 337 | predicted protein [Populus trichocarpa] |
| RefSeq | XP_002515511.1 | 0 | 17 | 330 | 5 | 328 | L-ascorbate peroxidase 1, cytosolic, putative [Ricinus communis] |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 1apx_D | 4e-36 | 118 | 324 | 35 | 245 | A Chain A, Crystal Structure Of Recombinant Ascorbate Peroxidase |
| PDB | 1apx_C | 4e-36 | 118 | 324 | 35 | 245 | A Chain A, Crystal Structure Of Recombinant Ascorbate Peroxidase |
| PDB | 1apx_B | 4e-36 | 118 | 324 | 35 | 245 | A Chain A, Crystal Structure Of Recombinant Ascorbate Peroxidase |
| PDB | 1apx_A | 4e-36 | 118 | 324 | 35 | 245 | A Chain A, Crystal Structure Of Recombinant Ascorbate Peroxidase |
| PDB | 2xj6_A | 3e-35 | 118 | 324 | 35 | 245 | A Chain A, Crystal Structure Of Recombinant Ascorbate Peroxidase |
| Hydropathy |
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| EST Download unfiltered results here | ||||
|---|---|---|---|---|
| Hit | Length | Start | End | EValue |
| CK120802 | 262 | 36 | 295 | 0 |
| EX899603 | 236 | 94 | 328 | 0 |
| DK539912 | 229 | 104 | 331 | 0 |
| EV107496 | 209 | 124 | 331 | 0 |
| BY825715 | 163 | 169 | 331 | 0 |
| Sequence Alignments (This image is cropped. Click for full image.) |
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