| Basic Information | |
|---|---|
| Species | Chlamydomonas reinhardtii |
| Cazyme ID | Cre06.g285150.t1.2 |
| Family | AA2 |
| Protein Properties | Length: 338 Molecular Weight: 35111.3 Isoelectric Point: 8.9738 |
| Chromosome | Chromosome/Scaffold: 6 Start: 5540720 End: 5544095 |
| Description | ascorbate peroxidase 6 |
| View CDS | |
| External Links |
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| NCBI Taxonomy |
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| AA2 | 110 | 332 | 0 |
| KNIPKTKTAVALRLAFHDAATFSAGAKDGGLNASIQYELDRPENFGLKRGWRIIEQVRADLKGTAAEGVVTDADLVALAGAFAVRLCGGPAIPLPIGRPV AAAARQDPPGRMPSENASAAELKANFAAKGLSVQEMVALSGAHTLGSKGFGDPVTFDNAYYVALLQKPWNNTKDAMASMIGLPSDHVLPDDPDCLPVIQR YAADQDLFFRDFSAAYIKMCGLG | |||
| Full Sequence |
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| Protein Sequence Length: 338 Download |
| MSTSVLSHRS LSNCTRHGNP RRACRVATHA KLRDLSQWRQ EGSGTSEPAV APELSRRAVL 60 KLGAALPALA AALAAATPPA LLLAPLPAAA EGPTLPSPAV AAALDKALAK NIPKTKTAVA 120 LRLAFHDAAT FSAGAKDGGL NASIQYELDR PENFGLKRGW RIIEQVRADL KGTAAEGVVT 180 DADLVALAGA FAVRLCGGPA IPLPIGRPVA AAARQDPPGR MPSENASAAE LKANFAAKGL 240 SVQEMVALSG AHTLGSKGFG DPVTFDNAYY VALLQKPWNN TKDAMASMIG LPSDHVLPDD 300 PDCLPVIQRY AADQDLFFRD FSAAYIKMCG LGVAGWA* 360 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| PLN02608 | PLN02608 | 4.0e-36 | 121 | 332 | 224 | + L-ascorbate peroxidase | ||
| cd00693 | secretory_peroxidase | 6.0e-38 | 121 | 333 | 252 | + Horseradish peroxidase and related secretory plant peroxidases. Secretory peroxidases belong to class III of the plant heme-dependent peroxidase superfamily. All members of the superfamily share a heme prosthetic group and catalyze a multistep oxidative reaction involving hydrogen peroxide as the electron acceptor. Class III peroxidases are found in the extracellular space or in the vacuole in plants where they have been implicated in hydrogen peroxide detoxification, auxin catabolism and lignin biosynthesis, and stress response. Class III peroxidases contain four conserved disulphide bridges and two conserved calcium binding sites. | ||
| pfam00141 | peroxidase | 4.0e-40 | 118 | 313 | 200 | + Peroxidase. | ||
| cd00314 | plant_peroxidase_like | 4.0e-53 | 121 | 328 | 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. | ||
| cd00691 | ascorbate_peroxidase | 2.0e-53 | 119 | 333 | 228 | + 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 | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| EMBL | CAL54759.1 | 0 | 99 | 332 | 28 | 266 | putative L-ascorbate peroxidase (ISS) [Ostreococcus tauri] |
| RefSeq | NP_194958.2 | 0 | 103 | 336 | 100 | 326 | APX6; L-ascorbate peroxidase/ heme binding / peroxidase [Arabidopsis thaliana] |
| RefSeq | XP_001419049.1 | 0 | 97 | 332 | 7 | 247 | predicted protein [Ostreococcus lucimarinus CCE9901] |
| RefSeq | XP_001695476.1 | 0 | 1 | 337 | 1 | 306 | L-ascorbate peroxidase [Chlamydomonas reinhardtii] |
| RefSeq | XP_002309628.1 | 0 | 104 | 336 | 109 | 334 | predicted protein [Populus trichocarpa] |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 2xj6_A | 1e-33 | 98 | 334 | 5 | 247 | A Chain A, Structural Basis For The Substrate Specificity Of The Feruloyl Esterase Domain Of The Cellulosomal Xylanase Z Of Clostridium Thermocellum |
| PDB | 2xih_A | 1e-33 | 98 | 334 | 5 | 247 | A Chain A, Structural Basis For The Substrate Specificity Of The Feruloyl Esterase Domain Of The Cellulosomal Xylanase Z Of Clostridium Thermocellum |
| PDB | 2xif_A | 1e-33 | 98 | 334 | 5 | 247 | A Chain A, The Structure Of Ascorbate Peroxidase Compound Ii |
| PDB | 2xi6_A | 1e-33 | 98 | 334 | 5 | 247 | A Chain A, The Structure Of Ascorbate Peroxidase Compound Ii |
| PDB | 2cl4_X | 1e-33 | 98 | 334 | 17 | 259 | X Chain X, Ascorbate Peroxidase R172a Mutant |
| Metabolic Pathways | |||
|---|---|---|---|
| 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 |
| Hydropathy |
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| EST Download unfiltered results here | ||||
|---|---|---|---|---|
| Hit | Length | Start | End | EValue |
| BI718422 | 199 | 1 | 199 | 0 |
| BE024394 | 194 | 1 | 194 | 0 |
| EX899603 | 225 | 112 | 336 | 0 |
| DK539912 | 225 | 112 | 336 | 0 |
| DW506209 | 225 | 112 | 336 | 0 |
| Sequence Alignments (This image is cropped. Click for full image.) |
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