| Basic Information | |
|---|---|
| Species | Zea mays |
| Cazyme ID | GRMZM2G120517_T01 |
| Family | AA2 |
| Protein Properties | Length: 235 Molecular Weight: 25590.2 Isoelectric Point: 9.3245 |
| Chromosome | Chromosome/Scaffold: 2 Start: 49721009 End: 49733233 |
| Description | thylakoidal ascorbate peroxidase |
| 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 | 16 | 171 | 0 |
| RELLRTTHSHPILVRLGWHDAGTYDKNIEEWPQRGGANGSLRFDVELKHGANAGLINALKLIQPIKDKYPSITYADLFQLASATAIEEAGGPKIPMKYGR VDVTGPEQCPPEGKLPDAGPSSPADHLREVFYRMGLNDKEIVALSGAHTLGRSRPE | |||
| Full Sequence |
|---|
| Protein Sequence Length: 235 Download |
| MASDAAQVKA AREDIRELLR TTHSHPILVR LGWHDAGTYD KNIEEWPQRG GANGSLRFDV 60 ELKHGANAGL INALKLIQPI KDKYPSITYA DLFQLASATA IEEAGGPKIP MKYGRVDVTG 120 PEQCPPEGKL PDAGPSSPAD HLREVFYRMG LNDKEIVALS GAHTLGRSRP ERSGWGKPET 180 KYTVCSYLLY VRCKAGTPAR KSVLSMNCSI RCLYQGLHST TTTKTFSPKQ VGIG* 240 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
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| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| PLN02364 | PLN02364 | 5.0e-48 | 8 | 175 | 169 | + L-ascorbate peroxidase 1 | ||
| PLN02879 | PLN02879 | 4.0e-48 | 8 | 175 | 168 | + L-ascorbate peroxidase | ||
| pfam00141 | peroxidase | 2.0e-48 | 11 | 164 | 162 | + Peroxidase. | ||
| PLN02608 | PLN02608 | 4.0e-66 | 6 | 181 | 176 | + L-ascorbate peroxidase | ||
| cd00691 | ascorbate_peroxidase | 1.0e-110 | 1 | 181 | 181 | + 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 | ACN31633.1 | 0 | 1 | 234 | 1 | 234 | unknown [Zea mays] |
| EMBL | CAH67301.1 | 0 | 7 | 183 | 88 | 264 | OSIGBa0102D10.4 [Oryza sativa (indica cultivar-group)] |
| RefSeq | NP_001052844.1 | 0 | 5 | 183 | 89 | 267 | Os04g0434800 [Oryza sativa (japonica cultivar-group)] |
| RefSeq | NP_001132683.1 | 0 | 1 | 183 | 65 | 247 | hypothetical protein LOC100194161 [Zea mays] |
| RefSeq | XP_002447862.1 | 0 | 2 | 183 | 71 | 252 | hypothetical protein SORBIDRAFT_06g017080 [Sorghum bicolor] |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 1iyn_A | 0 | 2 | 183 | 2 | 183 | A Chain A, Crystal Structure Of Chloroplastic Ascorbate Peroxidase From Tobacco Plants And Structural Insights For Its Instability |
| PDB | 1apx_D | 3.9937e-43 | 8 | 180 | 15 | 179 | A Chain A, Crystal Structure Of Recombinant Ascorbate Peroxidase |
| PDB | 1apx_C | 3.9937e-43 | 8 | 180 | 15 | 179 | A Chain A, Crystal Structure Of Recombinant Ascorbate Peroxidase |
| PDB | 1apx_B | 3.9937e-43 | 8 | 180 | 15 | 179 | A Chain A, Crystal Structure Of Recombinant Ascorbate Peroxidase |
| PDB | 1apx_A | 3.9937e-43 | 8 | 180 | 15 | 179 | A Chain A, Crystal Structure Of Recombinant Ascorbate Peroxidase |
| Hydropathy |
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