| Basic Information | |
|---|---|
| Species | Zea mays |
| Cazyme ID | GRMZM2G095404_T02 |
| Family | AA2 |
| Protein Properties | Length: 367 Molecular Weight: 40285.8 Isoelectric Point: 4.835 |
| Chromosome | Chromosome/Scaffold: 6 Start: 118788833 End: 118790352 |
| Description | Peroxidase superfamily protein |
| View CDS | |
| External Links |
|---|
| NCBI Taxonomy |
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| AA2 | 59 | 331 | 0 |
| VEHVVRTEMECAVRADTRNAALMLRLHFHDCFVQGCDGSVLLDDTATMIGEKQAEQNVNSLKGFDLVDKIKEKLEAECPGTVSCADLLAIAARDAVVLVG GPYWDVPVGRLDSKKASLDLANSDIPTAQQGLLTLIAKFWEKGLDATDMVALVGSHTIGFARCENFRDRIYGDFEMTSKYNPSSEAYLSKLKEVCPRDGG DDNISAMDSHTSDVFDNAYFETLIKGEGLLNSDQAMWSSIAGYSTSDTVNKYWADPEAFFKQFSDSMVKMGNI | |||
| Full Sequence |
|---|
| Protein Sequence Length: 367 Download |
| MLRMGRASAT AGVLRFVRAF ALCVATACLL LAAGMPSPVA AQDPSKLSLQ YYSKTCPNVE 60 HVVRTEMECA VRADTRNAAL MLRLHFHDCF VQGCDGSVLL DDTATMIGEK QAEQNVNSLK 120 GFDLVDKIKE KLEAECPGTV SCADLLAIAA RDAVVLVGGP YWDVPVGRLD SKKASLDLAN 180 SDIPTAQQGL LTLIAKFWEK GLDATDMVAL VGSHTIGFAR CENFRDRIYG DFEMTSKYNP 240 SSEAYLSKLK EVCPRDGGDD NISAMDSHTS DVFDNAYFET LIKGEGLLNS DQAMWSSIAG 300 YSTSDTVNKY WADPEAFFKQ FSDSMVKMGN ITNPRRRGQE DLQICQHIGY DNIYRMLETA 360 GETRWL* 420 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| cd00691 | ascorbate_peroxidase | 2.0e-14 | 70 | 328 | 279 | + 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. | ||
| cd00314 | plant_peroxidase_like | 3.0e-30 | 61 | 330 | 299 | + 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. | ||
| pfam00141 | peroxidase | 3.0e-62 | 63 | 216 | 154 | + Peroxidase. | ||
| PLN03030 | PLN03030 | 3.0e-72 | 51 | 331 | 286 | + cationic peroxidase; Provisional | ||
| cd00693 | secretory_peroxidase | 4.0e-145 | 46 | 331 | 287 | + 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. | ||
| 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 | ACG43658.1 | 0 | 4 | 366 | 1 | 364 | hypothetical protein [Zea mays] |
| GenBank | ADD60696.1 | 0 | 18 | 348 | 9 | 333 | putative peroxidase 49 precursor [Oryza officinalis] |
| EMBL | CAM31942.1 | 0 | 18 | 348 | 9 | 332 | hypothetical protein [Lolium perenne] |
| RefSeq | NP_001130123.1 | 0 | 1 | 366 | 1 | 366 | hypothetical protein LOC100191217 [Zea mays] |
| RefSeq | XP_002438233.1 | 0 | 12 | 348 | 5 | 342 | hypothetical protein SORBIDRAFT_10g010040 [Sorghum bicolor] |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 1qo4_A | 0 | 46 | 332 | 2 | 287 | A Chain A, Crystal Structure Of Human Glcat-P Apo Form |
| PDB | 1pa2_A | 0 | 46 | 332 | 2 | 287 | A Chain A, Arabidopsis Thaliana Peroxidase A2 |
| PDB | 1sch_B | 0 | 46 | 332 | 1 | 277 | A Chain A, Peanut Peroxidase |
| PDB | 1sch_A | 0 | 46 | 332 | 1 | 277 | A Chain A, Peanut Peroxidase |
| PDB | 1qgj_B | 0 | 46 | 333 | 1 | 285 | A Chain A, Arabidopsis Thaliana Peroxidase N |
