| Basic Information | |
|---|---|
| Species | Zea mays |
| Cazyme ID | GRMZM2G006791_T01 |
| Family | AA2 |
| Protein Properties | Length: 463 Molecular Weight: 50324.9 Isoelectric Point: 5.4045 |
| Chromosome | Chromosome/Scaffold: 5 Start: 172391880 End: 172397063 |
| Description | thylakoidal ascorbate peroxidase |
| View CDS | |
| External Links |
|---|
| NCBI Taxonomy |
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| AA2 | 84 | 350 | 0 |
| KELLKSTYCHPIMVRLGWHDSGTYDKNIKDWPQRGGANGSLRFDAELSHGANAGLINALKLIQPIKDKYPGITYADLFQLASATAIEEAGGPKIPMKYGR VDVTAAEQCPPEGRLPDAGPRDPAEHLREVFYRMGLDDKEIVALSGAHTLGRARPDRSGWGKLETKYTKDGPGEPGGQSWTVEWLKFDNSYFKEMKLFFL NEIQDMKFLSQLPWKEQKEQDLLVLPTDAALFEDPSFKVYAEKYAEDQEAFFKDYGEAHAKLSDLGA | |||
| Full Sequence |
|---|
| Protein Sequence Length: 463 Download |
| MAERLAASLL PAASPSPSAR RATVAAAAAA SFPSPCSARA GLRLRSRPPL FSQKAAGRGC 60 GLRVVRCMAA SDAVQLKAAR EDIKELLKST YCHPIMVRLG WHDSGTYDKN IKDWPQRGGA 120 NGSLRFDAEL SHGANAGLIN ALKLIQPIKD KYPGITYADL FQLASATAIE EAGGPKIPMK 180 YGRVDVTAAE QCPPEGRLPD AGPRDPAEHL REVFYRMGLD DKEIVALSGA HTLGRARPDR 240 SGWGKLETKY TKDGPGEPGG QSWTVEWLKF DNSYFKEMKL FFLNEIQDMK FLSQLPWKEQ 300 KEQDLLVLPT DAALFEDPSF KVYAEKYAED QEAFFKDYGE AHAKLSDLGA KFDPPEGFSL 360 DDDTCSSPSD EKTEEPTLVA VGAAVATATA DDNNGAAPQP EPFIAANYSY GKRELSDAMK 420 QKIRAEYEGF GGSPDKPMQS NYFLNIMILI AGLAFLTSLL GN* 480 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| cd00314 | plant_peroxidase_like | 6.0e-48 | 96 | 346 | 257 | + 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. | ||
| PLN02879 | PLN02879 | 5.0e-62 | 76 | 349 | 274 | + L-ascorbate peroxidase | ||
| PLN02364 | PLN02364 | 5.0e-64 | 76 | 349 | 275 | + L-ascorbate peroxidase 1 | ||
| PLN02608 | PLN02608 | 2.0e-97 | 68 | 355 | 293 | + L-ascorbate peroxidase | ||
| cd00691 | ascorbate_peroxidase | 2.0e-144 | 69 | 353 | 285 | + 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 | AAS80158.1 | 0 | 1 | 462 | 1 | 443 | thylakoid ascorbate peroxidase [Triticum aestivum] |
| GenBank | ACF88425.1 | 0 | 1 | 462 | 1 | 451 | unknown [Zea mays] |
| RefSeq | NP_001047111.1 | 0 | 1 | 462 | 1 | 478 | Os02g0553200 [Oryza sativa (japonica cultivar-group)] |
| RefSeq | NP_001149509.1 | 0 | 1 | 462 | 1 | 462 | thylakoid-bound ascorbate peroxidase APx8 [Zea mays] |
| RefSeq | XP_002453976.1 | 0 | 1 | 462 | 1 | 451 | hypothetical protein SORBIDRAFT_04g022560 [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 | 69 | 412 | 1 | 294 | A Chain A, Crystal Structure Of Chloroplastic Ascorbate Peroxidase From Tobacco Plants And Structural Insights For Its Instability |
| PDB | 2xj6_A | 0 | 76 | 349 | 15 | 245 | A Chain A, Crystal Structure Of Chloroplastic Ascorbate Peroxidase From Tobacco Plants And Structural Insights For Its Instability |
| PDB | 2xih_A | 0 | 76 | 349 | 15 | 245 | A Chain A, Crystal Structure Of Chloroplastic Ascorbate Peroxidase From Tobacco Plants And Structural Insights For Its Instability |
| PDB | 2xif_A | 0 | 76 | 349 | 15 | 245 | A Chain A, The Structure Of Ascorbate Peroxidase Compound Ii |
| PDB | 2xi6_A | 0 | 76 | 349 | 15 | 245 | A Chain A, The Structure Of Ascorbate Peroxidase Compound Ii |
