Basic Information | |
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Species | Arabidopsis lyrata |
Cazyme ID | 489772 |
Family | AA2 |
Protein Properties | Length: 346 Molecular Weight: 38175.7 Isoelectric Point: 8.5658 |
Chromosome | Chromosome/Scaffold: 6 Start: 18893342 End: 18895097 |
Description | Peroxidase superfamily protein |
View CDS |
External Links |
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NCBI Taxonomy |
Plaza |
CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
AA2 | 34 | 308 | 0 |
QVFDIVTNTIVNALRSDPRIAASIIRLHFHDCFVNGCDASILLDNTTSFRTEKDAFGNANSARGFDVIDKMKAAVEKACPRTVSCADLLAIAAQESVVLA GGPSWRVPNGRRDSLRGFMDLANNNLPAPSFTLKQLKDRFKNVGLDRASDLVALSGGHTFGKNQCRFIMDRLYNFSDTGLPDPTLDKSYLTTLRKQCPRN GNQSVLVDFDLRTPTLFDNKYYVNLKENKGLIQSDQELFSSPDASDTLPLVREFADGQGKFFDAFAKAMIRMSSL |
Full Sequence |
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Protein Sequence Length: 346 Download |
MHSSLIKLGF LLLLQVSLSH AQLSPSFYDK TCPQVFDIVT NTIVNALRSD PRIAASIIRL 60 HFHDCFVNGC DASILLDNTT SFRTEKDAFG NANSARGFDV IDKMKAAVEK ACPRTVSCAD 120 LLAIAAQESV VLAGGPSWRV PNGRRDSLRG FMDLANNNLP APSFTLKQLK DRFKNVGLDR 180 ASDLVALSGG HTFGKNQCRF IMDRLYNFSD TGLPDPTLDK SYLTTLRKQC PRNGNQSVLV 240 DFDLRTPTLF DNKYYVNLKE NKGLIQSDQE LFSSPDASDT LPLVREFADG QGKFFDAFAK 300 AMIRMSSLSP LTGKQGEIRL NCRVVNSKPR IMDVVEDAIK FASSM* |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
cd00691 | ascorbate_peroxidase | 6.0e-19 | 30 | 308 | 300 | + 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-37 | 37 | 307 | 301 | + 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-64 | 39 | 192 | 154 | + Peroxidase. | ||
PLN03030 | PLN03030 | 2.0e-84 | 27 | 326 | 307 | + cationic peroxidase; Provisional | ||
cd00693 | secretory_peroxidase | 4.0e-167 | 25 | 325 | 301 | + 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 | |
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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 | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
GenBank | AAM97030.1 | 0 | 14 | 345 | 15 | 346 | peroxidase C2 precursor-like protein [Arabidopsis thaliana] |
EMBL | CAA66959.1 | 0 | 3 | 345 | 12 | 352 | peroxidase [Arabidopsis thaliana] |
RefSeq | NP_192617.1 | 0 | 14 | 345 | 15 | 346 | peroxidase, putative [Arabidopsis thaliana] |
RefSeq | NP_192618.1 | 0 | 15 | 345 | 16 | 346 | peroxidase, putative [Arabidopsis thaliana] |
Swiss-Prot | P17179 | 0 | 16 | 345 | 19 | 347 | PER2_ARMRU RecName: Full=Peroxidase C2; Flags: Precursor |
Annotations - PDB Download unfiltered results here | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
PDB | 1w4y_A | 0 | 22 | 345 | 1 | 323 | A Chain A, Solution Structure Of The C-Terminal Domain Ole E 9 |
PDB | 1w4w_A | 0 | 22 | 345 | 1 | 323 | A Chain A, Ferric Horseradish Peroxidase C1a In Complex With Formate |
PDB | 7atj_A | 0 | 22 | 328 | 1 | 307 | A Chain A, Ferric Horseradish Peroxidase C1a In Complex With Formate |
PDB | 6atj_A | 0 | 22 | 328 | 1 | 307 | A Chain A, Recombinant Horseradish Peroxidase C Complex With Ferulic Acid |
PDB | 1h5m_A | 0 | 22 | 328 | 1 | 307 | A Chain A, Recombinant Horseradish Peroxidase C Complex With Ferulic Acid |