Q96520 · PER12_ARATH
- ProteinPeroxidase 12
- GenePER12
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids358 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Removal of H2O2, oxidation of toxic reductants, biosynthesis and degradation of lignin, suberization, auxin catabolism, response to environmental stresses such as wounding, pathogen attack and oxidative stress. These functions might be dependent on each isozyme/isoform in each plant tissue.
Exhibits a Ca2+-pectate binding affinity which could be interpreted in vivo as a specificity to interact with the pectic structure of the cell wall.
Miscellaneous
There are 73 peroxidase genes in A.thaliana.
Catalytic activity
- 2 a phenolic donor + H2O2 = 2 a phenolic radical donor + 2 H2O
Cofactor
Protein has several cofactor binding sites:
Note: Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.
Note: Binds 2 calcium ions per subunit.
Features
Showing features for site, active site, binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Site | 80 | Transition state stabilizer | ||||
Sequence: R | ||||||
Active site | 84 | Proton acceptor | ||||
Sequence: H | ||||||
Binding site | 85 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 88 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: V | ||||||
Binding site | 90 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 92 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 94 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 183 | substrate | ||||
Sequence: P | ||||||
Binding site | 213 | Fe (UniProtKB | ChEBI) of heme b (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: H | ||||||
Binding site | 214 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 259 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 262 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 267 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | extracellular region | |
Cellular Component | mitochondrion | |
Cellular Component | plant-type cell wall | |
Cellular Component | plant-type vacuole | |
Cellular Component | plasmodesma | |
Molecular Function | heme binding | |
Molecular Function | lactoperoxidase activity | |
Molecular Function | metal ion binding | |
Biological Process | hydrogen peroxide catabolic process | |
Biological Process | response to oxidative stress |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended namePeroxidase 12
- EC number
- Short namesAtperox P12
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > malvids > Brassicales > Brassicaceae > Camelineae > Arabidopsis
Accessions
- Primary accessionQ96520
- Secondary accessions
Proteomes
Organism-specific databases
Genome annotation databases
PTM/Processing
Features
Showing features for signal, chain, disulfide bond, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-31 | |||||
Sequence: MTKAYSTRVLTFLILISLMAVTLNLFPTVEA | ||||||
Chain | PRO_0000023678 | 32-358 | Peroxidase 12 | |||
Sequence: KKRSRDAPIVKGLSWNFYQKACPKVENIIRKELKKVFKRDIGLAAAILRIHFHDCFVQGCEASVLLAGSASGPGEQSSIPNLTLRQQAFVVINNLRALVQKKCGQVVSCSDILALAARDSVVLSGGPDYAVPLGRRDSLAFASQETTLNNLPPPFFNASQLIADFANRNLNITDLVALSGGHTIGIAHCPSFTDRLYPNQDPTMNQFFANSLKRTCPTANSSNTQVNDIRSPDVFDNKYYVDLMNRQGLFTSDQDLFVDKRTRGIVESFAIDQQLFFDYFTVAMIKMGQMSVLTGTQGEIRSNCSARNTQSFMSVLEEGIEEAISMI | ||||||
Disulfide bond | 53↔134 | |||||
Sequence: CPKVENIIRKELKKVFKRDIGLAAAILRIHFHDCFVQGCEASVLLAGSASGPGEQSSIPNLTLRQQAFVVINNLRALVQKKC | ||||||
Disulfide bond | 86↔91 | |||||
Sequence: CFVQGC | ||||||
Disulfide bond | 140↔335 | |||||
Sequence: CSDILALAARDSVVLSGGPDYAVPLGRRDSLAFASQETTLNNLPPPFFNASQLIADFANRNLNITDLVALSGGHTIGIAHCPSFTDRLYPNQDPTMNQFFANSLKRTCPTANSSNTQVNDIRSPDVFDNKYYVDLMNRQGLFTSDQDLFVDKRTRGIVESFAIDQQLFFDYFTVAMIKMGQMSVLTGTQGEIRSNC | ||||||
Glycosylation | 188 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 202 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 220↔247 | |||||
Sequence: CPSFTDRLYPNQDPTMNQFFANSLKRTC | ||||||
Glycosylation | 251 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 334 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Expressed in roots and leaves.
Induction
Induced either by incompatible fungal pathogen attack, or by methyl jasmonate, a plant defense-related signaling molecule.
Developmental stage
Expressed in the first stage of developing seeds.
Gene expression databases
Interaction
Protein-protein interaction databases
Structure
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length358
- Mass (Da)39,559
- Last updated1997-02-01 v1
- ChecksumB8F18C56CFCB4CB2
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 257 | in Ref. 1; CAA66962 | ||||
Sequence: V → G |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
X98318 EMBL· GenBank· DDBJ | CAA66962.1 EMBL· GenBank· DDBJ | mRNA | ||
X98773 EMBL· GenBank· DDBJ | CAA67309.1 EMBL· GenBank· DDBJ | mRNA | ||
AC012654 EMBL· GenBank· DDBJ | AAF43221.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AC016163 EMBL· GenBank· DDBJ | AAG51834.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CP002684 EMBL· GenBank· DDBJ | AEE35217.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF334732 EMBL· GenBank· DDBJ | AAG50110.1 EMBL· GenBank· DDBJ | mRNA | ||
BT000715 EMBL· GenBank· DDBJ | AAN31858.1 EMBL· GenBank· DDBJ | mRNA | ||
AY087964 EMBL· GenBank· DDBJ | AAM65511.1 EMBL· GenBank· DDBJ | mRNA |