Q93V93 · PER44_ARATH
- ProteinPeroxidase 44
- GenePER44
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids310 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score4/5
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.
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 | 58 | Transition state stabilizer | ||||
Sequence: R | ||||||
Active site | 62 | Proton acceptor | ||||
Sequence: H | ||||||
Binding site | 63 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 66 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: V | ||||||
Binding site | 68 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 70 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 72 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 156 | substrate | ||||
Sequence: P | ||||||
Binding site | 187 | Fe (UniProtKB | ChEBI) of heme b (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: H | ||||||
Binding site | 188 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 229 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 232 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 237 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | extracellular region | |
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 44
- EC number
- Short namesAtperox P44
- 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 accessionQ93V93
- Secondary accessions
Proteomes
Organism-specific databases
Genome annotation databases
Subcellular Location
PTM/Processing
Features
Showing features for signal, chain, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-20 | |||||
Sequence: MRSITALFFLFCFLAPSALA | ||||||
Chain | PRO_0000023710 | 21-310 | Peroxidase 44 | |||
Sequence: QLRTGFYSRSCPRAESIVASVVANRFRSDKSITAAFLRMQFHDCFVRGCDASLLIDPRPGRPSEKSTGPNASVRGYEIIDEAKRQLEAACPRTVSCADIVTLATRDSVALAGGPRFSVPTGRRDGLRSNPNDVNLPGPTIPVSASIQLFAAQGMNTNDMVTLIGGGHSVGVAHCSLFQDRLSDRAMEPSLKSSLRRKCSSPNDPTTFLDQKTSFTVDNAIYGEIRRQRGILRIDQNLGLDRSTSGIVSGYASSNTLFRKRFAEALVKMGTIKVLTGRSGEIRRNCRVFNN | ||||||
Disulfide bond | 31↔110 | |||||
Sequence: CPRAESIVASVVANRFRSDKSITAAFLRMQFHDCFVRGCDASLLIDPRPGRPSEKSTGPNASVRGYEIIDEAKRQLEAAC | ||||||
Disulfide bond | 64↔69 | |||||
Sequence: CFVRGC | ||||||
Disulfide bond | 116↔305 | |||||
Sequence: CADIVTLATRDSVALAGGPRFSVPTGRRDGLRSNPNDVNLPGPTIPVSASIQLFAAQGMNTNDMVTLIGGGHSVGVAHCSLFQDRLSDRAMEPSLKSSLRRKCSSPNDPTTFLDQKTSFTVDNAIYGEIRRQRGILRIDQNLGLDRSTSGIVSGYASSNTLFRKRFAEALVKMGTIKVLTGRSGEIRRNC | ||||||
Disulfide bond | 194↔218 | |||||
Sequence: CSLFQDRLSDRAMEPSLKSSLRRKC |
Keywords
- PTM
Proteomic databases
Expression
Gene expression databases
Interaction
Protein-protein interaction databases
Structure
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length310
- Mass (Da)33,806
- Last updated2001-12-01 v1
- ChecksumE14CEB2BA47B5550
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A1P8B428 | A0A1P8B428_ARATH | At4g26010 | 338 |
Sequence caution
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF452386 EMBL· GenBank· DDBJ | AAL40850.1 EMBL· GenBank· DDBJ | mRNA | ||
AL049483 EMBL· GenBank· DDBJ | CAB39666.1 EMBL· GenBank· DDBJ | Genomic DNA | Sequence problems. | |
AL161564 EMBL· GenBank· DDBJ | CAB79456.1 EMBL· GenBank· DDBJ | Genomic DNA | Sequence problems. | |
CP002687 EMBL· GenBank· DDBJ | AEE85144.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF412066 EMBL· GenBank· DDBJ | AAL06519.1 EMBL· GenBank· DDBJ | mRNA | ||
AF428430 EMBL· GenBank· DDBJ | AAL16199.1 EMBL· GenBank· DDBJ | mRNA | ||
AY090260 EMBL· GenBank· DDBJ | AAL90921.1 EMBL· GenBank· DDBJ | mRNA |