O04796 · PERN_IPOBA
- ProteinNeutral peroxidase
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids348 (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.
May contribute to protection against cold-induced oxidative stress.
Catalytic activity
- 2 a phenolic donor + H2O2 = 2 a phenolic radical donor + 2 H2O
Cofactor
Protein has several cofactor binding sites:
Note: Binds 2 calcium ions per subunit.
Note: Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.
Features
Showing features for site, active site, binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Site | 96 | Transition state stabilizer | ||||
Sequence: R | ||||||
Active site | 100 | Proton acceptor | ||||
Sequence: H | ||||||
Binding site | 101 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 104 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: V | ||||||
Binding site | 106 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 108 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 198 | substrate | ||||
Sequence: P | ||||||
Binding site | 228 | Fe (UniProtKB | ChEBI) of heme b (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: H | ||||||
Binding site | 229 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 269 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 271 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 276 | 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 nameNeutral peroxidase
- EC number
- Alternative names
Organism names
- Strain
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > asterids > lamiids > Solanales > Convolvulaceae > Ipomoeeae > Ipomoea
Accessions
- Primary accessionO04796
Subcellular Location
PTM/Processing
Features
Showing features for signal, propeptide, chain, disulfide bond, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-20 | |||||
Sequence: MASFVARLTLALSFIALALA | ||||||
Propeptide | PRO_0000023751 | 21-67 | ||||
Sequence: GYSLVQNTLSSPTHTRLNLIPTWLDSTFDSADVLSYLGFGKSSGRLS | ||||||
Chain | PRO_0000023752 | 68-348 | Neutral peroxidase | |||
Sequence: DSNCVFSAVKEIVDAAITAETRMGASLIRLHFHDCFVDGCDGGILLNDTANFTGEQGAPANSNSVRGFSVIDQAKRNAQTKCADTPVSCADVLAIAARDAFRKFTNQTYNITLGRQDARTANLTGANTQLPAPFDNLSIQTAKFADKGFNQREMVVLAGAHTVGFSRCAVLCTSTNLNQNRSATLQCTCPASANDTGLVGLDPSPGTFDKKYFEELVKGQGLLFSDQELMQSNATVTAVRRYRDATGAFLTDFAAAMVKMSNLPPSAGVQLEIRNVCSRVN | ||||||
Disulfide bond | 71↔149 | |||||
Sequence: CVFSAVKEIVDAAITAETRMGASLIRLHFHDCFVDGCDGGILLNDTANFTGEQGAPANSNSVRGFSVIDQAKRNAQTKC | ||||||
Disulfide bond | 102↔107 | |||||
Sequence: CFVDGC | ||||||
Glycosylation | 114 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 118 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 156↔344 | |||||
Sequence: CADVLAIAARDAFRKFTNQTYNITLGRQDARTANLTGANTQLPAPFDNLSIQTAKFADKGFNQREMVVLAGAHTVGFSRCAVLCTSTNLNQNRSATLQCTCPASANDTGLVGLDPSPGTFDKKYFEELVKGQGLLFSDQELMQSNATVTAVRRYRDATGAFLTDFAAAMVKMSNLPPSAGVQLEIRNVC | ||||||
Glycosylation | 173 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 177 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 189 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 203 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 235↔256 | |||||
Sequence: CAVLCTSTNLNQNRSATLQCTC | ||||||
Glycosylation | 247 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 261 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 300 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Keywords
- PTM
Expression
Tissue specificity
Highly expressed in suspension cultured cells. Weak expression also found in the stems of intact plants. No expression in leaf, tuberous root and non-tuberous root.
Induction
By wounding and cold stress. Induced by acclimation and repressed by chilling.
Developmental stage
Very low expression level 0.5 days after subculture (DAS).
Structure
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length348
- Mass (Da)37,186
- Last updated1997-07-01 v1
- Checksum3FA8C361B72CD383
Keywords
- Technical term