Q9XIV8 · PERN1_TOBAC
- ProteinPeroxidase N1
- GenepoxN1
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids330 (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. Can use NADH, NADPH and monolignols as substrates.
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.
pH Dependence
Optimum pH is 4.7.
Features
Showing features for site, active site, binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Site | 68 | Transition state stabilizer | ||||
Sequence: R | ||||||
Active site | 72 | Proton acceptor | ||||
Sequence: H | ||||||
Binding site | 73 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 76 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: V | ||||||
Binding site | 78 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 80 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 82 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 164 | substrate | ||||
Sequence: P | ||||||
Binding site | 194 | Fe (UniProtKB | ChEBI) of heme b (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: H | ||||||
Binding site | 195 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 246 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 254 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | extracellular region | |
Cellular Component | plant-type cell wall | |
Molecular Function | heme binding | |
Molecular Function | lactoperoxidase activity | |
Molecular Function | metal ion binding | |
Molecular Function | peroxidase activity | |
Biological Process | hydrogen peroxide catabolic process | |
Biological Process | response to oxidative stress | |
Biological Process | response to stress |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended namePeroxidase N1
- EC number
- Alternative names
Gene names
Organism names
- Strains
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > asterids > lamiids > Solanales > Solanaceae > Nicotianoideae > Nicotianeae > Nicotiana
Accessions
- Primary accessionQ9XIV8
- Secondary accessions
Proteomes
Subcellular Location
Phenotypes & Variants
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | 77 | |||||
Sequence: L → Q | ||||||
Natural variant | 101 | |||||
Sequence: K → R | ||||||
Natural variant | 111 | |||||
Sequence: T → K | ||||||
Natural variant | 281 | |||||
Sequence: Q → K |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 4 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for signal, modified residue, chain, disulfide bond, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-29 | |||||
Sequence: MEYYHHSINKMAMFMVILVLAIDVTMVLG | ||||||
Modified residue | 30 | Pyrrolidone carboxylic acid | ||||
Sequence: Q | ||||||
Chain | PRO_0000312842 | 30-330 | Peroxidase N1 | |||
Sequence: QGTRVGFYSSTCPRAESIVQSTVRAHFQSDPTVAPGILRMHFHDCFVLGCDGSILIEGSDAERTAIPNRNLKGFDVIEDAKTQIEAICPGVVSCADILALAARDSVVATRGLTWSVPTGRRDGRVSRAADAGDLPAFFDSVDIQKRKFLTKGLNTQDLVALTGAHTIGTAGCAVIRDRLFNFNSTGGPDPSIDATFLPQLRALCPQNGDASRRVGLDTGSVNNFDTSYFSNLRNGRGVLESDQKLWTDASTQVFVQRFLGIRGLLGLTFGVEFGRSMVKMSNIEVKTGTNGEIRKVCSAIN | ||||||
Disulfide bond | 41↔117 | |||||
Sequence: CPRAESIVQSTVRAHFQSDPTVAPGILRMHFHDCFVLGCDGSILIEGSDAERTAIPNRNLKGFDVIEDAKTQIEAIC | ||||||
Disulfide bond | 74↔79 | |||||
Sequence: CFVLGC | ||||||
Disulfide bond | 123↔326 | |||||
Sequence: CADILALAARDSVVATRGLTWSVPTGRRDGRVSRAADAGDLPAFFDSVDIQKRKFLTKGLNTQDLVALTGAHTIGTAGCAVIRDRLFNFNSTGGPDPSIDATFLPQLRALCPQNGDASRRVGLDTGSVNNFDTSYFSNLRNGRGVLESDQKLWTDASTQVFVQRFLGIRGLLGLTFGVEFGRSMVKMSNIEVKTGTNGEIRKVC | ||||||
Disulfide bond | 201↔233 | |||||
Sequence: CAVIRDRLFNFNSTGGPDPSIDATFLPQLRALC | ||||||
Glycosylation | 212 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Expressed at a high level in roots and at a trace level in lower leaves. Not expressed in upper leaves, stems, flowers, seeds and shoot apices.
Induction
Induced rapidly in leaves after wounding, mRNA is detectable 30 minutes after wounding, reaches maximum levels after 4 hours, and decreases slightly after 8 hours. When lower leaves are wounded, mRNA also accumulates in upper, unwounded, leaves. Wound-induced expression is enhanced by spermine, and suppressed by methyl jasmonite and coronatine. Salicylic acid and ethephon have no effect on wound-induced expression. Induced by infection with TMV.
Interaction
Protein-protein interaction databases
Structure
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length330
- Mass (Da)35,732
- Last updated1999-11-01 v1
- Checksum2034ACB6376B6180
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 86-88 | in Ref. 4; AA sequence | ||||
Sequence: EGS → DGT | ||||||
Sequence conflict | 98 | in Ref. 4; AA sequence | ||||
Sequence: R → S | ||||||
Sequence conflict | 129 | in Ref. 4; AA sequence | ||||
Sequence: L → V | ||||||
Sequence conflict | 162 | in Ref. 2; BAD97807 | ||||
Sequence: D → N | ||||||
Sequence conflict | 172 | in Ref. 2; BAD97807 | ||||
Sequence: I → V | ||||||
Sequence conflict | 175 | in Ref. 2; BAD97807 | ||||
Sequence: R → Q | ||||||
Sequence conflict | 178-179 | in Ref. 2; BAD97807 | ||||
Sequence: LT → TA | ||||||
Sequence conflict | 206 | in Ref. 2; BAD97807 | ||||
Sequence: D → G | ||||||
Sequence conflict | 230 | in Ref. 2; BAD97807 | ||||
Sequence: R → Q | ||||||
Sequence conflict | 240 | in Ref. 2; BAD97807 | ||||
Sequence: S → A | ||||||
Sequence conflict | 244 | in Ref. 2; BAD97807 | ||||
Sequence: G → A | ||||||
Sequence conflict | 250 | in Ref. 2; BAD97807 | ||||
Sequence: V → A | ||||||
Sequence conflict | 304 | in Ref. 3; CAH17984 | ||||
Sequence: R → G |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AB027753 EMBL· GenBank· DDBJ | BAA82307.1 EMBL· GenBank· DDBJ | mRNA | ||
AB044153 EMBL· GenBank· DDBJ | BAD97807.1 EMBL· GenBank· DDBJ | mRNA | ||
AB044154 EMBL· GenBank· DDBJ | BAD97808.1 EMBL· GenBank· DDBJ | mRNA | ||
AJ810538 EMBL· GenBank· DDBJ | CAH17984.1 EMBL· GenBank· DDBJ | Genomic DNA |