UniProtKB - G1JSL4 (PXG1_AVESA)
Peroxygenase 1
Functioni
Calcium-binding peroxygenase involved in cutin monomers biosynthesis. Can catalyze epoxidation of fatty acid and sulfoxidation reactions that can proceede competitively, although in favor of the sulfoxidation. Can only use unsaturated fatty acids with double bonds in the cis configuration as substrates. The preferred substrate is oleic acid and is inactive toward ricinoleic acid. Free fatty acid and fatty acid methyl esters are effective substrate forms, but not phospholipids and acyl-CoA. Hydroperoxy-trienoic (HPOT) acids are preferred over Hydroperoxy-dienoic (HPODT) acids as oxygen donors.
3 PublicationsCatalytic activityi
- RH + ROOH = ROH + ROH.3 Publications EC:1.11.2.3
Cofactori
Protein has several cofactor binding sites:- heme bBy similarityNote: Binds 1 heme b (iron(II)-protoporphyrin IX) group.By similarity
- Ca2+By similarity
Activity regulationi
Kineticsi
- KM=16.07 µM for 9-HPOD1 Publication
- KM=10.42 µM for 9-HPOT1 Publication
- KM=25.18 µM for 13-HPOD1 Publication
- KM=7.25 µM for 13-HPOT1 Publication
- KM=215.76 µM for cumene hydroperoxide1 Publication
- Vmax=214.04 pmol/sec/mg enzyme toward 9-HPOD1 Publication
- Vmax=188.69 pmol/sec/mg enzyme toward 9-HPOT1 Publication
- Vmax=306.57 pmol/sec/mg enzyme toward 13-HPOD1 Publication
- Vmax=173.49 pmol/sec/mg enzyme toward 13-HPOT1 Publication
- Vmax=883.34 pmol/sec/mg enzyme toward cumene hydroperoxide1 Publication
pH dependencei
Temperature dependencei
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Metal bindingi | 76 | Iron (heme axial ligand)By similarity | 1 | |
Metal bindingi | 81 | CalciumSequence analysis | 1 | |
Metal bindingi | 83 | CalciumSequence analysis | 1 | |
Metal bindingi | 85 | CalciumSequence analysis | 1 | |
Metal bindingi | 92 | CalciumSequence analysis | 1 |
GO - Molecular functioni
- 18-hydroxyoleate peroxygenase activity Source: UniProtKB-EC
- metal ion binding Source: UniProtKB-KW
- plant seed peroxidase activity Source: UniProtKB-EC
Keywordsi
Molecular function | Oxidoreductase |
Ligand | Calcium, Heme, Iron, Metal-binding |
Enzyme and pathway databases
BRENDAi | 1.11.2.3, 588 |
Names & Taxonomyi
Protein namesi | |
Organismi | Avena sativa (Oat) |
Taxonomic identifieri | 4498 [NCBI] |
Taxonomic lineagei | Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliopsida › Liliopsida › Poales › Poaceae › BOP clade › Pooideae › Poodae › Poeae › Aveninae › Avena |
Subcellular locationi
Endoplasmic reticulum
Other locations
Endoplasmic reticulum
- endoplasmic reticulum Source: UniProtKB-KW
Other locations
- lipid droplet Source: UniProtKB-SubCell
- membrane Source: UniProtKB-KW
Keywords - Cellular componenti
Endoplasmic reticulum, Lipid droplet, Membrane, MicrosomePTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000415559 | 1 – 249 | Peroxygenase 1Add BLAST | 249 |
Expressioni
Tissue specificityi
Interactioni
Subunit structurei
Homodimer.
By similarityStructurei
3D structure databases
AlphaFoldDBi | G1JSL4 |
ModBasei | Search... |
SWISS-MODEL-Workspacei | Submit a new modelling project... |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 68 – 103 | EF-handAdd BLAST | 36 |
Motif
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Motifi | 124 – 133 | Proline-knot | 10 |
Domaini
Sequence similaritiesi
Family and domain databases
InterProi | View protein in InterPro IPR007736, Caleosin-related |
PANTHERi | PTHR31495, PTHR31495, 1 hit |
Pfami | View protein in Pfam PF05042, Caleosin, 1 hit |
i Sequence
Sequence statusi: Complete.
10 20 30 40 50
MAEDAVVSDA VVVSDAMSSV AKGAPVTAQR PVRDDLEKHI PKPYLARALV
60 70 80 90 100
AVDVNNPEGT KGGRHEHGQK SVLQQHVSFF DQNGDGIIYP WETFRGLRRL
110 120 130 140 150
GFNLIVSFIV AIGIHTGLSY PTLPTWRPSL LFPVYIDRIH KAKHGSDTAT
160 170 180 190 200
FDTEGRFMPV NFENIFSKNA RSQPDKLTLR EIWMMTNDHR LAYDPFGWVA
210 220 230 240
NKGEWILLYM LAKDDEGYLP KEAIRGVYDG SLFEFLAEQR TKKAHGKQH
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | JN390966 mRNA Translation: AEL03786.1 |
Genome annotation databases
KEGGi | ag:AEL03786 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | JN390966 mRNA Translation: AEL03786.1 |
3D structure databases
AlphaFoldDBi | G1JSL4 |
ModBasei | Search... |
SWISS-MODEL-Workspacei | Submit a new modelling project... |
Genome annotation databases
KEGGi | ag:AEL03786 |
Enzyme and pathway databases
BRENDAi | 1.11.2.3, 588 |
Family and domain databases
InterProi | View protein in InterPro IPR007736, Caleosin-related |
PANTHERi | PTHR31495, PTHR31495, 1 hit |
Pfami | View protein in Pfam PF05042, Caleosin, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | PXG1_AVESA | |
Accessioni | G1JSL4Primary (citable) accession number: G1JSL4 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | February 22, 2012 |
Last sequence update: | October 19, 2011 | |
Last modified: | May 25, 2022 | |
This is version 32 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Plant Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
Direct protein sequencingDocuments
- SIMILARITY comments
Index of protein domains and families