A0A5S9YBA4 · A0A5S9YBA4_ARATH
- ProteinProstaglandin E synthase 2
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids816 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
Function
Catalytic activity
- 2 a phenolic donor + H2O2 = 2 a phenolic radical donor + 2 H2O
- prostaglandin H2 = (12S)-hydroxy-(5Z,8E,10E)-heptadecatrienoate + malonaldehydeThis reaction proceeds in the forward direction.
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.
Pathway
Lipid metabolism; prostaglandin biosynthesis.
Features
Showing features for site, active site, binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Site | 558 | Transition state stabilizer | ||||
Sequence: R | ||||||
Active site | 562 | Proton acceptor | ||||
Sequence: H | ||||||
Binding site | 563 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 566 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: V | ||||||
Binding site | 568 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 570 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 572 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 584 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 657 | substrate | ||||
Sequence: P | ||||||
Binding site | 687 | Fe (UniProtKB | ChEBI) of heme b (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: H | ||||||
Binding site | 688 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 740 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 742 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 747 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | extracellular region | |
Cellular Component | membrane | |
Cellular Component | vacuole | |
Molecular Function | 12-hydroxyheptadecatrienoic acid synthase activity | |
Molecular Function | heme binding | |
Molecular Function | hydrolase activity, acting on ester bonds | |
Molecular Function | lactoperoxidase activity | |
Molecular Function | metal ion binding | |
Molecular Function | prostaglandin-E synthase activity | |
Biological Process | hydrogen peroxide catabolic process | |
Biological Process | prostaglandin biosynthetic process | |
Biological Process | response to oxidative stress |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameProstaglandin E synthase 2
- EC number
- 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 accessionA0A5S9YBA4
Proteomes
PTM/Processing
Features
Showing features for disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Disulfide bond | 531↔610 | |||||
Sequence: CPQADHIVTNAVKKAMSNDQTVPAALLRMHFHDCFVRGCDGSVLLDSKGKNKAEKDGPPNISLHAFYVIDNAKKALEEQC | ||||||
Disulfide bond | 564↔569 | |||||
Sequence: CFVRGC | ||||||
Disulfide bond | 616↔812 | |||||
Sequence: CADILSLAARDAVALSGGPTWAVPKGRKDGRISKAIETRQLPAPTFNISQLRQNFGQRGLSMHDLVALSGGHTLGFAHCSSFQNRLHKFNTQKEVDPTLNPSFAARLEGVCPAHNTVKNAGSNMDGTVTSFDNIYYKMLIQGKSLFSSDESLLAVPSTKKLVAKYANSNEEFERAFVKSMIKMSSISGNGNEVRLNC | ||||||
Disulfide bond | 694↔726 | |||||
Sequence: CSSFQNRLHKFNTQKEVDPTLNPSFAARLEGVC |
Keywords
- PTM
Expression
Gene expression databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 86-162 | GST N-terminal | ||||
Sequence: KEVVLYQYEACPFCNKVKAFLDYNKIPYKVVEVNPISKKEIKWSDYKKVPILTVDGEQMVDSSVIIDSLFQKMHPEI | ||||||
Domain | 521-816 | Plant heme peroxidase family profile | ||||
Sequence: ALSPHYYDHTCPQADHIVTNAVKKAMSNDQTVPAALLRMHFHDCFVRGCDGSVLLDSKGKNKAEKDGPPNISLHAFYVIDNAKKALEEQCPGIVSCADILSLAARDAVALSGGPTWAVPKGRKDGRISKAIETRQLPAPTFNISQLRQNFGQRGLSMHDLVALSGGHTLGFAHCSSFQNRLHKFNTQKEVDPTLNPSFAARLEGVCPAHNTVKNAGSNMDGTVTSFDNIYYKMLIQGKSLFSSDESLLAVPSTKKLVAKYANSNEEFERAFVKSMIKMSSISGNGNEVRLNCRRVR |
Sequence similarities
Belongs to the 'GDSL' lipolytic enzyme family.
Belongs to the GST superfamily.
Belongs to the peroxidase family. Ascorbate peroxidase subfamily.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Length816
- Mass (Da)89,742
- Last updated2020-04-22 v1
- Checksum84A5E08DC4DC0930