| IED ID | IndEnz0010001314 |
| Enzyme Type ID | esterase001314 |
| Protein Name |
Strigolactone esterase D14 EC 3.1.-.- Protein DWARF 14 AtD14 |
| Gene Name | D14 At3g03990 T11I18.10 |
| Organism | Arabidopsis thaliana (Mouse-ear cress) |
| Taxonomic Lineage | cellular organisms Eukaryota Viridiplantae Streptophyta Streptophytina Embryophyta Tracheophyta Euphyllophyta Spermatophyta Magnoliopsida Mesangiospermae eudicotyledons Gunneridae Pentapetalae rosids malvids Brassicales Brassicaceae Camelineae Arabidopsis Arabidopsis thaliana (Mouse-ear cress) |
| Enzyme Sequence | MSQHNILEALNVRVVGTGDRILFLAHGFGTDQSAWHLILPYFTQNYRVVLYDLVCAGSVNPDYFDFNRYTTLDPYVDDLLNIVDSLGIQNCAYVGHSVSAMIGIIASIRRPELFSKLILIGFSPRFLNDEDYHGGFEEGEIEKVFSAMEANYEAWVHGFAPLAVGADVPAAVREFSRTLFNMRPDISLFVSRTVFNSDLRGVLGLVRVPTCVIQTAKDVSVPASVAEYLRSHLGGDTTVETLKTEGHLPQLSAPAQLAQFLRRALPR |
| Enzyme Length | 267 |
| Uniprot Accession Number | Q9SQR3 |
| Absorption | |
| Active Site | ACT_SITE 97; /note="Nucleophile"; /evidence="ECO:0000269|PubMed:23381136, ECO:0000269|PubMed:25425668"; ACT_SITE 218; /evidence="ECO:0000305|PubMed:23381136"; ACT_SITE 247; /evidence="ECO:0000305|PubMed:23381136" |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.1.-.- |
| Enzyme Function | FUNCTION: Involved in strigolactone signaling pathway (PubMed:22357928). Does not move long distances acropetally in the plant to regulate shoot branching and is rapidly degraded in the presence of strigolactones (PubMed:24610723). Functions downstream of strigolactone synthesis, as a component of hormone signaling and as an enzyme that participates in the conversion of strigolactones to the bioactive form (PubMed:22357928). Acts probably as a strigolactone receptor (PubMed:24610723). Strigolactones are hormones that inhibit tillering and shoot branching through the MAX-dependent pathway, contribute to the regulation of shoot architectural response to phosphate-limiting conditions and function as rhizosphere signal that stimulates hyphal branching of arbuscular mycorrhizal fungi and trigger seed germination of root parasitic weeds (PubMed:22357928). Hydrolyzes methyl carlactonoate (MeCLA), but not carlactone (CL) or carlactonoic acid (CLA) (PubMed:25425668). Hydrolyzes the butenolide ring of strigolactones (PubMed:23381136). The initial nucleophilic attack causes an electron shift, followed by the addition of a water molecule, to lead to the release of the ABC ring product and the formation of a 'Ser-97'-stabilized open lactone intermediate (PubMed:23381136). Has no esterase activity for 4-nitrophenyl butyrate (PubMed:23381136). Binds and hydrolyzes the synthetic strigolactone analog GR24 in vitro. Forms a stable covalent complex with the D-ring of strigolactone, which is essential for hormone bioactivity. The D-ring is attached to His-247 of the catalytic triad. The hydrolysis of strigolactone into a covalently linked intermediate molecule initiates a conformational change of D14 to facilitate interaction with MAX2 and formation of the D14-MAX2-SKP1/ASK1 complex to trigger strigolactone signaling. This mechanism defines D14 as a non-canonical hormone receptor with dual functions to generate and sense the active form of strigolactone (PubMed:27479325). {ECO:0000269|PubMed:22357928, ECO:0000269|PubMed:23381136, ECO:0000269|PubMed:24610723, ECO:0000269|PubMed:25425668, ECO:0000269|PubMed:27479325}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Beta strand (12); Chain (1); Helix (14); Mutagenesis (3); Sequence conflict (1); Turn (5) |
| Keywords | 3D-structure;Cytoplasm;Hydrolase;Nucleus;Reference proteome |
| Interact With | Q9SZN7 |
| Induction | INDUCTION: Not regulated by strigolactone, auxin signaling or bud growth status. {ECO:0000269|PubMed:24610723}. |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:24610723}. Nucleus {ECO:0000269|PubMed:24610723}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (2) |
| Cross Reference PDB | 4IH4; 5HZG; |
| Mapped Pubmed ID | 18650403; 26175507; 26228149; 26779242; 26875827; 27247031; 27317673; 28627464; 28970845; 29131815; 29365172; 29473784; 29523686; 29532023; 29538714; 29982999; 30643123; 30738662; 31465451; 31888087; 32022953; 32358074; 32501539; 32528176; 32665554; 32669036; |
| Motif | |
| Gene Encoded By | |
| Mass | 29,625 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |