ID DAD2_PETHY Reviewed; 267 AA. AC J9U5U9; DT 03-APR-2013, integrated into UniProtKB/Swiss-Prot. DT 28-NOV-2012, sequence version 1. DT 22-FEB-2023, entry version 36. DE RecName: Full=Probable strigolactone esterase DAD2; DE EC=3.1.-.-; DE AltName: Full=Protein DECREASED APICAL DOMINANCE 2; GN Name=DAD2; OS Petunia hybrida (Petunia). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC asterids; lamiids; Solanales; Solanaceae; Petunioideae; Petunia. OX NCBI_TaxID=4102; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS), RP CATALYTIC ACTIVITY, INTERACTION WITH MAX2A, MUTAGENESIS OF SER-96 AND RP HIS-246, AND DISRUPTION PHENOTYPE. RX PubMed=22959345; DOI=10.1016/j.cub.2012.08.007; RA Hamiaux C., Drummond R.S., Janssen B.J., Ledger S.E., Cooney J.M., RA Newcomb R.D., Snowden K.C.; RT "DAD2 is an alpha/beta hydrolase likely to be involved in the perception of RT the plant branching hormone, strigolactone."; RL Curr. Biol. 22:2032-2036(2012). CC -!- FUNCTION: Involved in strigolactone signaling pathway. May function CC downstream of strigolactone synthesis, as a component of hormone CC signaling or as an enzyme that participates in the conversion of CC strigolactones to the bioactive form. Can hydrolyze the synthetic CC strigolactone analog GR24 in vitro. Strigolactones are hormones that CC inhibit tillering and shoot branching through the MAX-dependent CC pathway, contribute to the regulation of shoot architectural response CC to phosphate-limiting conditions and function as rhizosphere signal CC that stimulates hyphal branching of arbuscular mycorrhizal fungi and CC trigger seed germination of root parasitic weeds. CC -!- SUBUNIT: Interacts with MAX2A in a strigolactone-dependent manner. CC {ECO:0000269|PubMed:22959345}. CC -!- DISRUPTION PHENOTYPE: Increased shoot branching. CC {ECO:0000269|PubMed:22959345}. CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; JQ654486; AFR68698.1; -; Genomic_DNA. DR PDB; 4DNP; X-ray; 2.15 A; A=1-267. DR PDB; 4DNQ; X-ray; 2.80 A; A/B/C/D/E/F/G/H/I/J/K/L=1-267. DR PDB; 6AP6; X-ray; 1.65 A; A/B=1-267. DR PDB; 6AP7; X-ray; 1.51 A; A/B=1-267. DR PDB; 6O5J; X-ray; 1.63 A; A/B=3-266. DR PDB; 6UH8; X-ray; 1.58 A; A/B=1-267. DR PDB; 6UH9; X-ray; 1.52 A; A/B=1-267. DR PDBsum; 4DNP; -. DR PDBsum; 4DNQ; -. DR PDBsum; 6AP6; -. DR PDBsum; 6AP7; -. DR PDBsum; 6O5J; -. DR PDBsum; 6UH8; -. DR PDBsum; 6UH9; -. DR AlphaFoldDB; J9U5U9; -. DR SMR; J9U5U9; -. DR ESTHER; pethy-dad2; RsbQ-like. DR GO; GO:0016788; F:hydrolase activity, acting on ester bonds; IDA:UniProtKB. DR GO; GO:0010223; P:secondary shoot formation; IMP:UniProtKB. DR GO; GO:1901601; P:strigolactone biosynthetic process; IDA:UniProtKB. DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1. DR InterPro; IPR029058; AB_hydrolase. DR InterPro; IPR000073; AB_hydrolase_1. DR PANTHER; PTHR43039; ESTERASE-RELATED; 1. DR PANTHER; PTHR43039:SF4; STRIGOLACTONE ESTERASE D14; 1. DR Pfam; PF12697; Abhydrolase_6; 1. DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1. PE 1: Evidence at protein level; KW 3D-structure; Hydrolase. FT CHAIN 1..267 FT /note="Probable strigolactone esterase DAD2" FT /id="PRO_0000422055" FT ACT_SITE 96 FT /note="Nucleophile" FT /evidence="ECO:0000269|PubMed:22959345" FT ACT_SITE 217 FT /evidence="ECO:0000250|UniProtKB:Q10QA5" FT ACT_SITE 246 FT /evidence="ECO:0000269|PubMed:22959345" FT MUTAGEN 96 FT /note="S->A: Loss of activity and abolish interaction with FT MAX2A." FT /evidence="ECO:0000269|PubMed:22959345" FT MUTAGEN 246 FT /note="H->A: Loss of activity." FT /evidence="ECO:0000269|PubMed:22959345" FT HELIX 4..8 FT /evidence="ECO:0007829|PDB:6AP7" FT STRAND 12..14 FT /evidence="ECO:0007829|PDB:6AP7" FT STRAND 18..24 FT /evidence="ECO:0007829|PDB:6AP7" FT HELIX 31..34 FT /evidence="ECO:0007829|PDB:6AP7" FT TURN 35..37 FT /evidence="ECO:0007829|PDB:6AP7" FT HELIX 38..40 FT /evidence="ECO:0007829|PDB:6AP7" FT TURN 41..44 FT /evidence="ECO:0007829|PDB:6AP7" FT STRAND 45..50 FT /evidence="ECO:0007829|PDB:6AP7" FT HELIX 60..62 FT /evidence="ECO:0007829|PDB:6AP7" FT TURN 65..67 FT /evidence="ECO:0007829|PDB:6AP7" FT STRAND 69..71 FT /evidence="ECO:0007829|PDB:6AP7" FT HELIX 72..85 FT /evidence="ECO:0007829|PDB:6AP7" FT STRAND 90..95 FT /evidence="ECO:0007829|PDB:6AP7" FT HELIX 97..108 FT /evidence="ECO:0007829|PDB:6AP7" FT STRAND 112..120 FT /evidence="ECO:0007829|PDB:6AP7" FT HELIX 137..149 FT /evidence="ECO:0007829|PDB:6AP7" FT HELIX 151..163 FT /evidence="ECO:0007829|PDB:6AP7" FT HELIX 168..180 FT /evidence="ECO:0007829|PDB:6AP7" FT HELIX 183..194 FT /evidence="ECO:0007829|PDB:6AP7" FT HELIX 199..204 FT /evidence="ECO:0007829|PDB:6AP7" FT STRAND 209..215 FT /evidence="ECO:0007829|PDB:6AP7" FT HELIX 222..231 FT /evidence="ECO:0007829|PDB:6AP7" FT STRAND 232..234 FT /evidence="ECO:0007829|PDB:6AP7" FT STRAND 236..246 FT /evidence="ECO:0007829|PDB:6AP7" FT HELIX 248..251 FT /evidence="ECO:0007829|PDB:6AP7" FT HELIX 253..265 FT /evidence="ECO:0007829|PDB:6AP7" SQ SEQUENCE 267 AA; 29712 MW; 49F4B5985C597C11 CRC64; MGQTLLDALN VRVVGSGERV LVLAHGFGTD QSAWNRILPF FLRDYRVVLY DLVCAGSVNP DFFDFRRYTT LDPYVDDLLH ILDALGIDCC AYVGHSVSAM IGILASIRRP ELFSKLILIG ASPRFLNDED YHGGFEQGEI EKVFSAMEAN YEAWVNGFAP LAVGADVPAA VREFSRTLFN MRPDITLFVS RTVFNSDMRG VLGLVKVPCH IFQTARDHSV PASVATYLKN HLGGKNTVHW LNIEGHLPHL SAPTLLAQEL RRALSHR //