DAD2_PETHY
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 25-MAY-2022, entry version 34.
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}.
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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; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000073; AB_hydrolase_1.
DR InterPro; IPR031143; D14_fam.
DR PANTHER; PTHR43039:SF4; PTHR43039:SF4; 1.
DR Pfam; PF12697; Abhydrolase_6; 1.
DR SUPFAM; SSF53474; SSF53474; 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
