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J9U5U9

- DAD2_PETHY

UniProt

J9U5U9 - DAD2_PETHY

Protein

Probable strigolactone esterase DAD2

Gene

DAD2

Organism
Petunia hybrida (Petunia)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 11 (01 Oct 2014)
      Sequence version 1 (28 Nov 2012)
      Previous versions | rss
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    Functioni

    Involved in strigolactone signaling pathway. May function downstream of strigolactone synthesis, as a component of hormone signaling or as an enzyme that participates in the conversion of strigolactones to the bioactive form. Can hydrolyze the synthetic strigolactone analog GR24 in vitro. 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.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei96 – 961NucleophileCurated
    Active sitei217 – 2171By similarity
    Active sitei246 – 2461Curated

    GO - Molecular functioni

    1. hydrolase activity, acting on ester bonds Source: UniProtKB

    GO - Biological processi

    1. secondary shoot formation Source: UniProtKB
    2. strigolactone biosynthetic process Source: UniProtKB

    Keywords - Molecular functioni

    Hydrolase

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Probable strigolactone esterase DAD2
    Short name:
    3.1.-.-
    Alternative name(s):
    Protein DECREASED APICAL DOMINANCE 2
    Gene namesi
    Name:DAD2
    OrganismiPetunia hybrida (Petunia)
    Taxonomic identifieri4102 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeasteridslamiidsSolanalesSolanaceaePetunioideaePetunia

    Pathology & Biotechi

    Disruption phenotypei

    Increased shoot branching.1 Publication

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi96 – 961S → A: Loss of activity and abolish interaction with MAX2A. 1 Publication
    Mutagenesisi246 – 2461H → A: Loss of activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 267267Probable strigolactone esterase DAD2PRO_0000422055Add
    BLAST

    Interactioni

    Subunit structurei

    Interacts with MAX2A in a strigolactone-depedent manner.1 Publication

    Structurei

    Secondary structure

    1
    267
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi4 – 85
    Beta strandi12 – 143
    Beta strandi18 – 247
    Helixi31 – 344
    Turni35 – 373
    Helixi38 – 414
    Turni42 – 443
    Beta strandi46 – 505
    Helixi60 – 623
    Turni65 – 673
    Beta strandi69 – 713
    Helixi72 – 8413
    Beta strandi89 – 957
    Helixi97 – 10812
    Turni110 – 1123
    Beta strandi113 – 1208
    Helixi137 – 14913
    Helixi151 – 16313
    Helixi168 – 18013
    Helixi183 – 19412
    Helixi199 – 2046
    Beta strandi209 – 2179
    Helixi222 – 23110
    Beta strandi232 – 2343
    Beta strandi236 – 24611
    Helixi248 – 2514
    Helixi253 – 26412

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4DNPX-ray2.15A1-267[»]
    4DNQX-ray2.80A/B/C/D/E/F/G/H/I/J/K/L1-267[»]
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the AB hydrolase superfamily.Curated

    Family and domain databases

    Gene3Di3.40.50.1820. 1 hit.
    InterProiIPR029058. AB_hydrolase.
    [Graphical view]
    SUPFAMiSSF53474. SSF53474. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    J9U5U9-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGQTLLDALN VRVVGSGERV LVLAHGFGTD QSAWNRILPF FLRDYRVVLY    50
    DLVCAGSVNP DFFDFRRYTT LDPYVDDLLH ILDALGIDCC AYVGHSVSAM 100
    IGILASIRRP ELFSKLILIG ASPRFLNDED YHGGFEQGEI EKVFSAMEAN 150
    YEAWVNGFAP LAVGADVPAA VREFSRTLFN MRPDITLFVS RTVFNSDMRG 200
    VLGLVKVPCH IFQTARDHSV PASVATYLKN HLGGKNTVHW LNIEGHLPHL 250
    SAPTLLAQEL RRALSHR 267
    Length:267
    Mass (Da):29,712
    Last modified:November 28, 2012 - v1
    Checksum:i49F4B5985C597C11
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    JQ654486 Genomic DNA. Translation: AFR68698.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    JQ654486 Genomic DNA. Translation: AFR68698.1 .

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4DNP X-ray 2.15 A 1-267 [» ]
    4DNQ X-ray 2.80 A/B/C/D/E/F/G/H/I/J/K/L 1-267 [» ]
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Family and domain databases

    Gene3Di 3.40.50.1820. 1 hit.
    InterProi IPR029058. AB_hydrolase.
    [Graphical view ]
    SUPFAMi SSF53474. SSF53474. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "DAD2 is an alpha/beta hydrolase likely to be involved in the perception of the plant branching hormone, strigolactone."
      Hamiaux C., Drummond R.S., Janssen B.J., Ledger S.E., Cooney J.M., Newcomb R.D., Snowden K.C.
      Curr. Biol. 22:2032-2036(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS), CATALYTIC ACTIVITY, INTERACTION WITH MAX2A, MUTAGENESIS OF SER-96 AND HIS-246, DISRUPTION PHENOTYPE.

    Entry informationi

    Entry nameiDAD2_PETHY
    AccessioniPrimary (citable) accession number: J9U5U9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 3, 2013
    Last sequence update: November 28, 2012
    Last modified: October 1, 2014
    This is version 11 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3