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J9U5U9

- DAD2_PETHY

UniProt

J9U5U9 - DAD2_PETHY

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Protein

Probable strigolactone esterase DAD2

Gene

DAD2

Organism
Petunia hybrida (Petunia)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

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
Complete GO annotation...

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 – 85Combined sources
Beta strandi12 – 143Combined sources
Beta strandi18 – 247Combined sources
Helixi31 – 344Combined sources
Turni35 – 373Combined sources
Helixi38 – 414Combined sources
Turni42 – 443Combined sources
Beta strandi46 – 505Combined sources
Helixi60 – 623Combined sources
Turni65 – 673Combined sources
Beta strandi69 – 713Combined sources
Helixi72 – 8413Combined sources
Beta strandi89 – 957Combined sources
Helixi97 – 10812Combined sources
Turni110 – 1123Combined sources
Beta strandi113 – 1208Combined sources
Helixi137 – 14913Combined sources
Helixi151 – 16313Combined sources
Helixi168 – 18013Combined sources
Helixi183 – 19412Combined sources
Helixi199 – 2046Combined sources
Beta strandi209 – 2179Combined sources
Helixi222 – 23110Combined sources
Beta strandi232 – 2343Combined sources
Beta strandi236 – 24611Combined sources
Helixi248 – 2514Combined sources
Helixi253 – 26412Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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

        10         20         30         40         50
MGQTLLDALN VRVVGSGERV LVLAHGFGTD QSAWNRILPF FLRDYRVVLY
60 70 80 90 100
DLVCAGSVNP DFFDFRRYTT LDPYVDDLLH ILDALGIDCC AYVGHSVSAM
110 120 130 140 150
IGILASIRRP ELFSKLILIG ASPRFLNDED YHGGFEQGEI EKVFSAMEAN
160 170 180 190 200
YEAWVNGFAP LAVGADVPAA VREFSRTLFN MRPDITLFVS RTVFNSDMRG
210 220 230 240 250
VLGLVKVPCH IFQTARDHSV PASVATYLKN HLGGKNTVHW LNIEGHLPHL
260
SAPTLLAQEL RRALSHR
Length:267
Mass (Da):29,712
Last modified:November 28, 2012 - v1
Checksum:i49F4B5985C597C11
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
JQ654486 Genomic DNA. Translation: AFR68698.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
JQ654486 Genomic DNA. Translation: AFR68698.1 .

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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 29, 2014
This is version 12 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