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Protein

Probable strigolactone esterase DAD2

Gene

DAD2

Organism
Petunia hybrida (Petunia)
Status
Reviewed-Annotation score: 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)DescriptionActionsGraphical viewLength
Active sitei96Nucleophile1 Publication1
Active sitei217By similarity1
Active sitei2461 Publication1

GO - Molecular functioni

  • hydrolase activity, acting on ester bonds Source: UniProtKB

GO - Biological processi

  • secondary shoot formation Source: UniProtKB
  • strigolactone biosynthetic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Protein family/group databases

ESTHERipethy-dad2. RsbQ-like.

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)DescriptionActionsGraphical viewLength
Mutagenesisi96S → A: Loss of activity and abolish interaction with MAX2A. 1 Publication1
Mutagenesisi246H → A: Loss of activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004220551 – 267Probable strigolactone esterase DAD2Add BLAST267

Interactioni

Subunit structurei

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

Structurei

Secondary structure

1267
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi4 – 8Combined sources5
Beta strandi12 – 14Combined sources3
Beta strandi18 – 24Combined sources7
Helixi31 – 34Combined sources4
Turni35 – 37Combined sources3
Helixi38 – 41Combined sources4
Turni42 – 44Combined sources3
Beta strandi46 – 50Combined sources5
Helixi60 – 62Combined sources3
Turni65 – 67Combined sources3
Beta strandi69 – 71Combined sources3
Helixi72 – 84Combined sources13
Beta strandi89 – 95Combined sources7
Helixi97 – 108Combined sources12
Turni110 – 112Combined sources3
Beta strandi113 – 120Combined sources8
Helixi137 – 149Combined sources13
Helixi151 – 163Combined sources13
Helixi168 – 180Combined sources13
Helixi183 – 194Combined sources12
Helixi199 – 204Combined sources6
Beta strandi209 – 217Combined sources9
Helixi222 – 231Combined sources10
Beta strandi232 – 234Combined sources3
Beta strandi236 – 246Combined sources11
Helixi248 – 251Combined sources4
Helixi253 – 264Combined sources12

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4DNPX-ray2.15A1-267[»]
4DNQX-ray2.80A/B/C/D/E/F/G/H/I/J/K/L1-267[»]
SMRiJ9U5U9.
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.
IPR000073. AB_hydrolase_1.
IPR031143. D14_fam.
[Graphical view]
PANTHERiPTHR10992:SF891. PTHR10992:SF891. 1 hit.
PfamiPF12697. Abhydrolase_6. 1 hit.
[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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4DNPX-ray2.15A1-267[»]
4DNQX-ray2.80A/B/C/D/E/F/G/H/I/J/K/L1-267[»]
SMRiJ9U5U9.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

ESTHERipethy-dad2. RsbQ-like.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR000073. AB_hydrolase_1.
IPR031143. D14_fam.
[Graphical view]
PANTHERiPTHR10992:SF891. PTHR10992:SF891. 1 hit.
PfamiPF12697. Abhydrolase_6. 1 hit.
[Graphical view]
SUPFAMiSSF53474. SSF53474. 1 hit.
ProtoNetiSearch...

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: November 2, 2016
This is version 18 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.