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Protein

Dihydroxy-acid dehydratase, chloroplastic

Gene

DHAD

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the dehydration of 2,3-dihydroxy-3-isovalerate or 2,3-dihydroxy-3-methylvalerate to the 2-oxo acids 3-methyl-2-oxobutanoate (3MOB) or 3-methyl-2-oxopentanoate (3MOP).1 Publication

Catalytic activityi

2,3-dihydroxy-3-methylbutanoate = 3-methyl-2-oxobutanoate + H2O.UniRule annotation

Cofactori

[4Fe-4S] clusterUniRule annotationNote: Binds 1 [4Fe-4S] cluster.UniRule annotation

Pathwayi: L-isoleucine biosynthesis

This protein is involved in step 3 of the subpathway that synthesizes L-isoleucine from 2-oxobutanoate.UniRule annotation
Proteins known to be involved in the 4 steps of the subpathway in this organism are:
  1. Acetolactate synthase, chloroplastic (ALS), Acetolactate synthase small subunit 1, chloroplastic (VAT1), Acetolactate synthase small subunit 2, chloroplastic (At2g31810)
  2. Ketol-acid reductoisomerase, chloroplastic (At3g58610), Ketol-acid reductoisomerase (At3g58610)
  3. Dihydroxy-acid dehydratase, chloroplastic (DHAD)
  4. Branched-chain-amino-acid aminotransferase 6 (BCAT6), Branched-chain-amino-acid aminotransferase 2, chloroplastic (BCAT2), Branched-chain-amino-acid aminotransferase 5, chloroplastic (BCAT5), Branched-chain-amino-acid aminotransferase 3, chloroplastic (BCAT3)
This subpathway is part of the pathway L-isoleucine biosynthesis, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-isoleucine from 2-oxobutanoate, the pathway L-isoleucine biosynthesis and in Amino-acid biosynthesis.

Pathwayi: L-valine biosynthesis

This protein is involved in step 3 of the subpathway that synthesizes L-valine from pyruvate.UniRule annotation
Proteins known to be involved in the 4 steps of the subpathway in this organism are:
  1. Acetolactate synthase, chloroplastic (ALS), Acetolactate synthase small subunit 1, chloroplastic (VAT1), Acetolactate synthase small subunit 2, chloroplastic (At2g31810)
  2. Ketol-acid reductoisomerase, chloroplastic (At3g58610), Ketol-acid reductoisomerase (At3g58610)
  3. Dihydroxy-acid dehydratase, chloroplastic (DHAD)
  4. Branched-chain-amino-acid aminotransferase 6 (BCAT6), Branched-chain-amino-acid aminotransferase 2, chloroplastic (BCAT2), Branched-chain-amino-acid aminotransferase 5, chloroplastic (BCAT5), Branched-chain-amino-acid aminotransferase 3, chloroplastic (BCAT3)
This subpathway is part of the pathway L-valine biosynthesis, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-valine from pyruvate, the pathway L-valine biosynthesis and in Amino-acid biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi173 – 1731Iron-sulfur (4Fe-4S)UniRule annotation
Metal bindingi245 – 2451Iron-sulfur (4Fe-4S)UniRule annotation

GO - Molecular functioni

  • 4 iron, 4 sulfur cluster binding Source: UniProtKB-KW
  • copper ion binding Source: TAIR
  • dihydroxy-acid dehydratase activity Source: GO_Central
  • hydro-lyase activity Source: TAIR

GO - Biological processi

  • branched-chain amino acid biosynthetic process Source: TAIR
  • embryo sac development Source: TAIR
  • isoleucine biosynthetic process Source: UniProtKB-UniPathway
  • pollen development Source: TAIR
  • response to salt stress Source: TAIR
  • root development Source: TAIR
  • valine biosynthetic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Amino-acid biosynthesis, Branched-chain amino acid biosynthesis

Keywords - Ligandi

4Fe-4S, Iron, Iron-sulfur, Metal-binding

Enzyme and pathway databases

BioCyciARA:AT3G23940-MONOMER.
ARA:GQT-1269-MONOMER.
UniPathwayiUPA00047; UER00057.
UPA00049; UER00061.

Names & Taxonomyi

Protein namesi
Recommended name:
Dihydroxy-acid dehydratase, chloroplasticUniRule annotation (EC:4.2.1.9UniRule annotation)
Short name:
AtDHADCurated
Short name:
DADUniRule annotation
Gene namesi
Name:DHADCurated
Synonyms:ILVDUniRule annotation
Ordered Locus Names:At3g23940Imported
ORF Names:F14O13.131 Publication
OrganismiArabidopsis thaliana (Mouse-ear cress)Imported
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 3

Organism-specific databases

TAIRiAT3G23940.

Subcellular locationi

GO - Cellular componenti

  • chloroplast Source: TAIR
  • chloroplast stroma Source: TAIR
  • plastid Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Plastid

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 3434ChloroplastCombined sourcesAdd
BLAST
Chaini35 – 608574Dihydroxy-acid dehydratase, chloroplasticPRO_0000430600Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei35 – 351N-acetylserineCombined sources

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiQ9LIR4.
PRIDEiQ9LIR4.

PTM databases

SwissPalmiQ9LIR4.

Expressioni

Gene expression databases

ExpressionAtlasiQ9LIR4. baseline and differential.
GenevisibleiQ9LIR4. AT.

Interactioni

Protein-protein interaction databases

IntActiQ9LIR4. 1 interaction.
STRINGi3702.AT3G23940.1.

Structurei

3D structure databases

ProteinModelPortaliQ9LIR4.
SMRiQ9LIR4. Positions 26-607.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the IlvD/Edd family.UniRule annotation

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG2448. Eukaryota.
COG0129. LUCA.
HOGENOMiHOG000173155.
InParanoidiQ9LIR4.
KOiK01687.
OMAiGYEGNPC.
PhylomeDBiQ9LIR4.

Family and domain databases

HAMAPiMF_00012. IlvD.
InterProiIPR015928. Aconitase/3IPM_dehydase_swvl.
IPR004404. DihydroxyA_deHydtase.
IPR000581. DiOHA_6PGluconate_deHydtase.
IPR020558. DiOHA_6PGluconate_deHydtase_CS.
[Graphical view]
PANTHERiPTHR21000. PTHR21000. 1 hit.
PfamiPF00920. ILVD_EDD. 1 hit.
[Graphical view]
SUPFAMiSSF52016. SSF52016. 1 hit.
TIGRFAMsiTIGR00110. ilvD. 1 hit.
PROSITEiPS00886. ILVD_EDD_1. 1 hit.
PS00887. ILVD_EDD_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9LIR4-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MQATIFSPRA TLFPCKPLLP SHNVNSRRPS IISCSAQSVT ADPSPPITDT
60 70 80 90 100
NKLNKYSSRI TEPKSQGGSQ AILHGVGLSD DDLLKPQIGI SSVWYEGNTC
110 120 130 140 150
NMHLLKLSEA VKEGVENAGM VGFRFNTIGV SDAISMGTRG MCFSLQSRDL
160 170 180 190 200
IADSIETVMS AQWYDGNISI PGCDKNMPGT IMAMGRLNRP GIMVYGGTIK
210 220 230 240 250
PGHFQDKTYD IVSAFQSYGE FVSGSISDEQ RKTVLHHSCP GAGACGGMYT
260 270 280 290 300
ANTMASAIEA MGMSLPYSSS IPAEDPLKLD ECRLAGKYLL ELLKMDLKPR
310 320 330 340 350
DIITPKSLRN AMVSVMALGG STNAVLHLIA IARSVGLELT LDDFQKVSDA
360 370 380 390 400
VPFLADLKPS GKYVMEDIHK IGGTPAVLRY LLELGLMDGD CMTVTGQTLA
410 420 430 440 450
QNLENVPSLT EGQEIIRPLS NPIKETGHIQ ILRGDLAPDG SVAKITGKEG
460 470 480 490 500
LYFSGPALVF EGEESMLAAI SADPMSFKGT VVVIRGEGPK GGPGMPEMLT
510 520 530 540 550
PTSAIMGAGL GKECALLTDG RFSGGSHGFV VGHICPEAQE GGPIGLIKNG
560 570 580 590 600
DIITIDIGKK RIDTQVSPEE MNDRRKKWTA PAYKVNRGVL YKYIKNVQSA

SDGCVTDE
Length:608
Mass (Da):64,914
Last modified:October 1, 2000 - v1
Checksum:i017A5E0CD3CDFA69
GO
Isoform 2 (identifier: Q9LIR4-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     393-394: Missing.

Note: No experimental confirmation available. Derived from EST data.Curated
Show »
Length:606
Mass (Da):64,713
Checksum:i66313A4BDCFC2389
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti259 – 2591E → G in AAK64025 (PubMed:14593172).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei393 – 3942Missing in isoform 2. 1 PublicationVSP_056812

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP001297 Genomic DNA. Translation: BAB03011.1.
CP002686 Genomic DNA. Translation: AEE76834.1.
CP002686 Genomic DNA. Translation: AEE76835.1.
AF446360 mRNA. Translation: AAL48233.1.
BT000972 mRNA. Translation: AAN41372.1.
AY039921 mRNA. Translation: AAK64025.1.
RefSeqiNP_001189959.1. NM_001203030.1. [Q9LIR4-2]
NP_189036.1. NM_113299.4. [Q9LIR4-1]
UniGeneiAt.8280.

Genome annotation databases

EnsemblPlantsiAT3G23940.1; AT3G23940.1; AT3G23940. [Q9LIR4-1]
AT3G23940.2; AT3G23940.2; AT3G23940. [Q9LIR4-2]
GeneIDi821977.
KEGGiath:AT3G23940.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP001297 Genomic DNA. Translation: BAB03011.1.
CP002686 Genomic DNA. Translation: AEE76834.1.
CP002686 Genomic DNA. Translation: AEE76835.1.
AF446360 mRNA. Translation: AAL48233.1.
BT000972 mRNA. Translation: AAN41372.1.
AY039921 mRNA. Translation: AAK64025.1.
RefSeqiNP_001189959.1. NM_001203030.1. [Q9LIR4-2]
NP_189036.1. NM_113299.4. [Q9LIR4-1]
UniGeneiAt.8280.

3D structure databases

ProteinModelPortaliQ9LIR4.
SMRiQ9LIR4. Positions 26-607.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9LIR4. 1 interaction.
STRINGi3702.AT3G23940.1.

PTM databases

SwissPalmiQ9LIR4.

Proteomic databases

PaxDbiQ9LIR4.
PRIDEiQ9LIR4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT3G23940.1; AT3G23940.1; AT3G23940. [Q9LIR4-1]
AT3G23940.2; AT3G23940.2; AT3G23940. [Q9LIR4-2]
GeneIDi821977.
KEGGiath:AT3G23940.

Organism-specific databases

TAIRiAT3G23940.

Phylogenomic databases

eggNOGiKOG2448. Eukaryota.
COG0129. LUCA.
HOGENOMiHOG000173155.
InParanoidiQ9LIR4.
KOiK01687.
OMAiGYEGNPC.
PhylomeDBiQ9LIR4.

Enzyme and pathway databases

UniPathwayiUPA00047; UER00057.
UPA00049; UER00061.
BioCyciARA:AT3G23940-MONOMER.
ARA:GQT-1269-MONOMER.

Miscellaneous databases

PROiQ9LIR4.

Gene expression databases

ExpressionAtlasiQ9LIR4. baseline and differential.
GenevisibleiQ9LIR4. AT.

Family and domain databases

HAMAPiMF_00012. IlvD.
InterProiIPR015928. Aconitase/3IPM_dehydase_swvl.
IPR004404. DihydroxyA_deHydtase.
IPR000581. DiOHA_6PGluconate_deHydtase.
IPR020558. DiOHA_6PGluconate_deHydtase_CS.
[Graphical view]
PANTHERiPTHR21000. PTHR21000. 1 hit.
PfamiPF00920. ILVD_EDD. 1 hit.
[Graphical view]
SUPFAMiSSF52016. SSF52016. 1 hit.
TIGRFAMsiTIGR00110. ilvD. 1 hit.
PROSITEiPS00886. ILVD_EDD_1. 1 hit.
PS00887. ILVD_EDD_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC clones."
    Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.
    DNA Res. 7:217-221(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  2. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. ColumbiaImported.
  3. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
    Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.
    , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
    Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Strain: cv. Columbia.
  4. "Biosynthesis of branched chain amino acids: from test tube to field."
    Singh B.K., Shaner D.L.
    Plant Cell 7:935-944(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  5. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-35, CLEAVAGE OF TRANSIT PEPTIDE [LARGE SCALE ANALYSIS] AFTER CYS-34, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiILVD_ARATH
AccessioniPrimary (citable) accession number: Q9LIR4
Secondary accession number(s): F4J5B4, Q94BS6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 29, 2014
Last sequence update: October 1, 2000
Last modified: February 17, 2016
This is version 113 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

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. 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.