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Protein

Dihydroxy-acid dehydratase, mitochondrial

Gene

ILV3

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Miscellaneous

Present with 171000 molecules/cell in log phase SD medium.1 Publication

Catalytic activityi

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

Cofactori

[4Fe-4S] clusterCuratedNote: Binds 1 [4Fe-4S] cluster.Curated

Pathwayi: L-isoleucine biosynthesis

This protein is involved in step 3 of the subpathway that synthesizes L-isoleucine from 2-oxobutanoate.
Proteins known to be involved in the 4 steps of the subpathway in this organism are:
  1. Acetolactate synthase small subunit, mitochondrial (ILV6), Acetolactate synthase catalytic subunit, mitochondrial (ILV2)
  2. Ketol-acid reductoisomerase, mitochondrial (ILV5)
  3. Dihydroxy-acid dehydratase, mitochondrial (ILV3)
  4. Branched-chain-amino-acid aminotransferase, mitochondrial (BAT1), Branched-chain-amino-acid aminotransferase, cytosolic (BAT2)
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.
Proteins known to be involved in the 4 steps of the subpathway in this organism are:
  1. Acetolactate synthase small subunit, mitochondrial (ILV6), Acetolactate synthase catalytic subunit, mitochondrial (ILV2)
  2. Ketol-acid reductoisomerase, mitochondrial (ILV5)
  3. Dihydroxy-acid dehydratase, mitochondrial (ILV3)
  4. Branched-chain-amino-acid aminotransferase, mitochondrial (BAT1), Branched-chain-amino-acid aminotransferase, cytosolic (BAT2)
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)DescriptionActionsGraphical viewLength
Metal bindingi143Iron-sulfur (4Fe-4S)Sequence analysis1
Metal bindingi221Iron-sulfur (4Fe-4S)Sequence analysis1

GO - Molecular functioni

  • 4 iron, 4 sulfur cluster binding Source: UniProtKB-KW
  • dihydroxy-acid dehydratase activity Source: SGD
  • metal ion binding Source: UniProtKB-KW

GO - Biological processi

  • branched-chain amino acid biosynthetic process Source: SGD
  • isoleucine biosynthetic process Source: UniProtKB-UniPathway
  • valine biosynthetic process Source: UniProtKB-UniPathway

Keywordsi

Molecular functionLyase
Biological processAmino-acid biosynthesis, Branched-chain amino acid biosynthesis
Ligand4Fe-4S, Iron, Iron-sulfur, Metal-binding

Enzyme and pathway databases

BioCyciYEAST:YJR016C-MONOMER
UniPathwayiUPA00047; UER00057
UPA00049; UER00061

Names & Taxonomyi

Protein namesi
Recommended name:
Dihydroxy-acid dehydratase, mitochondrial (EC:4.2.1.9)
Short name:
DAD
Alternative name(s):
2,3-dihydroxy acid hydrolyase
Gene namesi
Name:ILV3
Ordered Locus Names:YJR016C
ORF Names:J1450
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome X

Organism-specific databases

EuPathDBiFungiDB:YJR016C
SGDiS000003777 ILV3

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_0000015636? – 585Dihydroxy-acid dehydratase, mitochondrial
Transit peptidei1 – ?MitochondrionSequence analysis

Proteomic databases

MaxQBiP39522
PaxDbiP39522
PRIDEiP39522
TopDownProteomicsiP39522

PTM databases

iPTMnetiP39522

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

BioGridi33772, 131 interactors
DIPiDIP-6456N
IntActiP39522, 33 interactors
MINTiP39522
STRINGi4932.YJR016C

Structurei

3D structure databases

ProteinModelPortaliP39522
SMRiP39522
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the IlvD/Edd family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

HOGENOMiHOG000173155
InParanoidiP39522
KOiK01687
OMAiIPGHVHL
OrthoDBiEOG092C1HK3

Family and domain databases

HAMAPiMF_00012 IlvD, 1 hit
InterProiView protein in InterPro
IPR004404 DihydroxyA_deHydtase
IPR000581 DiOHA_6PGluconate_deHydtase
IPR020558 DiOHA_6PGluconate_deHydtase_CS
IPR037237 IlvD/EDD_N
PfamiView protein in Pfam
PF00920 ILVD_EDD, 1 hit
SUPFAMiSSF143975 SSF143975, 1 hit
TIGRFAMsiTIGR00110 ilvD, 1 hit
PROSITEiView protein in PROSITE
PS00886 ILVD_EDD_1, 1 hit
PS00887 ILVD_EDD_2, 1 hit

Sequencei

Sequence statusi: Complete.

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

P39522-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGLLTKVATS RQFSTTRCVA KKLNKYSYII TEPKGQGASQ AMLYATGFKK
60 70 80 90 100
EDFKKPQVGV GSCWWSGNPC NMHLLDLNNR CSQSIEKAGL KAMQFNTIGV
110 120 130 140 150
SDGISMGTKG MRYSLQSREI IADSFETIMM AQHYDANIAI PSCDKNMPGV
160 170 180 190 200
MMAMGRHNRP SIMVYGGTIL PGHPTCGSSK ISKNIDIVSA FQSYGEYISK
210 220 230 240 250
QFTEEEREDV VEHACPGPGS CGGMYTANTM ASAAEVLGLT IPNSSSFPAV
260 270 280 290 300
SKEKLAECDN IGEYIKKTME LGILPRDILT KEAFENAITY VVATGGSTNA
310 320 330 340 350
VLHLVAVAHS AGVKLSPDDF QRISDTTPLI GDFKPSGKYV MADLINVGGT
360 370 380 390 400
QSVIKYLYEN NMLHGNTMTV TGDTLAERAK KAPSLPEGQE IIKPLSHPIK
410 420 430 440 450
ANGHLQILYG SLAPGGAVGK ITGKEGTYFK GRARVFEEEG AFIEALERGE
460 470 480 490 500
IKKGEKTVVV IRYEGPRGAP GMPEMLKPSS ALMGYGLGKD VALLTDGRFS
510 520 530 540 550
GGSHGFLIGH IVPEAAEGGP IGLVRDGDEI IIDADNNKID LLVSDKEMAQ
560 570 580
RKQSWVAPPP RYTRGTLSKY AKLVSNASNG CVLDA
Length:585
Mass (Da):62,861
Last modified:November 1, 1995 - v2
Checksum:i35AB3C679BA6E8D0
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti82 – 89SQSIEKAG → MFSIIEKR in AAA34568 (PubMed:8299945).Curated8
Sequence conflicti238G → S in AAA34568 (PubMed:8299945).Curated1
Sequence conflicti242P → S in AAA34568 (PubMed:8299945).Curated1
Sequence conflicti492A → T in AAA34568 (PubMed:8299945).Curated1
Sequence conflicti520P → R in AAA34568 (PubMed:8299945).Curated1
Sequence conflicti551R → A in AAA34568 (PubMed:8299945).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X87611 Genomic DNA Translation: CAA60939.1
Z49516 Genomic DNA Translation: CAA89540.1
L13975 Genomic DNA Translation: AAA34568.1 Different termination.
BK006943 Genomic DNA Translation: DAA08808.1
PIRiS55205
RefSeqiNP_012550.1, NM_001181674.1

Genome annotation databases

EnsemblFungiiYJR016C; YJR016C; YJR016C
GeneIDi853473
KEGGisce:YJR016C

Similar proteinsi

Entry informationi

Entry nameiILV3_YEAST
AccessioniPrimary (citable) accession number: P39522
Secondary accession number(s): D6VWJ2
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: November 1, 1995
Last modified: May 23, 2018
This is version 154 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

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