UniProtKB - P39522 (ILV3_YEAST)
Dihydroxy-acid dehydratase, mitochondrial
ILV3
Functioni
Dihydroxyacid dehydratase that catalyzes the third step in the common pathway leading to biosynthesis of branched-chain amino acids (PubMed:20008079, PubMed:21798060, PubMed:21987576, PubMed:22954227, PubMed:25280745, PubMed:26543501, PubMed:27532773, PubMed:28505306, PubMed:31303893, PubMed:30850698, PubMed:33620449, PubMed:8299945).
Catalyzes the dehydration of (2R,3R)-2,3-dihydroxy-3-methylpentanoate (2,3-dihydroxy-3-methylvalerate) into 2-oxo-3-methylpentanoate (2-oxo-3-methylvalerate) and of (2R)-2,3-dihydroxy-3-methylbutanoate (2,3-dihydroxyisovalerate) into 2-oxo-3-methylbutanoate (2-oxoisovalerate), the penultimate precursor to L-isoleucine and L-valine, respectively (PubMed:27532773, PubMed:20008079).
Required for the synthesis of alpha-isopropylmalate which modulates the activity of LEU3 and subsequently regulates the expression of LEU1 (PubMed:20008079).
1 Publication11 PublicationsMiscellaneous
Catalytic activityi
- EC:4.2.1.92 PublicationsThis reaction proceeds in the forward2 Publications direction.
- EC:4.2.1.9By similarityThis reaction proceeds in the forwardBy similarity direction.
Cofactori
Protein has several cofactor binding sites:- [2Fe-2S] cluster2 PublicationsNote: Binds 1 [2Fe-2S] cluster per subunit.2 Publications
- Mg2+By similarity
Activity regulationi
: L-isoleucine biosynthesis Pathwayi
This protein is involved in step 3 of the subpathway that synthesizes L-isoleucine from 2-oxobutanoate.Curated 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.Curated 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 key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Metal bindingi | 70 | Iron-sulfur (2Fe-2S)By similarity | 1 | |
Metal bindingi | 102 | MagnesiumBy similarity | 1 | |
Metal bindingi | 143 | Iron-sulfur (2Fe-2S)By similarity | 1 | |
Metal bindingi | 144 | MagnesiumBy similarity | 1 | |
Metal bindingi | 221 | Iron-sulfur (2Fe-2S)By similarity | 1 | |
Metal bindingi | 474 | MagnesiumBy similarity | 1 | |
Active sitei | 500 | Proton acceptorBy similarity | 1 |
GO - Molecular functioni
- 2 iron, 2 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 function | Lyase |
Biological process | Amino-acid biosynthesis, Branched-chain amino acid biosynthesis |
Ligand | 2Fe-2S, Iron, Iron-sulfur, Magnesium, Metal-binding |
Enzyme and pathway databases
UniPathwayi | UPA00047;UER00057 UPA00049;UER00061 |
Names & Taxonomyi
Protein namesi | Recommended name: Dihydroxy-acid dehydratase, mitochondrial1 Publication (EC:4.2.1.92 Publications)Short name: DAD1 Publication |
Gene namesi | Name:ILV31 Publication Ordered Locus Names:YJR016C ORF Names:J1450 |
Organismi | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
Taxonomic identifieri | 559292 [NCBI] |
Taxonomic lineagei | Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › |
Proteomesi |
|
Organism-specific databases
SGDi | S000003777, ILV3 |
VEuPathDBi | FungiDB:YJR016C |
Subcellular locationi
Mitochondrion
- Mitochondrion 2 Publications
Mitochondrion
- mitochondrion Source: SGD
Keywords - Cellular componenti
MitochondrionPathology & Biotechi
Biotechnological usei
Disruption phenotypei
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Transit peptidei | 1 – 20 | MitochondrionSequence analysisAdd BLAST | 20 | |
ChainiPRO_0000015636 | 21 – 585 | Dihydroxy-acid dehydratase, mitochondrialAdd BLAST | 565 |
Proteomic databases
MaxQBi | P39522 |
PaxDbi | P39522 |
PRIDEi | P39522 |
TopDownProteomicsi | P39522 |
PTM databases
iPTMneti | P39522 |
Expressioni
Inductioni
Interactioni
Protein-protein interaction databases
BioGRIDi | 33772, 139 interactors |
DIPi | DIP-6456N |
IntActi | P39522, 33 interactors |
MINTi | P39522 |
STRINGi | 4932.YJR016C |
Miscellaneous databases
RNActi | P39522, protein |
Family & Domainsi
Sequence similaritiesi
Keywords - Domaini
Transit peptidePhylogenomic databases
eggNOGi | KOG2448, Eukaryota |
HOGENOMi | CLU_014271_4_1_1 |
InParanoidi | P39522 |
OMAi | TQGRNMA |
Family and domain databases
Gene3Di | 3.50.30.80, 1 hit |
HAMAPi | MF_00012, IlvD, 1 hit |
InterProi | View protein in InterPro IPR042096, Dihydro-acid_dehy_C IPR004404, DihydroxyA_deHydtase IPR000581, DiOHA_6PGluconate_deHydtase IPR020558, DiOHA_6PGluconate_deHydtase_CS IPR037237, IlvD/EDD_N |
Pfami | View protein in Pfam PF00920, ILVD_EDD, 1 hit |
SUPFAMi | SSF143975, SSF143975, 1 hit |
TIGRFAMsi | TIGR00110, ilvD, 1 hit |
PROSITEi | View protein in PROSITE PS00886, ILVD_EDD_1, 1 hit PS00887, ILVD_EDD_2, 1 hit |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
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
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 82 – 89 | SQSIEKAG → MFSIIEKR in AAA34568 (PubMed:8299945).Curated | 8 | |
Sequence conflicti | 238 | G → S in AAA34568 (PubMed:8299945).Curated | 1 | |
Sequence conflicti | 242 | P → S in AAA34568 (PubMed:8299945).Curated | 1 | |
Sequence conflicti | 492 | A → T in AAA34568 (PubMed:8299945).Curated | 1 | |
Sequence conflicti | 520 | P → R in AAA34568 (PubMed:8299945).Curated | 1 | |
Sequence conflicti | 551 | R → A in AAA34568 (PubMed:8299945).Curated | 1 |
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 BK006943 Genomic DNA Translation: DAA08808.1 |
PIRi | S55205 |
RefSeqi | NP_012550.1, NM_001181674.1 |
Genome annotation databases
EnsemblFungii | YJR016C_mRNA; YJR016C; YJR016C |
GeneIDi | 853473 |
KEGGi | sce:YJR016C |
Similar proteinsi
Cross-referencesi
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 BK006943 Genomic DNA Translation: DAA08808.1 |
PIRi | S55205 |
RefSeqi | NP_012550.1, NM_001181674.1 |
3D structure databases
AlphaFoldDBi | P39522 |
SMRi | P39522 |
ModBasei | Search... |
Protein-protein interaction databases
BioGRIDi | 33772, 139 interactors |
DIPi | DIP-6456N |
IntActi | P39522, 33 interactors |
MINTi | P39522 |
STRINGi | 4932.YJR016C |
PTM databases
iPTMneti | P39522 |
Proteomic databases
MaxQBi | P39522 |
PaxDbi | P39522 |
PRIDEi | P39522 |
TopDownProteomicsi | P39522 |
Genome annotation databases
EnsemblFungii | YJR016C_mRNA; YJR016C; YJR016C |
GeneIDi | 853473 |
KEGGi | sce:YJR016C |
Organism-specific databases
SGDi | S000003777, ILV3 |
VEuPathDBi | FungiDB:YJR016C |
Phylogenomic databases
eggNOGi | KOG2448, Eukaryota |
HOGENOMi | CLU_014271_4_1_1 |
InParanoidi | P39522 |
OMAi | TQGRNMA |
Enzyme and pathway databases
UniPathwayi | UPA00047;UER00057 UPA00049;UER00061 |
Miscellaneous databases
PROi | PR:P39522 |
RNActi | P39522, protein |
Family and domain databases
Gene3Di | 3.50.30.80, 1 hit |
HAMAPi | MF_00012, IlvD, 1 hit |
InterProi | View protein in InterPro IPR042096, Dihydro-acid_dehy_C IPR004404, DihydroxyA_deHydtase IPR000581, DiOHA_6PGluconate_deHydtase IPR020558, DiOHA_6PGluconate_deHydtase_CS IPR037237, IlvD/EDD_N |
Pfami | View protein in Pfam PF00920, ILVD_EDD, 1 hit |
SUPFAMi | SSF143975, SSF143975, 1 hit |
TIGRFAMsi | TIGR00110, ilvD, 1 hit |
PROSITEi | View protein in PROSITE PS00886, ILVD_EDD_1, 1 hit PS00887, ILVD_EDD_2, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | ILV3_YEAST | |
Accessioni | P39522Primary (citable) accession number: P39522 Secondary accession number(s): D6VWJ2 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | February 1, 1995 |
Last sequence update: | November 1, 1995 | |
Last modified: | May 25, 2022 | |
This is version 175 of the entry and version 2 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Fungal Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
Reference proteomeDocuments
- Yeast
Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD - Yeast chromosome X
Yeast (Saccharomyces cerevisiae) chromosome X: entries and gene names - PATHWAY comments
Index of metabolic and biosynthesis pathways - SIMILARITY comments
Index of protein domains and families