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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: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi143 – 1431Iron-sulfur (4Fe-4S)Sequence analysis
Metal bindingi221 – 2211Iron-sulfur (4Fe-4S)Sequence analysis

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
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

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

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini? – 585Dihydroxy-acid dehydratase, mitochondrialPRO_0000015636
Transit peptidei1 – ?MitochondrionSequence analysis

Proteomic databases

MaxQBiP39522.
PRIDEiP39522.
TopDownProteomicsiP39522.

PTM databases

iPTMnetiP39522.

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

BioGridi33772. 120 interactions.
DIPiDIP-6456N.
IntActiP39522. 32 interactions.
MINTiMINT-700348.

Structurei

3D structure databases

ProteinModelPortaliP39522.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the IlvD/Edd family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

HOGENOMiHOG000173155.
InParanoidiP39522.
KOiK01687.
OMAiGYEGNPC.
OrthoDBiEOG7966RD.

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]

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti82 – 898SQSIEKAG → MFSIIEKR in AAA34568 (PubMed:8299945).Curated
Sequence conflicti238 – 2381G → S in AAA34568 (PubMed:8299945).Curated
Sequence conflicti242 – 2421P → S in AAA34568 (PubMed:8299945).Curated
Sequence conflicti492 – 4921A → T in AAA34568 (PubMed:8299945).Curated
Sequence conflicti520 – 5201P → R in AAA34568 (PubMed:8299945).Curated
Sequence conflicti551 – 5511R → A in AAA34568 (PubMed:8299945).Curated

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.

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. Different termination.
BK006943 Genomic DNA. Translation: DAA08808.1.
PIRiS55205.
RefSeqiNP_012550.1. NM_001181674.1.

3D structure databases

ProteinModelPortaliP39522.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi33772. 120 interactions.
DIPiDIP-6456N.
IntActiP39522. 32 interactions.
MINTiMINT-700348.

PTM databases

iPTMnetiP39522.

Proteomic databases

MaxQBiP39522.
PRIDEiP39522.
TopDownProteomicsiP39522.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYJR016C; YJR016C; YJR016C.
GeneIDi853473.
KEGGisce:YJR016C.

Organism-specific databases

EuPathDBiFungiDB:YJR016C.
SGDiS000003777. ILV3.

Phylogenomic databases

HOGENOMiHOG000173155.
InParanoidiP39522.
KOiK01687.
OMAiGYEGNPC.
OrthoDBiEOG7966RD.

Enzyme and pathway databases

UniPathwayiUPA00047; UER00057.
UPA00049; UER00061.
BioCyciYEAST:YJR016C-MONOMER.

Miscellaneous databases

PROiP39522.

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. "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X."
    Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C., Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D., Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J., Heumann K.
    , Hilger F., Hollenberg C.P., Huang M.-E., Jacq C., Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E., Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T., Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R., Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N., To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H., von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.
    EMBO J. 15:2031-2049(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  3. "Cloning of the dihydroxyacid dehydratase-encoding gene (ILV3) from Saccharomyces cerevisiae."
    Velasco J.A., Cansado J., Pena M.C., Kawakami T., Laborda J., Notario V.
    Gene 137:179-185(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 82-585.
    Strain: ATCC 26109 / X2180.
  4. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiILV3_YEAST
AccessioniPrimary (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: July 6, 2016
This is version 139 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

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

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome X
    Yeast (Saccharomyces cerevisiae) chromosome X: entries and gene names

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.