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Protein

3-isopropylmalate dehydratase

Gene

LEU1

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

Functioni

Catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate.

Miscellaneous

Present with 96300 molecules/cell in log phase SD medium.1 Publication

Catalytic activityi

(2R,3S)-3-isopropylmalate = (2S)-2-isopropylmalate.

Cofactori

[4Fe-4S] clusterBy similarityNote: Binds 1 [4Fe-4S] cluster per subunit.By similarity

Pathwayi: L-leucine biosynthesis

This protein is involved in step 2 of the subpathway that synthesizes L-leucine from 3-methyl-2-oxobutanoate.
Proteins known to be involved in the 4 steps of the subpathway in this organism are:
  1. 2-isopropylmalate synthase (LEU4), 2-isopropylmalate synthase 2, mitochondrial (LEU9)
  2. 3-isopropylmalate dehydratase (LEU1)
  3. 3-isopropylmalate dehydrogenase (LEU2)
  4. Branched-chain-amino-acid aminotransferase, mitochondrial (BAT1), Branched-chain-amino-acid aminotransferase, cytosolic (BAT2)
This subpathway is part of the pathway L-leucine 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-leucine from 3-methyl-2-oxobutanoate, the pathway L-leucine biosynthesis and in Amino-acid biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi360Iron-sulfur (4Fe-4S)By similarity1
Metal bindingi421Iron-sulfur (4Fe-4S)By similarity1
Metal bindingi424Iron-sulfur (4Fe-4S)By similarity1

GO - Molecular functioni

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

GO - Biological processi

  • leucine biosynthetic process Source: SGD

Keywordsi

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

Enzyme and pathway databases

BioCyciYEAST:YGL009C-MONOMER
UniPathwayiUPA00048; UER00071

Names & Taxonomyi

Protein namesi
Recommended name:
3-isopropylmalate dehydratase (EC:4.2.1.33)
Alternative name(s):
Alpha-IPM isomerase
Short name:
IPMI
Isopropylmalate isomerase
Gene namesi
Name:LEU1
Ordered Locus Names:YGL009C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome VII

Organism-specific databases

EuPathDBiFungiDB:YGL009C
SGDiS000002977 LEU1

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000768941 – 7793-isopropylmalate dehydrataseAdd BLAST779

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei488PhosphoserineCombined sources1
Modified residuei494PhosphothreonineCombined sources1
Modified residuei495PhosphoserineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP07264
PaxDbiP07264
PRIDEiP07264

PTM databases

iPTMnetiP07264

Interactioni

Subunit structurei

Monomer.

Protein-protein interaction databases

BioGridi33237, 84 interactors
DIPiDIP-6715N
IntActiP07264, 10 interactors
MINTiP07264
STRINGi4932.YGL009C

Structurei

3D structure databases

ProteinModelPortaliP07264
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the aconitase/IPM isomerase family.Curated

Phylogenomic databases

GeneTreeiENSGT00730000114222
HOGENOMiHOG000226972
InParanoidiP07264
KOiK01702
OMAiTHATVDH
OrthoDBiEOG092C0T13

Family and domain databases

CDDicd01583 IPMI, 1 hit
cd01577 IPMI_Swivel, 1 hit
Gene3Di3.20.19.10, 1 hit
3.30.499.10, 1 hit
HAMAPiMF_01026 LeuC_type1, 1 hit
MF_01031 LeuD_type1, 1 hit
InterProiView protein in InterPro
IPR004430 3-IsopropMal_deHydase_lsu
IPR004431 3-IsopropMal_deHydase_ssu
IPR012235 3-IsopropMal_deHydtase_ssu/lsu
IPR015931 Acnase/IPM_dHydase_lsu_aba_1/3
IPR001030 Acoase/IPM_deHydtase_lsu_aba
IPR015928 Aconitase/3IPM_dehydase_swvl
IPR018136 Aconitase_4Fe-4S_BS
IPR036008 Aconitase_4Fe-4S_dom
IPR000573 AconitaseA/IPMdHydase_ssu_swvl
IPR033941 IPMI_cat
IPR033940 IPMI_Swivel
PfamiView protein in Pfam
PF00330 Aconitase, 1 hit
PF00694 Aconitase_C, 1 hit
PIRSFiPIRSF001418 ACN, 1 hit
PRINTSiPR00415 ACONITASE
SUPFAMiSSF53732 SSF53732, 1 hit
TIGRFAMsiTIGR00170 leuC, 1 hit
TIGR00171 leuD, 1 hit
PROSITEiView protein in PROSITE
PS00450 ACONITASE_1, 1 hit
PS01244 ACONITASE_2, 1 hit

Sequencei

Sequence statusi: Complete.

P07264-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVYTPSKGPR TLYDKVFDAH VVHQDENGSF LLYIDRHLVH EVTSPQAFEG
60 70 80 90 100
LENAGRKVRR VDCTLATVDH NIPTESRKNF KSLDTFIKQT DSRLQVKTLE
110 120 130 140 150
NNVKQFGVPY FGMSDARQGI VHTIGPEEGF TLPGTTVVCG DSHTSTHGAF
160 170 180 190 200
GSLAFGIGTS EVEHVLATQT IIQAKSKNMR ITVNGKLSPG ITSKDLILYI
210 220 230 240 250
IGLIGTAGGT GCVIEFAGEA IEALSMEARM SMCNMAIEAG ARAGMIKPDE
260 270 280 290 300
TTFQYTKGRP LAPKGAEWEK AVAYWKTLKT DEGAKFDHEI NIEAVDVIPT
310 320 330 340 350
ITWGTSPQDA LPITGSVPDP KNVTDPIKKS GMERALAYMG LEPNTPLKSI
360 370 380 390 400
KVDKVFIGSC TNGRIEDLRS AAAVVRGQKL ASNIKLAMVV PGSGLVKKQA
410 420 430 440 450
EAEGLDKIFQ EAGFEWREAG CSICLGMNPD ILDAYERCAS TSNRNFEGRQ
460 470 480 490 500
GALSRTHLMS PAMAAAAGIA GHFVDIREFE YKDQDQSSPK VEVTSEDEKE
510 520 530 540 550
LESAAYDHAE PVQPEDAPQD IANDELKDIP VKSDDTPAKP SSSGMKPFLT
560 570 580 590 600
LEGISAPLDK ANVDTDAIIP KQFLKTIKRT GLKKGLFYEW RFRKDDQGKD
610 620 630 640 650
QETDFVLNVE PWREAEILVV TGDNFGCGSS REHAPWALKD FGIKSIIAPS
660 670 680 690 700
YGDIFYNNSF KNGLLPIRLD QQIIIDKLIP IANKGGKLCV DLPNQKILDS
710 720 730 740 750
DGNVLVDHFE IEPFRKHCLV NGLDDIGITL QKEEYISRYE ALRREKYSFL
760 770
EGGSKLLKFD NVPKRKAVTT TFDKVHQDW
Length:779
Mass (Da):85,794
Last modified:October 1, 1996 - v3
Checksum:iBD409A9702AE3E57
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti291N → TLKH in AAB19612 (PubMed:1840714).Curated1
Sequence conflicti423I → M in AAB19612 (PubMed:1840714).Curated1
Sequence conflicti459M → I in AAB19612 (PubMed:1840714).Curated1
Sequence conflicti744R → K in AAB19612 (PubMed:1840714).Curated1
Sequence conflicti744R → K in S58126 (PubMed:1882553).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S57886 Genomic DNA Translation: AAB19612.1
Z72531 Genomic DNA Translation: CAA96709.1
K01969 Genomic DNA Translation: AAA34742.1
S58126 Genomic DNA No translation available.
BK006941 Genomic DNA Translation: DAA08089.1
PIRiS64011
RefSeqiNP_011506.1, NM_001180874.1

Genome annotation databases

EnsemblFungiiYGL009C; YGL009C; YGL009C
GeneIDi852875
KEGGisce:YGL009C

Similar proteinsi

Entry informationi

Entry nameiLEUC_YEAST
AccessioniPrimary (citable) accession number: P07264
Secondary accession number(s): D6VUC8
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: October 1, 1996
Last modified: May 23, 2018
This is version 181 of the entry and version 3 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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