ID   LEU3_SOLTU              Reviewed;         357 AA.
AC   P29696;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   03-AUG-2022, entry version 125.
DE   RecName: Full=3-isopropylmalate dehydrogenase, chloroplastic;
DE            Short=3-IPM-DH;
DE            Short=IMDH;
DE            EC=1.1.1.85;
DE   AltName: Full=Beta-IPM dehydrogenase;
DE   Flags: Precursor;
OS   Solanum tuberosum (Potato).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum.
OX   NCBI_TaxID=4113;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Desiree; TISSUE=Leaf;
RX   PubMed=8437576; DOI=10.1007/bf00277127;
RA   Jackson S.D., Sonnewald U., Willmitzer L.;
RT   "Cloning and expression analysis of beta-isopropylmalate dehydrogenase from
RT   potato.";
RL   Mol. Gen. Genet. 236:309-314(1993).
CC   -!- FUNCTION: Catalyzes the oxidation of 3-carboxy-2-hydroxy-4-
CC       methylpentanoate (3-isopropylmalate) to 3-carboxy-4-methyl-2-
CC       oxopentanoate. The product decarboxylates to 4-methyl-2 oxopentanoate.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2R,3S)-3-isopropylmalate + NAD(+) = 4-methyl-2-oxopentanoate
CC         + CO2 + NADH; Xref=Rhea:RHEA:32271, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:17865, ChEBI:CHEBI:35121, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945; EC=1.1.1.85;
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC       Note=Binds 1 Mg(2+) or Mn(2+) ion per subunit. {ECO:0000250};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine
CC       from 3-methyl-2-oxobutanoate: step 3/4.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC   -!- SIMILARITY: Belongs to the isocitrate and isopropylmalate
CC       dehydrogenases family. {ECO:0000305}.
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DR   EMBL; X67310; CAA47720.1; -; mRNA.
DR   PIR; S30897; S30897.
DR   RefSeq; NP_001305547.1; NM_001318618.1.
DR   AlphaFoldDB; P29696; -.
DR   SMR; P29696; -.
DR   STRING; 4113.PGSC0003DMT400067503; -.
DR   PRIDE; P29696; -.
DR   ProMEX; P29696; -.
DR   GeneID; 102592957; -.
DR   KEGG; sot:102592957; -.
DR   eggNOG; KOG0785; Eukaryota.
DR   UniPathway; UPA00048; UER00072.
DR   Proteomes; UP000011115; Unassembled WGS sequence.
DR   ExpressionAtlas; P29696; baseline.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0003862; F:3-isopropylmalate dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004449; F:isocitrate dehydrogenase (NAD+) activity; IBA:GO_Central.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0006102; P:isocitrate metabolic process; IBA:GO_Central.
DR   GO; GO:0009098; P:leucine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IBA:GO_Central.
DR   InterPro; IPR019818; IsoCit/isopropylmalate_DH_CS.
DR   InterPro; IPR004434; Isocitrate_DH_NAD.
DR   InterPro; IPR024084; IsoPropMal-DH-like_dom.
DR   Pfam; PF00180; Iso_dh; 1.
DR   SMART; SM01329; Iso_dh; 1.
DR   TIGRFAMs; TIGR00175; mito_nad_idh; 1.
DR   PROSITE; PS00470; IDH_IMDH; 1.
PE   2: Evidence at transcript level;
KW   Amino-acid biosynthesis; Branched-chain amino acid biosynthesis;
KW   Chloroplast; Leucine biosynthesis; Magnesium; Manganese; Metal-binding;
KW   NAD; Oxidoreductase; Plastid; Reference proteome; Transit peptide.
FT   TRANSIT         1..29
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           30..357
FT                   /note="3-isopropylmalate dehydrogenase, chloroplastic"
FT                   /id="PRO_0000014457"
FT   BINDING         120
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         130
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         151
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         238
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         238
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         262
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         266
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         296..308
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   SITE            158
FT                   /note="Important for catalysis"
FT                   /evidence="ECO:0000250"
FT   SITE            205
FT                   /note="Important for catalysis"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   357 AA;  39766 MW;  A37CDEE42EE118E6 CRC64;
     MALQIAKRLL RCRADSVASS VRFFDRTFTS ESNSNLIRAT LFPGDGIGPE IAESVRQIFK
     VAEVPIEWEE HYVGTEVDPR TNSFLTWESL ESVRRNKVGL KGPMATPIGK GHRSLNLTLR
     KELNLYANVR PCYSLPGYKT RYDDVNLITI RENTEGEYSG LEHQVVRGVV ESLKIITRQA
     SLRVAEYAFH YAKTHGRERV SAIHKANIMQ KTDGLFLKCC REVAEKYPEI KYEEVVIDNC
     CMMLVKNPAL FDVLVMPNLY GDIISDLCAG LIGGLGLTPS CNIGEGGIAL AEAVHGSAPD
     IAGKNLANPT ALLLSSVSML RHLELHDKAD RIQDAILKTI AGGKVPNWRP WRHCYNN