ID   LEU3_BRANA              Reviewed;         406 AA.
AC   P29102;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-1992, sequence version 1.
DT   03-AUG-2022, entry version 110.
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   Brassica napus (Rape).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX   NCBI_TaxID=3708;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Svalofs Karat 20516-K;
RX   PubMed=1371407; DOI=10.1007/bf00040671;
RA   Ellerstroem M., Josefsson L.G., Rask L., Ronne H.;
RT   "Cloning of a cDNA for rape chloroplast 3-isopropylmalate dehydrogenase by
RT   genetic complementation in yeast.";
RL   Plant Mol. Biol. 18:557-566(1992).
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; X59970; CAA42596.1; -; mRNA.
DR   PIR; S20510; S20510.
DR   RefSeq; NP_001303020.1; NM_001316091.1.
DR   AlphaFoldDB; P29102; -.
DR   SMR; P29102; -.
DR   GeneID; 106398379; -.
DR   KEGG; bna:106398379; -.
DR   BRENDA; 1.1.1.85; 944.
DR   UniPathway; UPA00048; UER00072.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0003862; F:3-isopropylmalate dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0009098; P:leucine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   HAMAP; MF_01033; LeuB_type1; 1.
DR   InterPro; IPR019818; IsoCit/isopropylmalate_DH_CS.
DR   InterPro; IPR024084; IsoPropMal-DH-like_dom.
DR   InterPro; IPR004429; Isopropylmalate_DH.
DR   PANTHER; PTHR42979; PTHR42979; 1.
DR   Pfam; PF00180; Iso_dh; 1.
DR   SMART; SM01329; Iso_dh; 1.
DR   TIGRFAMs; TIGR00169; leuB; 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; Phosphoprotein; Plastid; Transit peptide.
FT   TRANSIT         1..34
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           35..406
FT                   /note="3-isopropylmalate dehydrogenase, chloroplastic"
FT                   /id="PRO_0000014456"
FT   BINDING         117..130
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         137
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         147
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         175
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         265
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         265
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         289
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         293
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         323..335
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   SITE            182
FT                   /note="Important for catalysis"
FT                   /evidence="ECO:0000250"
FT   SITE            233
FT                   /note="Important for catalysis"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         71
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9FMT1"
SQ   SEQUENCE   406 AA;  43351 MW;  2C8CCEA3B28FF192 CRC64;
     MAAALQTNIR PVKFPATLRA LTKQSSPAPF RVRCAAASPG KKRYNITLLP GDGIGPEVIS
     IAKNVLQQAG SLEGLEFSFQ EMPVGGAALD LVGVPLPEET VSAAKESDAV LLGAIGGYKW
     DKNEKHLKPE TGLLQLRAGL KVFANLRPAT VLPQLVDAST LKREVAEGVD LMVVRELTGG
     IYFGVPRGIK TNENGEEVGY NTEVYAAHEI DRIARVAFET ARKRRGKLCS VDKANVLDAS
     ILWRRRVTAL AAEYPDVELS HMYVDNAAMQ LVRDPKQFDT IVTNNIFGDI LSDEASMITG
     SIGMLPSASL SDSGPGLFEP IHGSAPDIAG QDKANPLATI LSAAMLLKYG LGEEKAAKRI
     EDAVLGALNK GFRTGDIYSA GTKLVGCKEM GEEVLKSVDS HVQASV