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   25-NOV-2008, entry version 57.
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; Magnoliophyta; eudicotyledons; core eudicotyledons;
OC   rosids; eurosids II; Brassicales; Brassicaceae; Brassica.
OX   NCBI_TaxID=3708;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Svalofs Karat 20516-K;
RX   MEDLINE=92163020; 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
RT   dehydrogenase by 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
CC       oxopentanoate.
CC   -!- CATALYTIC ACTIVITY: (2R,3S)-3-isopropylmalate + NAD(+) = 4-methyl-
CC       2-oxopentanoate + CO(2) + NADH.
CC   -!- COFACTOR: Binds 1 magnesium or manganese ion per subunit (By
CC       similarity).
CC   -!- PATHWAY: Amino-acid biosynthesis; L-leucine biosynthesis; L-
CC       leucine from 3-methyl-2-oxobutanoate: step 3/4.
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC   -!- SIMILARITY: Belongs to the isocitrate and isopropylmalate
CC       dehydrogenases family.
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DR   EMBL; X59970; CAA42596.1; -; mRNA.
DR   PIR; S20510; S20510.
DR   HSSP; Q56268; 1A05.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-KW.
DR   GO; GO:0003862; F:3-isopropylmalate dehydrogenase activity; IEA:InterPro.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0009098; P:leucine biosynthetic process; IEA:InterPro.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR004429; 3-isopropylmalate_DHase.
DR   InterPro; IPR001804; IsoCit_IM_DHase.
DR   Gene3D; G3DSA:3.40.718.10; IDH_IMDH; 1.
DR   PANTHER; PTHR11835; IDH_IMDH_dimeric; 1.
DR   PANTHER; PTHR11835:SF13; IPMDH; 1.
DR   Pfam; PF00180; 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;
KW   Metal-binding; NAD; Oxidoreductase; Plastid; Transit peptide.
FT   TRANSIT       1     34       Chloroplast (Potential).
FT   CHAIN        35    406       3-isopropylmalate dehydrogenase,
FT                                chloroplastic.
FT                                /FTId=PRO_0000014456.
FT   NP_BIND     117    130       NAD (By similarity).
FT   NP_BIND     323    335       NAD (By similarity).
FT   METAL       265    265       Magnesium or manganese (By similarity).
FT   METAL       289    289       Magnesium or manganese (By similarity).
FT   METAL       293    293       Magnesium or manganese (By similarity).
FT   BINDING     137    137       Substrate (By similarity).
FT   BINDING     147    147       Substrate (By similarity).
FT   BINDING     175    175       Substrate (By similarity).
FT   BINDING     265    265       Substrate (By similarity).
FT   SITE        182    182       Important for catalysis (By similarity).
FT   SITE        233    233       Important for catalysis (By similarity).
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
//