ID   LEU3_ZYMTR              Reviewed;         365 AA.
AC   Q9Y897;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=3-isopropylmalate dehydrogenase;
DE            Short=3-IPM-DH;
DE            Short=IMDH;
DE            EC=1.1.1.85;
DE   AltName: Full=Beta-IPM dehydrogenase;
GN   Name=LEUC;
OS   Zymoseptoria tritici (Speckled leaf blotch fungus) (Septoria tritici).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Zymoseptoria.
OX   NCBI_TaxID=1047171;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Strit1;
RA   Skinner W.S., Hargreaves J.A., Bailey A.M.;
RT   "A gene encoding 3-isopropylmalate dehydrogenase from the wheat leaf spot
RT   pathogen Mycosphaerella graminicola.";
RL   Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases.
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: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the isocitrate and isopropylmalate
CC       dehydrogenases family. {ECO:0000305}.
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DR   EMBL; AF156181; AAD40111.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9Y897; -.
DR   SMR; Q9Y897; -.
DR   PRIDE; Q9Y897; -.
DR   VEuPathDB; FungiDB:ZT3D1_G2658; -.
DR   VEuPathDB; FungiDB:ZTRI_2.512; -.
DR   OMA; EYDLGAR; -.
DR   BRENDA; 1.1.1.85; 7075.
DR   UniPathway; UPA00048; UER00072.
DR   GO; GO:0005737; C:cytoplasm; 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   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   3: Inferred from homology;
KW   Amino-acid biosynthesis; Branched-chain amino acid biosynthesis; Cytoplasm;
KW   Leucine biosynthesis; Magnesium; Manganese; Metal-binding; NAD;
KW   Oxidoreductase.
FT   CHAIN           1..365
FT                   /note="3-isopropylmalate dehydrogenase"
FT                   /id="PRO_0000083612"
FT   BINDING         78..89
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         96
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         106
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         135
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         224
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         224
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         249
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         253
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         289..301
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   SITE            142
FT                   /note="Important for catalysis"
FT                   /evidence="ECO:0000250"
FT   SITE            191
FT                   /note="Important for catalysis"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   365 AA;  38760 MW;  C4C0DE1F0A8E019D CRC64;
     MPTYNIVVFG GDHCGPEVTA EALKVLDVID NSNADVHFNI QPHLLGGASI DAHGEPLTDE
     ALAAAKAADA VILGAIGGPK WGTGKVRPEQ GILRLRKEMG TYGNLRPCFF ASESLVKTSP
     LKEEVCRGVN FNIVRELTGG IYFGERTEDD GSGYAVDTEP YSRAEIERVA RLAGFLALAE
     DPPCPVWSLD KANVMATSRL WRKTVTDVFA NEFPQLKIGH HLIDSAAMLM VKNPRALNGV
     IVTSNLFGDI ISDEASVIPG SLGLLPSASL TASPDGKSKC NGIYEPIHGS APDISGKGIV
     NPVAMILSLG MMCKYSLQQP ELAKKIDEAV RNVIEKGINT ADIGGSAKTA EVGDAIAKEL
     EALLK