ID   LEU3_KODOH              Reviewed;         368 AA.
AC   P41926;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 97.
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=LEU2;
OS   Kodamaea ohmeri (Yeast) (Yamadazyma ohmeri).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Kodamaea.
OX   NCBI_TaxID=34356;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=7725795; DOI=10.1002/yea.320101209;
RA   Piredda S., Gaillardin C.;
RT   "Development of a transformation system for the yeast Yamadazyma (Pichia)
RT   ohmeri.";
RL   Yeast 10:1601-1612(1994).
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; Z35101; CAA84484.1; -; Genomic_DNA.
DR   PIR; S50698; S50698.
DR   AlphaFoldDB; P41926; -.
DR   SMR; P41926; -.
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..368
FT                   /note="3-isopropylmalate dehydrogenase"
FT                   /id="PRO_0000083620"
FT   BINDING         77..88
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         95
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         105
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         134
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         226
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         226
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         251
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         255
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         290..301
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   SITE            141
FT                   /note="Important for catalysis"
FT                   /evidence="ECO:0000250"
FT   SITE            193
FT                   /note="Important for catalysis"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   368 AA;  39315 MW;  5E33ECBBA2CBD84D CRC64;
     MSTKTITVVP GDHVGTEICD EAIKVLKAIE KVSPVKFEFK HHLIGGAAID ATGVPLPDET
     LEAAKSSDAV LLGAVGGPKW GTGAVRPEQG LLKIRKELNL YANLRPCNFV SDSLLELSPL
     KSEIVKGTNF TVVRELVGGI YFGERQEQEE SSDGQSAWDT EKYSVEEVTR ITRMAAFMAL
     QHNPPLPIWS LDKANVLALS RLWRKTVDHV MSTEFPQLKV QHQLIDSAAM ILVKSPSQLN
     GVIITSNMFG DIISDEASVI PGSLGLLPSA SLASLPDTNS AFGLYEPCHG SAPDLPANKV
     NPVATILSVA MMLRLSLDCL KEAEALEKAV GQVLDAGIRT ADLRGSSSTK EVGDAVAAAV
     EKILAEGK