ID   LEU3_CANMA              Reviewed;         373 AA.
AC   P07139;
DT   01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1988, sequence version 1.
DT   03-AUG-2022, entry version 108.
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   Candida maltosa (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=5479;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2897248; DOI=10.1007/bf00384606;
RA   Takagi M., Kobayashi N., Sugimoto M., Fujii T., Watari J., Yano K.;
RT   "Nucleotide sequencing analysis of a LEU gene of Candida maltosa which
RT   complements leuB mutation of Escherichia coli and leu2 mutation of
RT   Saccharomyces cerevisiae.";
RL   Curr. Genet. 11:451-457(1987).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=G587;
RX   PubMed=7859302; DOI=10.1007/bf00309549;
RA   Becher D., Schulze S., Kasuske A., Schulze H., Samsonova I.A., Oliver S.G.;
RT   "Molecular analysis of a leu2-mutant of Candida maltosa demonstrates the
RT   presence of multiple alleles.";
RL   Curr. Genet. 26:208-216(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; X05459; CAA29024.1; -; Genomic_DNA.
DR   EMBL; X72940; CAA51445.1; -; Genomic_DNA.
DR   PIR; S48228; S48228.
DR   AlphaFoldDB; P07139; -.
DR   SMR; P07139; -.
DR   BRENDA; 1.1.1.85; 1125.
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..373
FT                   /note="3-isopropylmalate dehydrogenase"
FT                   /id="PRO_0000083604"
FT   BINDING         82..93
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         100
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         110
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         139
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         231
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         231
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         256
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         260
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         295..306
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   SITE            146
FT                   /note="Important for catalysis"
FT                   /evidence="ECO:0000250"
FT   SITE            198
FT                   /note="Important for catalysis"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   373 AA;  40173 MW;  256E9886219BA529 CRC64;
     MSVKTKTITI LPGDHVGTEI VNEAIKVLEA IEAATPYQKI HFDFKHHLIG GAAIDATGVP
     LPDDALESAK NSDAVLLGAV GGPKWGTGAL RPEQGLLKIR KELNLYANIR PCNFASDSLL
     ELSPLRPEVV KGTNLIIVRE LVGGIYFGDR EEQEESADKQ TAWDTEKYTV DEVTRITRMA
     AFMALQHTPP LPIWSLDKAN VLASSRLWRR TVDKVISEEF PTLSVQHQLI DSAAMILIQN
     PTKLNGIIIT SNMFGDIISD EASVIPGSLG LLPSASLASL PDTNTAFGLY EPCHGSAPDL
     PANKVNPIAT ILSAASMLRL SLDCVKEAEA LEEAVKQVLD KGIRTADLRG TSSTTEVGDA
     IVEAVTKILK EKA