ID   LEU3_BACCA              Reviewed;         366 AA.
AC   P05644;
DT   01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1988, sequence version 1.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=3-isopropylmalate dehydrogenase;
DE            EC=1.1.1.85;
DE   AltName: Full=3-IPM-DH;
DE   AltName: Full=Beta-IPM dehydrogenase;
DE            Short=IMDH;
GN   Name=leuB;
OS   Bacillus caldotenax.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus;
OC   Geobacillus thermoleovorans group.
OX   NCBI_TaxID=1395;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3547331; DOI=10.1093/nar/15.2.853;
RA   Sekiguchi T., Suda M., Ishii T., Nosoh Y., Tsuda K.;
RT   "The nucleotide sequence of 3-isopropylmalate dehydrogenase gene from
RT   Bacillus caldotenax.";
RL   Nucleic Acids Res. 15:853-853(1987).
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       (By similarity). {ECO:0000250}.
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 {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the isocitrate and isopropylmalate
CC       dehydrogenases family. LeuB type 1 subfamily. {ECO:0000305}.
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DR   EMBL; X04762; CAA28455.1; -; Genomic_DNA.
DR   PIR; A26447; A26447.
DR   AlphaFoldDB; P05644; -.
DR   SMR; P05644; -.
DR   UniPathway; UPA00048; UER00072.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003862; F:3-isopropylmalate dehydrogenase activity; IEA:UniProtKB-UniRule.
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-UniRule.
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   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..366
FT                   /note="3-isopropylmalate dehydrogenase"
FT                   /id="PRO_0000083633"
FT   BINDING         77..90
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         97
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         107
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         135
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         223
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         223
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         246
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         250
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         280..292
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   366 AA;  39636 MW;  530C88B3A60C630D CRC64;
     MGNYRIAVLP GDGIGKEVTS GAVEVLKAVG IRFGHEFTFE YGLIGGAAID EAGTPLPEET
     VRLCRESDAV LLGAVGGPKW DDNPPHLRPE KGLLAIRKQL DLYANLRPVV CYDSLVSRSP
     LKPDLVQGVD FVIVRELTGG IYFGQPSAVV ENGEEKAVDT LLYKKEEIER IVRMAFELAR
     GRRKKVTSVD KANVLSSSRL WREVAEEVAN EFPDVTLEHM LVDMRMQLIR APKQFDVIVT
     ENMFGDILSD EASMLSGSLG MLPSASLSAS GPSLYEPVHG SAPDIAGMNK ANPIAAILSA
     AMMLRLSFGL TAEAGGRARV WQALALGSGS RLGQRRPHLS TNEMVEEIKA AVLDYTAIAQ
     IMTVYA