ID   LEU3_AZOVI              Reviewed;         360 AA.
AC   P96197;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   03-AUG-2022, entry version 101.
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   Azotobacter vinelandii.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Azotobacter.
OX   NCBI_TaxID=354;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 13705 / OP1 / DSM 366 / NCIMB 11614 / LMG 3878 / UW;
RX   PubMed=9108283; DOI=10.1007/s004380050409;
RA   Manna A.C., Das H.K.;
RT   "Characterization and mutagenesis of the leucine biosynthetic genes of
RT   Azotobacter vinelandii: an analysis of the rarity of amino acid
RT   auxotrophs.";
RL   Mol. Gen. Genet. 254:207-217(1997).
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. LeuB type 1 subfamily. {ECO:0000305}.
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DR   EMBL; Y11280; CAA72151.1; -; Genomic_DNA.
DR   AlphaFoldDB; P96197; -.
DR   SMR; P96197; -.
DR   BRENDA; 1.1.1.85; 49.
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; 2.
DR   Pfam; PF00180; Iso_dh; 2.
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..360
FT                   /note="3-isopropylmalate dehydrogenase"
FT                   /id="PRO_0000083631"
FT   REGION          66..101
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        66..80
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         133
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         247
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         251
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   SITE            140
FT                   /note="Important for catalysis"
FT                   /evidence="ECO:0000250"
FT   SITE            191
FT                   /note="Important for catalysis"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   360 AA;  38974 MW;  16AAEC7966EDAC6A CRC64;
     MSKQILVLPG DGIGPEIMAE AVKVLQLANE KYQLGFVLGY DELGGAAVDK YGVPLADETL
     ERARRRCHPA RRRRRSEMGR HRPGHPPGAR PAENPFATGP VRQPAPGVLY PQLAEASTLR
     PEVVAGLDIL IVRELTGGIY FGAPRESRLL ANGERMAYDT LPYSESEIRR IAKVGFDMAR
     VRGKKLCSVD KANVLASSQL WRAVVEEVAK DYPDVVLSHM YVDNAAMQLV RAPKQFDVIV
     TDNMFGDILS DEASMLTGSI GMLPSASLDA DNKGMYEPCH GSRRPDIAGK GIANPLATIL
     SVSMMLRYSF GQVEAANAIE QAVSKVLDQG LRTGDIWSEG CRKVGTAEMG DAVVAALATL