ID   LEU3B_ASPNG             Reviewed;         371 AA.
AC   P87257;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=3-isopropylmalate dehydrogenase B;
DE            Short=3-IPM-DH B;
DE            Short=IMDH B;
DE            EC=1.1.1.85;
DE   AltName: Full=Beta-IPM dehydrogenase B;
GN   Name=leu2B;
OS   Aspergillus niger.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=5061;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=A733;
RX   PubMed=8781173; DOI=10.1007/s002940050137;
RA   Williams B.A., Sillaots S., Tsang A., Storms R.;
RT   "Isolation by genetic complementation of two differentially expressed genes
RT   for beta-isopropylmalate dehydrogenase from Aspergillus niger.";
RL   Curr. Genet. 30:305-311(1996).
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; S83229; AAB50828.1; -; mRNA.
DR   EMBL; U51131; AAD10279.1; -; mRNA.
DR   PIR; S72210; S72210.
DR   AlphaFoldDB; P87257; -.
DR   SMR; P87257; -.
DR   STRING; 5061.CADANGAP00004627; -.
DR   PRIDE; P87257; -.
DR   VEuPathDB; FungiDB:An04g10130; -.
DR   VEuPathDB; FungiDB:ASPNIDRAFT2_1223020; -.
DR   VEuPathDB; FungiDB:ATCC64974_86770; -.
DR   VEuPathDB; FungiDB:M747DRAFT_326113; -.
DR   eggNOG; KOG0786; Eukaryota.
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   2: Evidence at transcript level;
KW   Amino-acid biosynthesis; Branched-chain amino acid biosynthesis; Cytoplasm;
KW   Leucine biosynthesis; Magnesium; Manganese; Metal-binding; NAD;
KW   Oxidoreductase.
FT   CHAIN           1..371
FT                   /note="3-isopropylmalate dehydrogenase B"
FT                   /id="PRO_0000083600"
FT   BINDING         79..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         142
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         229
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         229
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         254
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         258
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         296..308
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   SITE            149
FT                   /note="Important for catalysis"
FT                   /evidence="ECO:0000250"
FT   SITE            196
FT                   /note="Important for catalysis"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   371 AA;  40126 MW;  6A0978667BA6EA65 CRC64;
     MSGTRAYNIL VLPGDGIGPE VMAEAIKVLR TFNSSSMQFH LQEELIGGIS IDTHGHSVTQ
     PVKDAAVAAD AVLFAAVGGS KVDHIRRGLD GPEGGLLQVR KAMDIYANLR PCSVDVPSRE
     IARDFSPFRQ EVIEGVDFVV VRENCGGAYF GKKVEEENYA MDEWGYSTTE IQRIARLAAE
     LALRHDPPWP VISLDKANVL ASSRLWRRVV ENTISVEYPQ VKLVHQLADS ASLIMATDPR
     VLNGVILADN TFGDMLSDQA GSLIGTLGVL PSASLDGLPH PGKQEKVRGL YEPTHGSAPT
     IAGKNIANPT AMILCVSLMF RYSFNMENEA RQIEDAVRAV LDRGLRTPDL GGNSSTQEFG
     DAVVAALQGK Y