AC   MF_01033;
DC   Protein; auto
TR   HAMAP; MF_01033; -; 1; level=0
XX
Names: LeuB_type1
XX
ID   LEU3
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;
XX
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;
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC       Note=Binds 1 Mg(2+) or Mn(2+) ion per subunit.;
CC   -!- PATHWAY: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine
CC       from 3-methyl-2-oxobutanoate: step 3/4.
CC   -!- SUBUNIT: Homodimer.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the isocitrate and isopropylmalate
CC       dehydrogenases family. LeuB type 1 subfamily.
XX
DR   Pfam; PF00180; Iso_dh; 1; trigger=no
DR   NCBIfam; TIGR00169; LeuB; 1; trigger=no
DR   PROSITE; PS00470; IDH_IMDH; 1; trigger=no
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KW   Cytoplasm
KW   Amino-acid biosynthesis
KW   Branched-chain amino acid biosynthesis
KW   Leucine biosynthesis
KW   Magnesium
KW   Manganese
KW   Metal-binding
KW   NAD
KW   Oxidoreductase
XX
GO   GO:0003862; F:3-isopropylmalate dehydrogenase activity
GO   GO:0009098; P:leucine biosynthetic process
GO   GO:0005737; C:cytoplasm
XX
FT   From: LEU3_THET8 (Q5SIY4)
FT   BINDING         74..87
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT   Optional; Condition: G-[PYSAEKRT]-[KQHTAER]-x(0,3)-[WYV]-x(6,8)-P-E
FT   BINDING         274..286
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT   Optional; Condition: G-S-A-P-[DNT]-[IL]-x(4,5)-[AV]-N
FT   BINDING         217
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT   Group: 1; Condition: D
FT   BINDING         241
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT   Group: 1; Condition: D
FT   BINDING         245
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT   Group: 1; Condition: D
FT   BINDING         94
FT                   /ligand="substrate"
FT   Condition: R
FT   BINDING         104
FT                   /ligand="substrate"
FT   Condition: R
FT   BINDING         132
FT                   /ligand="substrate"
FT   Condition: R
FT   BINDING         217
FT                   /ligand="substrate"
FT   Condition: D
FT   SITE            139
FT                   /note="Important for catalysis"
FT   Condition: Y
FT   SITE            185
FT                   /note="Important for catalysis"
FT   Condition: K
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Size: 344-381;
Related: MF_01035;
Template: P30125; P37412; P61495; Q56268; Q5SIY4;
Scope:
 Bacteria
Fusion:
 Nter: None
 Cter: None
Duplicate: in BORBR, BRADU, DECAR
Plasmid: in BUCAI, BUCAP, BUCDN, BUCML, BUCRP, BUCTS, BUCUA, BUCUD, BUCUE,
 BUCUH, BUCUM, BUCUN, BUCUO, BUCUS
Comments: See MF_01035 for Actinomycetales leuB.
 Archaeal leuB are divergent and are not included in the alignment.
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# Revision 1.41 2023/06/01
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