AC   MF_01026;
DC   Protein; auto
TR   HAMAP; MF_01026; -; 1; level=0
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Names: LeuC_type1
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ID   LEUC
DE   RecName: Full=3-isopropylmalate dehydratase large subunit;
DE            EC=4.2.1.33;
DE   AltName: Full=Alpha-IPM isomerase;
DE            Short=IPMI;
DE   AltName: Full=Isopropylmalate isomerase;
GN   Name=leuC;
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CC   -!- FUNCTION: Catalyzes the isomerization between 2-isopropylmalate and 3-
CC       isopropylmalate, via the formation of 2-isopropylmaleate.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2R,3S)-3-isopropylmalate = (2S)-2-isopropylmalate;
CC         Xref=Rhea:RHEA:32287, ChEBI:CHEBI:1178, ChEBI:CHEBI:35121;
CC         EC=4.2.1.33;
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC       Note=Binds 1 [4Fe-4S] cluster per subunit.;
CC   -!- PATHWAY: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine
CC       from 3-methyl-2-oxobutanoate: step 2/4.
CC   -!- SUBUNIT: Heterodimer of LeuC and LeuD.
CC   -!- SIMILARITY: Belongs to the aconitase/IPM isomerase family. LeuC type 1
CC       subfamily.
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DR   Pfam; PF00330; Aconitase; 1; trigger=no
DR   PRINTS; PR00415; ACONITASE; 1; trigger=no
DR   NCBIfam; TIGR00170; LeuC; 1; trigger=no
DR   PROSITE; PS00450; ACONITASE_1; 1; trigger=no
DR   PROSITE; PS01244; ACONITASE_2; 1; trigger=no
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KW   Amino-acid biosynthesis
KW   Branched-chain amino acid biosynthesis
KW   Leucine biosynthesis
KW   Lyase
KW   Metal-binding
KW   Iron
KW   Iron-sulfur
KW   4Fe-4S
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GO   GO:0003861; F:3-isopropylmalate dehydratase activity
GO   GO:0009098; P:leucine biosynthetic process
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FT   From: LEUC_ECOLI (P0A6A6)
FT   BINDING         347
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT   Condition: C
FT   BINDING         407
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT   Condition: C
FT   BINDING         410
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT   Condition: C
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Size: 455-486;
Related: MF_01027;
Template: P0A6A6; P15717;
Scope:
 Bacteria
 Archaea; Halobacteria
Fusion:
 Nter: None
 Cter: None
Duplicate: in BRADU, MANSM, SALCH, SALTY
Plasmid: in BUCAI, BUCAI, BUCAP, BUCDN, BUCML, BUCRP, BUCTS, BUCUA, BUCUD,
 BUCUE, BUCUH, BUCUM, BUCUN, BUCUO, BUCUS
Comments: None
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# Revision 1.45 2023/06/01
//