ID   LEUC_CUPNE              Reviewed;         267 AA.
AC   Q44023;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 96.
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;
DE   Flags: Fragment;
GN   Name=leuC;
OS   Cupriavidus necator (Alcaligenes eutrophus) (Ralstonia eutropha).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=106590;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=H16 / SK4040;
RX   PubMed=7851418; DOI=10.1111/j.1432-1033.1995.tb20358.x;
RA   Valentin H.E., Zwingmann G., Schoenebaum A., Steinbuechel A.;
RT   "Metabolic pathway for biosynthesis of poly(3-hydroxybutyrate-co-4-
RT   hydroxybutyrate) from 4-hydroxybutyrate by Alcaligenes eutrophus.";
RL   Eur. J. Biochem. 227:43-60(1995).
CC   -!- FUNCTION: Catalyzes the isomerization between 2-isopropylmalate and 3-
CC       isopropylmalate, via the formation of 2-isopropylmaleate.
CC       {ECO:0000250}.
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; Evidence={ECO:0000250};
CC       Note=Binds 1 [4Fe-4S] cluster per subunit. {ECO:0000250};
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. {ECO:0000305}.
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DR   EMBL; L36817; AAC41429.1; -; Genomic_DNA.
DR   PIR; I39573; I39573.
DR   AlphaFoldDB; Q44023; -.
DR   SMR; Q44023; -.
DR   UniPathway; UPA00048; UER00071.
DR   GO; GO:0003861; F:3-isopropylmalate dehydratase activity; IEA:UniProtKB-EC.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0009098; P:leucine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.30.499.10; -; 2.
DR   InterPro; IPR015931; Acnase/IPM_dHydase_lsu_aba_1/3.
DR   InterPro; IPR001030; Acoase/IPM_deHydtase_lsu_aba.
DR   InterPro; IPR018136; Aconitase_4Fe-4S_BS.
DR   InterPro; IPR036008; Aconitase_4Fe-4S_dom.
DR   Pfam; PF00330; Aconitase; 1.
DR   PRINTS; PR00415; ACONITASE.
DR   SUPFAM; SSF53732; SSF53732; 1.
DR   PROSITE; PS00450; ACONITASE_1; 1.
PE   3: Inferred from homology;
KW   4Fe-4S; Amino-acid biosynthesis; Branched-chain amino acid biosynthesis;
KW   Iron; Iron-sulfur; Leucine biosynthesis; Lyase; Metal-binding.
FT   CHAIN           <1..267
FT                   /note="3-isopropylmalate dehydratase large subunit"
FT                   /id="PRO_0000076791"
FT   BINDING         146
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         206
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         209
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   NON_TER         1
SQ   SEQUENCE   267 AA;  28516 MW;  B24338F5077A4096 CRC64;
     EFGGSAVRSL PVEARLTLCN LAVEFSAFSG IVAPDDTVFE YLAGRPYAPA GAQWEPALWH
     WRSLYSDADA VFDRELSVDC RQLAPMVTWG TSPQHGVAVD GAVPNPAMAI DADTRQAMER
     ALSYMDLRPG QRMADIAIDA AFIGSCTNSR LSDLRSAAGV LAGRKVAPGV TAICVPVSSA
     VKRAAEAEGL DRVFREAGFE WRESGCSMCF YAGGESFGHR QRVISSTNRN FESRQGPQTR
     THLAGPATVA ASAVLGRIAD PRRPPGA