ID   LEUC_LISMH              Reviewed;         462 AA.
AC   B8DBU2;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 70.
DE   RecName: Full=3-isopropylmalate dehydratase large subunit {ECO:0000255|HAMAP-Rule:MF_01026};
DE            EC=4.2.1.33 {ECO:0000255|HAMAP-Rule:MF_01026};
DE   AltName: Full=Alpha-IPM isomerase {ECO:0000255|HAMAP-Rule:MF_01026};
DE            Short=IPMI {ECO:0000255|HAMAP-Rule:MF_01026};
DE   AltName: Full=Isopropylmalate isomerase {ECO:0000255|HAMAP-Rule:MF_01026};
GN   Name=leuC {ECO:0000255|HAMAP-Rule:MF_01026}; OrderedLocusNames=LMHCC_0571;
OS   Listeria monocytogenes serotype 4a (strain HCC23).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=552536;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HCC23;
RX   PubMed=21602330; DOI=10.1128/jb.05236-11;
RA   Steele C.L., Donaldson J.R., Paul D., Banes M.M., Arick T., Bridges S.M.,
RA   Lawrence M.L.;
RT   "Genome sequence of lineage III Listeria monocytogenes strain HCC23.";
RL   J. Bacteriol. 193:3679-3680(2011).
CC   -!- FUNCTION: Catalyzes the isomerization between 2-isopropylmalate and 3-
CC       isopropylmalate, via the formation of 2-isopropylmaleate.
CC       {ECO:0000255|HAMAP-Rule:MF_01026}.
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; Evidence={ECO:0000255|HAMAP-Rule:MF_01026};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01026};
CC       Note=Binds 1 [4Fe-4S] cluster per subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_01026};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine
CC       from 3-methyl-2-oxobutanoate: step 2/4. {ECO:0000255|HAMAP-
CC       Rule:MF_01026}.
CC   -!- SUBUNIT: Heterodimer of LeuC and LeuD. {ECO:0000255|HAMAP-
CC       Rule:MF_01026}.
CC   -!- SIMILARITY: Belongs to the aconitase/IPM isomerase family. LeuC type 1
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_01026}.
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DR   EMBL; CP001175; ACK38928.1; -; Genomic_DNA.
DR   RefSeq; WP_012581033.1; NC_011660.1.
DR   AlphaFoldDB; B8DBU2; -.
DR   SMR; B8DBU2; -.
DR   KEGG; lmh:LMHCC_0571; -.
DR   HOGENOM; CLU_006714_3_4_9; -.
DR   OMA; CNMSIEM; -.
DR   UniPathway; UPA00048; UER00071.
DR   GO; GO:0003861; F:3-isopropylmalate dehydratase activity; IEA:UniProtKB-UniRule.
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-UniRule.
DR   CDD; cd01583; IPMI; 1.
DR   Gene3D; 3.30.499.10; -; 2.
DR   HAMAP; MF_01026; LeuC_type1; 1.
DR   InterPro; IPR004430; 3-IsopropMal_deHydase_lsu.
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   InterPro; IPR033941; IPMI_cat.
DR   Pfam; PF00330; Aconitase; 1.
DR   PRINTS; PR00415; ACONITASE.
DR   SUPFAM; SSF53732; SSF53732; 1.
DR   TIGRFAMs; TIGR00170; leuC; 1.
DR   PROSITE; PS00450; ACONITASE_1; 1.
DR   PROSITE; PS01244; ACONITASE_2; 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..462
FT                   /note="3-isopropylmalate dehydratase large subunit"
FT                   /id="PRO_1000149367"
FT   BINDING         337
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01026"
FT   BINDING         397
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01026"
FT   BINDING         400
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01026"
SQ   SEQUENCE   462 AA;  51054 MW;  E1C46CE6D74B32E8 CRC64;
     MGKTLFDKLW NRHVIYGKEG EPQLLYVDLH LIHEVTSPQA FEGLRMENRP LRRPDKTFAT
     MDHNVPTEDI FNIQDLVAKK QIEALQTNCE EFGVTLADMG SDRQGIVHMV GPETGLTQPG
     KVIVCGDSHT ATHGAFGAIG FGIGSSEVEH VFATQTIWQQ KPKSMGIEIN GKLPKGVYAK
     DIILHLIATY GVAFGTGYAV EYYGETIRNM SMEERMTICN MAIEGGAKMG MMAPDETTFE
     YVRGREYAPA DMEKAIRDWK TLQTDPDAEY DLHIEMDASI LEPYVTWGTN PEMGVPFSKA
     FPEIKDMNYE RAYEYMGLKP GQTAEEIELG YVFIGSCTNA RLSDLEEAAR IVKGNKVKNN
     IRALVVPGSR QVRNAAESIG LDKIFIEAGF EWREPGCSMC LGMNPDQVPD GVHCASTSNR
     NFEGRQGKGA RTHLVSPAMA AAAAINGHFI DIRKEAIISG GN