ID   LEUC_ECOK1              Reviewed;         466 AA.
AC   A1A7C0;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   03-AUG-2022, entry version 99.
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=Ecok1_00660;
GN   ORFNames=APECO1_1911;
OS   Escherichia coli O1:K1 / APEC.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=405955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17293413; DOI=10.1128/jb.01726-06;
RA   Johnson T.J., Kariyawasam S., Wannemuehler Y., Mangiamele P., Johnson S.J.,
RA   Doetkott C., Skyberg J.A., Lynne A.M., Johnson J.R., Nolan L.K.;
RT   "The genome sequence of avian pathogenic Escherichia coli strain O1:K1:H7
RT   shares strong similarities with human extraintestinal pathogenic E. coli
RT   genomes.";
RL   J. Bacteriol. 189:3228-3236(2007).
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; CP000468; ABI99559.1; -; Genomic_DNA.
DR   RefSeq; WP_001140652.1; NC_008563.1.
DR   AlphaFoldDB; A1A7C0; -.
DR   SMR; A1A7C0; -.
DR   EnsemblBacteria; ABI99559; ABI99559; APECO1_1911.
DR   GeneID; 66671638; -.
DR   KEGG; ecv:APECO1_1911; -.
DR   HOGENOM; CLU_006714_3_4_6; -.
DR   OMA; CNMSIEM; -.
DR   UniPathway; UPA00048; UER00071.
DR   Proteomes; UP000008216; Chromosome.
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..466
FT                   /note="3-isopropylmalate dehydratase large subunit"
FT                   /id="PRO_1000063550"
FT   BINDING         347
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01026"
FT   BINDING         407
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01026"
FT   BINDING         410
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01026"
SQ   SEQUENCE   466 AA;  49882 MW;  2B225514207C5EFA CRC64;
     MAKTLYEKLF DAHVVYEAEN ETPLLYIDRH LVHEVTSPQA FDGLRAHGRP VRQPGKTFAT
     MDHNVSTQTK DINACGEMAR IQMQELIKNC KEFGVELYDL NHPYQGIVHV MGPEQGVTLP
     GMTIVCGDSH TATHGAFGAL AFGIGTSEVE HVLATQTLKQ GRAKTMKIEV QGKAAPGITA
     KDIVLAIIGK TGSAGGTGHV VEFCGEAIRD LSMEGRMTLC NMAIEMGAKA GLVAPDETTF
     NYVKGRLHAP KGKDFDDAVA YWKTLQTDEG ATFDTVVTLQ AEEISPQVTW GTNPGQVISV
     NDNIPDPASF ADPVERASAE KALAYMGLKP GIPLTEVAID KVFIGSCTNS RIEDLRAAAE
     IAKGRKVAPG VQALVVPGSG PVKAQAEAEG LDKIFIEAGF EWRLPGCSMC LAMNNDRLNP
     GERCASTSNR NFEGRQGRGG RTHLVSPAMA AAAAVTGHFA DIRNIK