ID   LEUC2_SALTY             Reviewed;         473 AA.
AC   Q8ZRJ0;
DT   02-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 119.
DE   RecName: Full=3-isopropylmalate dehydratase large subunit 2 {ECO:0000255|HAMAP-Rule:MF_01026};
DE            EC=4.2.1.33 {ECO:0000255|HAMAP-Rule:MF_01026};
DE   AltName: Full=Alpha-IPM isomerase 2 {ECO:0000255|HAMAP-Rule:MF_01026};
DE            Short=IPMI 2 {ECO:0000255|HAMAP-Rule:MF_01026};
DE   AltName: Full=Isopropylmalate isomerase 2 {ECO:0000255|HAMAP-Rule:MF_01026};
GN   Name=leuC2 {ECO:0000255|HAMAP-Rule:MF_01026}; OrderedLocusNames=STM0329;
OS   Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=99287;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX   PubMed=11677609; DOI=10.1038/35101614;
RA   McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA   Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA   Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA   Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA   Wilson R.K.;
RT   "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL   Nature 413:852-856(2001).
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; AE006468; AAL19283.1; -; Genomic_DNA.
DR   RefSeq; NP_459324.1; NC_003197.2.
DR   RefSeq; WP_001274854.1; NC_003197.2.
DR   AlphaFoldDB; Q8ZRJ0; -.
DR   SMR; Q8ZRJ0; -.
DR   STRING; 99287.STM0329; -.
DR   PaxDb; Q8ZRJ0; -.
DR   EnsemblBacteria; AAL19283; AAL19283; STM0329.
DR   GeneID; 1251848; -.
DR   KEGG; stm:STM0329; -.
DR   PATRIC; fig|99287.12.peg.349; -.
DR   HOGENOM; CLU_006714_3_4_6; -.
DR   OMA; GCGPCMG; -.
DR   PhylomeDB; Q8ZRJ0; -.
DR   BioCyc; SENT99287:STM0329-MON; -.
DR   UniPathway; UPA00048; UER00071.
DR   Proteomes; UP000001014; 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;
KW   Reference proteome.
FT   CHAIN           1..473
FT                   /note="3-isopropylmalate dehydratase large subunit 2"
FT                   /id="PRO_0000076804"
FT   BINDING         350
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"
FT   BINDING         413
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01026"
SQ   SEQUENCE   473 AA;  51446 MW;  66CAE0EEC6ECC6C8 CRC64;
     MSAKTLYEKL VESHTIRELD NEGHVLLYID RSILNEYTSP QAFSGLRERG RTVRHPDTFL
     LNIDHVNPTR SQRDDLMTDP GGQLQVDYFR ENAADFGITL FDVLDPRQGI EHVVAHEQGL
     VMPGMVIAAG DSHTTTYGAF GALGFGIGTS EIEHLLATQT LVYRKLKTMR VSVQGELPFA
     CSAKDIVLEL LERIGADGAT GYAIEFVGEA ISALSVEGRM TLCNMAVEAG ARGAIIAPDK
     KVFDYIYGKP QMPVGELWQQ ALLEWSQLSS DADAVFDKTV AINCHDLEPK VTWGISPDQT
     GSITGRVPFP EQETNPLKRL ALEKALHYMG LTAGMLLKDI RISHAFIGSC TNGRIEDLRA
     VAKVLEGRKI ASHVRGIIVP GSTMVRRQAE EEGLAKIFIA AGFEWRQSGC SMCLAMNEDV
     LSPGDRCASG TNRNFPGRQG AGARTHLMSP AMVAAAAVAG HLVDVRSLLQ AGE