ID   LEUC_BRUMB              Reviewed;         469 AA.
AC   C0RFF1;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 1.
DT   27-MAR-2024, entry version 76.
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};
GN   OrderedLocusNames=BMEA_A1961;
OS   Brucella melitensis biotype 2 (strain ATCC 23457).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX   NCBI_TaxID=546272;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 23457;
RA   Setubal J.C., Boyle S., Crasta O.R., Gillespie J.J., Kenyon R.W., Lu J.,
RA   Mane S., Nagrani S., Shallom J.M., Shallom S., Shukla M., Snyder E.E.,
RA   Sobral B.W., Wattam A.R., Will R., Williams K., Yoo H., Munk C., Tapia R.,
RA   Han C., Detter J.C., Bruce D., Brettin T.S.;
RT   "Brucella melitensis ATCC 23457 whole genome shotgun sequencing project.";
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
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; CP001488; ACO01623.1; -; Genomic_DNA.
DR   RefSeq; WP_004684442.1; NC_012441.1.
DR   AlphaFoldDB; C0RFF1; -.
DR   SMR; C0RFF1; -.
DR   GeneID; 29594568; -.
DR   KEGG; bmi:BMEA_A1961; -.
DR   HOGENOM; CLU_006714_3_4_5; -.
DR   UniPathway; UPA00048; UER00071.
DR   PRO; PR:C0RFF1; -.
DR   Proteomes; UP000001748; Chromosome I.
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; Aconitase, domain 3; 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   NCBIfam; TIGR00170; leuC; 1.
DR   PANTHER; PTHR43822:SF9; 3-ISOPROPYLMALATE DEHYDRATASE; 1.
DR   PANTHER; PTHR43822; HOMOACONITASE, MITOCHONDRIAL-RELATED; 1.
DR   Pfam; PF00330; Aconitase; 1.
DR   PRINTS; PR00415; ACONITASE.
DR   SUPFAM; SSF53732; Aconitase iron-sulfur domain; 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..469
FT                   /note="3-isopropylmalate dehydratase large subunit"
FT                   /id="PRO_1000149356"
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   469 AA;  50692 MW;  14442D949C40BCDF CRC64;
     MSAPRTLYDK IWDDHVVDQQ EDGTCLLYID RHLVHEVTSP QAFEGLHMAG RPVRHPEKTL
     AVVDHNVPTS PDRINGIQNE ESRIQVEALA RNAADFGVEY YSERDKRQGI VHIVGPEQGF
     TLPGMTIVCG DSHTSTHGAF GALAHGIGTS EVEHVLATQT LIQKKAKNML VRVDGKLPAG
     VTAKDIVLAI IGEIGTAGGT GYVIEYAGEA IRSLSMEGRM TICNMSIEGG ARAGLIAPDE
     TTFEYIKGRP RAPQGETLEQ AINYWKTLHS DEGAHFDKIV TLDAGSLPPI VSWGSSPEDV
     VSVTGVVPNP DDIADETKRA SKWRALDYMG LKPGTKITDI AVDRVFIGSC TNGRIEDLRA
     AAKVVEGKKV APTVNAMIVP GSGLVKEQAE AEGLHKIFIE AGFDWREPGC SMCLAMNDDR
     LKPGERCAST SNRNFEGRQG FKGRTHLVSP AMAAAAAIAG HFVDIRAWK
//