ID   LEUC_METRJ              Reviewed;         470 AA.
AC   B1LXK9;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 83.
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=Mrad2831_0764;
OS   Methylobacterium radiotolerans (strain ATCC 27329 / DSM 1819 / JCM 2831 /
OS   NBRC 15690 / NCIMB 10815 / 0-1).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Methylobacteriaceae; Methylobacterium.
OX   NCBI_TaxID=426355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27329 / DSM 1819 / JCM 2831 / NBRC 15690 / NCIMB 10815 / 0-1;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Kiss H., Brettin T., Detter J.C., Han C.,
RA   Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Marx C.J., Richardson P.;
RT   "Complete sequence of chromosome of Methylobacterium radiotolerans JCM
RT   2831.";
RL   Submitted (MAR-2008) 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; CP001001; ACB22775.1; -; Genomic_DNA.
DR   RefSeq; WP_012317768.1; NC_010505.1.
DR   AlphaFoldDB; B1LXK9; -.
DR   SMR; B1LXK9; -.
DR   STRING; 426355.Mrad2831_0764; -.
DR   EnsemblBacteria; ACB22775; ACB22775; Mrad2831_0764.
DR   KEGG; mrd:Mrad2831_0764; -.
DR   eggNOG; COG0065; Bacteria.
DR   HOGENOM; CLU_006714_3_4_5; -.
DR   OMA; CNMSIEM; -.
DR   OrthoDB; 749418at2; -.
DR   UniPathway; UPA00048; UER00071.
DR   Proteomes; UP000006589; 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..470
FT                   /note="3-isopropylmalate dehydratase large subunit"
FT                   /id="PRO_1000135694"
FT   BINDING         349
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01026"
FT   BINDING         409
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01026"
FT   BINDING         412
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01026"
SQ   SEQUENCE   470 AA;  50749 MW;  227610AFF4D102CA CRC64;
     MTSPRTLYDK IWDDHVVDVQ PDGSSLLYID RHLVHEVTSP QAFEGLRVAG RKVRHPEKTL
     AVVDHNVQTS DRSQGIDDPE SRTQLEALAE NVRDFGIEFY DALDRRQGIV HIIGPEQGFT
     LPGQTIVCGD SHTSTHGAFG ALAHGIGTSE VEHVLATQTL VQRKARNMRV SVDGTLPPGV
     TAKDIILAII GEIGTAGGTG HVIEYAGEAI RALSMEGRMT ICNMSIEGGA RAGMVAPDAT
     TFAYVKDRPK APKGAAFDAA RRYWESLVTD AGAHFDREVR LDAANLPPIV SWGTSPEDVI
     SVQGRIPDPS EIADENKRQS KEKALAYMGL TPGTRITDIT LDRIFIGSCT NGRIEDLREV
     ARVVGDRKVH EGVSAMIVPG SGLVKAQAEA EGLDKILKAA GFDWREPGCS MCLGMNPDKL
     RPGERCASTS NRNFEGRQGP RGRTHLVSPA MAAAAAVAGR FVDIREWPQG