ID   LEUC_MUCCL              Reviewed;         644 AA.
AC   P17279;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1990, sequence version 1.
DT   03-AUG-2022, entry version 109.
DE   RecName: Full=3-isopropylmalate dehydratase;
DE            EC=4.2.1.33;
DE   AltName: Full=Alpha-IPM isomerase;
DE            Short=IPMI;
DE   AltName: Full=Isopropylmalate isomerase;
GN   Name=LEUA;
OS   Mucor circinelloides f. lusitanicus (Mucor racemosus var. lusitanicus).
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC   Mucoromycetes; Mucorales; Mucorineae; Mucoraceae; Mucor.
OX   NCBI_TaxID=29924;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 1216b / BCRC 32522 / CBS 277.49 / NRRL 3631;
RX   PubMed=2693214; DOI=10.1016/0378-1119(89)90508-8;
RA   Isabel M., Roncero G., Jepsen L.P., Stroeman P., van Heeswijck R.;
RT   "Characterization of a leuA gene and an ARS element from Mucor
RT   circinelloides.";
RL   Gene 84:335-343(1989).
CC   -!- FUNCTION: Catalyzes the isomerization between 2-isopropylmalate and 3-
CC       isopropylmalate, via the formation of 2-isopropylmaleate.
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;
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250};
CC       Note=Binds 1 [4Fe-4S] cluster per subunit. {ECO:0000250};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine
CC       from 3-methyl-2-oxobutanoate: step 2/4.
CC   -!- SUBUNIT: Monomer.
CC   -!- SIMILARITY: Belongs to the aconitase/IPM isomerase family.
CC       {ECO:0000305}.
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DR   EMBL; M33166; AAA33422.1; -; Genomic_DNA.
DR   PIR; JQ0160; JQ0160.
DR   AlphaFoldDB; P17279; -.
DR   SMR; P17279; -.
DR   PRIDE; P17279; -.
DR   UniPathway; UPA00048; UER00071.
DR   GO; GO:0003861; F:3-isopropylmalate dehydratase activity; IEA:UniProtKB-EC.
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-UniPathway.
DR   CDD; cd01583; IPMI; 1.
DR   Gene3D; 3.20.19.10; -; 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; IPR015928; Aconitase/3IPM_dehydase_swvl.
DR   InterPro; IPR018136; Aconitase_4Fe-4S_BS.
DR   InterPro; IPR036008; Aconitase_4Fe-4S_dom.
DR   InterPro; IPR000573; AconitaseA/IPMdHydase_ssu_swvl.
DR   InterPro; IPR033941; IPMI_cat.
DR   Pfam; PF00330; Aconitase; 1.
DR   Pfam; PF00694; Aconitase_C; 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..644
FT                   /note="3-isopropylmalate dehydratase"
FT                   /id="PRO_0000076891"
FT   REGION          521..568
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        551..568
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         400
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         460
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         463
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   644 AA;  69939 MW;  087FC2C518BD497E CRC64;
     MISSISLSQD KCKYLLYNNL LVDERENFLV SLTCSYILFQ KTIPYIQNVS TLYDKVWDDH
     VIDQQEDGTC LIYIDRHLVH EVTSPQAFEG LRNANRPVRR PDCTLATVDH NIPTTTRKIF
     KNITTFIKEA DSRTQCETLE QNIEAFGLTY FGMEDSRQGI VHVIGPEQGF TLPATTVVCG
     DSHTSTHGAF GALAFGIGTS EVEHVLATQT LLQKKSKNMR IRVQGKALPG VTSKDIVLHI
     IGVIGTAGGT GCVIEFCGDT IAALSMESRM SICNMSIEAG ARAGMVAPDE VTFEYLRDKP
     LAPKGADWDR AVKYWKSLSS DADAKYDINV EINAADIAPT LTWGTSPQDV VPITGSTPDP
     AKIEDPIRRS AVQRALDYIG IAPNTPMEGV KVDKVFIGSC TNSRIEDLRA AAAVVKGKRA
     AEWVDAMVVP GSGLVKRQAE REGLDKIFTD AGFDWREAGC SMCLGMNPDQ LKPGERCAST
     SNRNFEGRQG AGGRTHLVSP AMAAAAGIKG CLTDVRNMEV SEIPGTPKQS PRQEVVAEFE
     SEEDDVDSSS VDSAPVATPP STGDSAGMPK FTTLKGYAAP LDISNVDTDM IIPKQFLKTI
     KRTGLGSALF YALRFDPATG AENPDFVLNL RALPSRTYLG LHRS