ID   LEUC_CANMA              Reviewed;         770 AA.
AC   Q00464;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 91.
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=LEU1;
OS   Candida maltosa (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=5479;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=L4;
RA   Becher D., Jomantiene R., Schulze S., Bode R., Oliver S.G.;
RT   "Genetic and sequence analyses demonstrate bifunctional nature of LEU1 gene
RT   in Candida maltosa.";
RL   Submitted (JUL-1996) 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   -!- 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. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the aconitase/IPM isomerase family.
CC       {ECO:0000305}.
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DR   EMBL; U60167; AAB03335.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q00464; -.
DR   SMR; Q00464; -.
DR   UniPathway; UPA00048; UER00071.
DR   GO; GO:0009316; C:3-isopropylmalate dehydratase complex; IEA:InterPro.
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   CDD; cd01577; IPMI_Swivel; 1.
DR   Gene3D; 3.20.19.10; -; 1.
DR   Gene3D; 3.30.499.10; -; 2.
DR   HAMAP; MF_01026; LeuC_type1; 1.
DR   HAMAP; MF_01031; LeuD_type1; 1.
DR   InterPro; IPR004430; 3-IsopropMal_deHydase_lsu.
DR   InterPro; IPR004431; 3-IsopropMal_deHydase_ssu.
DR   InterPro; IPR012235; 3-IsopropMal_deHydtase_ssu/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   InterPro; IPR033940; IPMI_Swivel.
DR   Pfam; PF00330; Aconitase; 1.
DR   Pfam; PF00694; Aconitase_C; 1.
DR   PIRSF; PIRSF001418; ACN; 1.
DR   PRINTS; PR00415; ACONITASE.
DR   SUPFAM; SSF53732; SSF53732; 1.
DR   TIGRFAMs; TIGR00170; leuC; 1.
DR   TIGRFAMs; TIGR00171; leuD; 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..770
FT                   /note="3-isopropylmalate dehydratase"
FT                   /id="PRO_0000076887"
FT   BINDING         354
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         415
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         418
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   770 AA;  85317 MW;  CB1C26A56D7C3C1A CRC64;
     MSPKTLYDKV FEDHIVYEDE SGSNLLYIDR HLVHEVTSPQ AFEGLKNAGR TVRRTDCTLA
     TVDHNIPTIS RVNFKTLLTF IDQDDSRLQV QTLEQNVKDF DVTYFGMTDD RQGIVHVVGP
     EQGFTLPGTT VVCGDSHTST HGAFGALAFG IGTSEVEHVL ATQTTIQANP KNMRITIDGE
     LSEGITSKDL VLHVIGVIGT AGGTGCVIEF AGKAIEDLSM EARMSICNMA IEAGARAGMI
     KPDEKTFEYI KGRPLAPKGD EWEKALKYWK TLHTDDGAKL HYDIKIAASD IVPTITWGNS
     PQDALPITAS VPDPANVSDP IKKSGMERAL KYQGLTPNTP FVVIKMHKAF IGSCTNSRIE
     DLRAAAKVAK GHKKADNVKL VLVVPGSGLI KKQAEKEGLD KIFESAGFTW REAGCSMCLG
     MNPDILDPEE RCASTSNRNF EGRQGARSRT HLMSPAMAAA AAIKGHFTDI REFDYVDNDE
     PSITIEHEVE DKELQDAVYE HEKEIIEGTP GTEAERSTTS LKMNQNSKKP NQMLIKMVPI
     TVLPFLTGIT APLYKANVDT DAIIPKQFLK TIKRTGLKNG LFYESRFVKM PMVRCQTDFV
     LNVEPYRQAE ILLVTGDNFG CGSSREHAPW ALKDFGIKSI IAPSFGDIFY NNSFKNFLLP
     IRIPQDVIES KLVPVVKAGH KLTIDLPNQQ IKDGETGDVL IEKFDVEEFR KHCLVNGLDD
     IGLTLQKEEY IQEYEAKRRE KFSFLEGGSK LIKPIKGTKK SIYGNKAQEW