ID   LEUC_RHIPU              Reviewed;         755 AA.
AC   P55251;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 98.
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   Rhizomucor pusillus.
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC   Mucoromycetes; Mucorales; Lichtheimiaceae; Rhizomucor.
OX   NCBI_TaxID=4840;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8766701; DOI=10.1007/s002530050743;
RA   Wada M., Beppu T., Horinouchi S.;
RT   "Integrative transformation of the zygomycete Rhizomucor pusillus by
RT   homologous recombination.";
RL   Appl. Microbiol. Biotechnol. 45:652-657(1996).
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; D67033; BAA11052.1; -; Genomic_DNA.
DR   AlphaFoldDB; P55251; -.
DR   SMR; P55251; -.
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..755
FT                   /note="3-isopropylmalate dehydratase"
FT                   /id="PRO_0000076890"
FT   REGION          427..446
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          471..493
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          510..529
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        427..441
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         353
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         413
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         416
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   755 AA;  82486 MW;  4E40537136BA6D11 CRC64;
     MGRTLYDKVW DDHVVDQQED GTCLIYIDRH LVHEVTSPQA FEGLRNAGRK VRRPDCTLAT
     VDHNIPTTPR KNFKNVSTFI QEADSRTQCE TLEHNVKEFG LTYFGMDDSR QGIVHVIGPE
     QGFTLPGCTV NCGDSHTSTH GAFGALAFGI GTSEVEHVLA TQTLLQKKSK NMRVKVDGKL
     APGVTSKDIV LHIIGVIGTA GGTGCVIEFC GSAFEQMSME ARMSVCNMSI EAGARAGMIA
     PDETTFEYIR GRPLAPTGAE WDKAVEYWRS LRSDPDAKYD VDVFIDAADI APTLTWGTSP
     QDVVAITGTT PDPSTVSDPI RRQAMERALD YIGLKPNTPM QEVKIDKVFI GSCTNSRIED
     LRAAAAIAKG RHVADWVYAM VVPGSGLVKK QAEQEGLDRI FKEAGFDWRE AGCSMCLGMN
     PDQLKPGERC ASTSNRNFEG RQGAGGRTHL MSPAMAAAAA VTGYFTDVRK LTPAQQDRPA
     SPTPKKIETE LEPPVEDHAK AADQADIVTD APATGASPPS PAPSDAAGMP KFTTLRGYAA
     PLDIANVDTD MIIPKQFLKT IKRTGLGTAL FYNIRFDGAT GEENPDFVLN QEPYRQSRIL
     VCTGPNFGCG SSREHAPWAF NDFGIRSIIA PSFADIFFNN CFKNGMLPIT LPQDKVEMLA
     EHAKQKAELE VDLVNQVVRY PGGEVPFDVE PFRKHCLVNG LDDIGLTMQK ADLIEAFEAK
     RSQTWPWLDG KDYAGKATKF TPVATNTAKK QKLDW