ID   LEUC_RHINI              Reviewed;         750 AA.
AC   P55811;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 99.
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   Rhizopus niveus.
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC   Mucoromycetes; Mucorales; Mucorineae; Rhizopodaceae; Rhizopus.
OX   NCBI_TaxID=4844;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=NBRC 4810 / AS 3.4817;
RX   PubMed=8901103; DOI=10.1271/bbb.60.448;
RA   Takaya N., Yanai K., Horiuchi H., Ohta A., Takagi M.;
RT   "Cloning and characterization of the Rhizopus niveus leu1 gene and its use
RT   for homologous transformation.";
RL   Biosci. Biotechnol. Biochem. 60:448-452(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; D63833; BAA09893.1; -; Genomic_DNA.
DR   AlphaFoldDB; P55811; -.
DR   SMR; P55811; -.
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..750
FT                   /note="3-isopropylmalate dehydratase"
FT                   /id="PRO_0000076889"
FT   REGION          492..524
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        497..524
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   750 AA;  81309 MW;  7D7BE28304E26AB3 CRC64;
     MARTLYDKVL EDHIIDRQEY GTCLIYIDRH LVHEVTSPQA FEGLRNAGRP VRRPDCTLAT
     VDHNIPTSPR RNFKDIATFI KEGDSSTQCE TLGENIEAFG LTYFGMEDSR QGIVHVIGPE
     QGFTLPGTTV VCGDSHTSTH GAFGALAFGI GTSEVEHVLA TQTLLQKKSK NMRIRVEGKP
     SAGVTSKDIA LHVIGVIGTA GGTGCVIEFC GEANESLSME SRMSICNMSI EAGARAGMIA
     PDDITFEYLC NKPLASKGEE WDRAVAYWKT LKFDADAQYD ITVDIKASDI APTVTWGTSP
     QDVAPITGKT PDLDSIADPL RRLAVQRALD YIGIASNTPL EGVKIDKVFI GSCTNSRIED
     LGPAAAIVKG KRVADWVDAM VVPGSALVKR QAERKGLDKI FQEAGFNWRE AGCSMCLGMN
     PDQLKPGERC ASTSNRNFKG RQGAGGRTHL LSPAMAAAAG IKGCLTDVRH MEVAGIALTG
     NESPRQEVVA SKYDGSPEVF KSTQDTTPAV KPPQPASDSS SSGGMPAFTT LKGYAAPLDI
     SNIDTDMIIP KQFLKTIKRT GLGSALFYSL RFDPQTGAEN PAFVLKERTF RQARILVCTG
     PNFGCGSSRE HAPWAFNDFG IRCILAPSFA DIFFNNCFKN GMLPIVLPQA QLEAIAAEAQ
     KGVEVEVDLV QQIVRNPGGE VSFDVEEFRK HCLVNGLDDI GLTMQKADKI AQFETKRTQT
     WPWLDGKGYK GKATKIEING GQQKKAKLDW