ID   LEUC_ACTTI              Reviewed;         485 AA.
AC   Q44427;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 104.
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};
OS   Actinoplanes teichomyceticus.
OC   Bacteria; Actinobacteria; Micromonosporales; Micromonosporaceae;
OC   Actinoplanes.
OX   NCBI_TaxID=1867;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 31121 / DSM 43866 / BCRC 12106 / JCM 3252 / KCTC 9543 / NBRC
RC   13999 / NCIMB 12640 / NRRL B-16726 /AB 8327;
RX   PubMed=7789819; DOI=10.1016/0378-1119(95)00142-s;
RA   Castelli P., Donadio S., Marinelli F., Borghi A., Sosio M.;
RT   "Complementation of a Streptomyces lividans Leu- mutant by the Actinoplanes
RT   teichomyceticus leuC gene.";
RL   Gene 158:97-100(1995).
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.
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; X84647; CAA59140.1; -; Genomic_DNA.
DR   PIR; I39699; I39699.
DR   AlphaFoldDB; Q44427; -.
DR   SMR; Q44427; -.
DR   UniPathway; UPA00048; UER00071.
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.
FT   CHAIN           1..485
FT                   /note="3-isopropylmalate dehydratase large subunit"
FT                   /id="PRO_0000076688"
FT   REGION          439..462
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        439..455
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         367
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01026"
FT   BINDING         427
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01026"
FT   BINDING         430
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01026"
SQ   SEQUENCE   485 AA;  51783 MW;  EA8EF4FBAAF5BA15 CRC64;
     MVGVTPQSGK PRTLAEKVWD DHVVRTAAEG EPDLLFIDLH LLHEVTSPQA FDGLRMAGRR
     VRRTDLTLAT EDHNTPTGYA DPSFNTRRGE LLTIADTVSR TQIETLRKNC AEFGVEIRPL
     GDVNQGIVHV IGPQLGLTQP GMTIVCGDSH TATHGASGAL AFGIGTSEVE HVLATQTLPQ
     SKPKTMAVTV VGELRPGVSA KDLILTLITQ TGTGGGNGHI VEYRGEAIRK LSMEGRMTIC
     NMSIEWGAKA GMIAPDETTF DYLSGRKHAR RGADWDAAVA YWKTLATDEG AEYDTEIILD
     ASKISPFITW GTNPGQGAAL DGVVPDPQDF LDEVERGAAE RALAYMGLTP GTPFRDVPVD
     VVFVGSCTNG RLEDLRAAAD VIRGRKVADG VRMMIVPGSY QVREQAEAEG LDKIFIDAGA
     EWRFAGCSMC LGMNPDTLSP GQRAASTSNR NFEGRQGKGG RTHLVSPQVA AATAVVGKLA
     APADL