ID   LEUC_PICTO              Reviewed;         413 AA.
AC   Q6L0K5;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 109.
DE   RecName: Full=3-isopropylmalate dehydratase large subunit {ECO:0000255|HAMAP-Rule:MF_01027};
DE            EC=4.2.1.33 {ECO:0000255|HAMAP-Rule:MF_01027};
DE   AltName: Full=Alpha-IPM isomerase {ECO:0000255|HAMAP-Rule:MF_01027};
DE            Short=IPMI {ECO:0000255|HAMAP-Rule:MF_01027};
DE   AltName: Full=Isopropylmalate isomerase {ECO:0000255|HAMAP-Rule:MF_01027};
GN   Name=leuC {ECO:0000255|HAMAP-Rule:MF_01027}; OrderedLocusNames=PTO0912;
OS   Picrophilus torridus (strain ATCC 700027 / DSM 9790 / JCM 10055 / NBRC
OS   100828).
OC   Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC   Picrophilaceae; Picrophilus.
OX   NCBI_TaxID=263820;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828;
RX   PubMed=15184674; DOI=10.1073/pnas.0401356101;
RA   Fuetterer O., Angelov A., Liesegang H., Gottschalk G., Schleper C.,
RA   Schepers B., Dock C., Antranikian G., Liebl W.;
RT   "Genome sequence of Picrophilus torridus and its implications for life
RT   around pH 0.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:9091-9096(2004).
CC   -!- FUNCTION: Catalyzes the isomerization between 2-isopropylmalate and 3-
CC       isopropylmalate, via the formation of 2-isopropylmaleate.
CC       {ECO:0000255|HAMAP-Rule:MF_01027}.
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_01027};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01027};
CC       Note=Binds 1 [4Fe-4S] cluster per subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_01027};
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_01027}.
CC   -!- SUBUNIT: Heterodimer of LeuC and LeuD. {ECO:0000255|HAMAP-
CC       Rule:MF_01027}.
CC   -!- SIMILARITY: Belongs to the aconitase/IPM isomerase family. LeuC type 2
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_01027}.
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DR   EMBL; AE017261; AAT43497.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q6L0K5; -.
DR   SMR; Q6L0K5; -.
DR   STRING; 263820.PTO0912; -.
DR   EnsemblBacteria; AAT43497; AAT43497; PTO0912.
DR   KEGG; pto:PTO0912; -.
DR   PATRIC; fig|263820.9.peg.950; -.
DR   eggNOG; arCOG01698; Archaea.
DR   HOGENOM; CLU_006714_3_4_2; -.
DR   OMA; GIEHCLL; -.
DR   UniPathway; UPA00048; UER00071.
DR   Proteomes; UP000000438; Chromosome.
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_01027; LeuC_type2; 1.
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; IPR011826; HAcnase/IPMdehydase_lsu_prok.
DR   InterPro; IPR006251; Homoacnase/IPMdehydase_lsu.
DR   InterPro; IPR033941; IPMI_cat.
DR   Pfam; PF00330; Aconitase; 1.
DR   PRINTS; PR00415; ACONITASE.
DR   SUPFAM; SSF53732; SSF53732; 1.
DR   TIGRFAMs; TIGR01343; hacA_fam; 1.
DR   TIGRFAMs; TIGR02086; IPMI_arch; 1.
DR   PROSITE; PS00450; ACONITASE_1; 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;
KW   Reference proteome.
FT   CHAIN           1..413
FT                   /note="3-isopropylmalate dehydratase large subunit"
FT                   /id="PRO_0000076876"
FT   BINDING         293
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01027"
FT   BINDING         353
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01027"
FT   BINDING         356
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01027"
SQ   SEQUENCE   413 AA;  45059 MW;  3AEED78CE4E94D16 CRC64;
     MKTAVEKIFS DKSGNDARAG DYVIANLDYV MVNDITGPIA IDAFNELGYK PLSDRIVVIP
     DHFVPPKDIN SAIQYKKVKD FALKHNTHFY DLGRGGVCHQ VMMEKGFAAP GRLIAGADSH
     TNTYGALSCV SVGIGSTEAG VIFGTGRMWF KVPETDLIRI NGRPKKGVYG KDIILNVLSR
     IGNGGSAYKC MEFTGSTIDY LDINERMTMA NMTTEAGAKC SFFNADEKTL DYIRNKTNDY
     KIYKDDENAE YSRIIDIDAS EIEPSVAIPN SPDNVRPVSK VSERIDQAYI GSCTNGRIED
     IRRAALILKD KKIDKNVRLM VVPASQEVYN QALKEGLVDI ITDAGGYFAG TTCGACLGGY
     MGVLGPGETC ISTTNRNFIG RMGDRTSRVY LANPEVVAAS AIMGRIASPE EIQ