ID   LEUC_CAMC5              Reviewed;         421 AA.
AC   A7H0L8;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   03-AUG-2022, entry version 88.
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};
GN   OrderedLocusNames=Ccur92_17060; ORFNames=CCV52592_0608;
OS   Campylobacter curvus (strain 525.92).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=360105;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=525.92;
RA   Fouts D.E., Mongodin E.F., Puiu D., Sebastian Y., Miller W.G.,
RA   Mandrell R.E., Lastovica A.J., Nelson K.E.;
RT   "Genome sequence of Campylobacter curvus 525.92 isolated from human
RT   feces.";
RL   Submitted (JUL-2007) 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       {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; CP000767; EAU01448.1; -; Genomic_DNA.
DR   RefSeq; WP_011992759.1; NC_009715.2.
DR   AlphaFoldDB; A7H0L8; -.
DR   SMR; A7H0L8; -.
DR   STRING; 360105.CCV52592_0608; -.
DR   EnsemblBacteria; EAU01448; EAU01448; CCV52592_0608.
DR   KEGG; ccv:CCV52592_0608; -.
DR   HOGENOM; CLU_006714_3_4_7; -.
DR   OMA; GIEHCLL; -.
DR   OrthoDB; 749418at2; -.
DR   UniPathway; UPA00048; UER00071.
DR   Proteomes; UP000006380; 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   InterPro; IPR011823; IsopropMal_deHydtase_lsu_bac.
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   TIGRFAMs; TIGR02083; LEU2; 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;
KW   Reference proteome.
FT   CHAIN           1..421
FT                   /note="3-isopropylmalate dehydratase large subunit"
FT                   /id="PRO_1000063640"
FT   BINDING         302
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01027"
FT   BINDING         362
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01027"
FT   BINDING         365
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01027"
SQ   SEQUENCE   421 AA;  45650 MW;  EAD98A25976BB02E CRC64;
     MHQTITEKIF SDHVGREVFA NEIIESGIDM VIGNDITTPI SIKQFERSGA TKLANPEGFC
     IVMDHYIPAK DILSANQAKI SRDFAYKHDL KYFFDEKDMG IEHALLPEKG LIVPGDVIIG
     ADSHTCTHGA LGAFSTGMGS TDLAYAMITG KNWFKVPPTI KVVFRGKLGR HVYGKDLILE
     IIRQIGVDGA RYKALEFCGE TIDALDMDGR FSMCNMAIEA GGKSGIIAVD ETTREFLKGK
     NLRAEPKFFY SDEGAGYERV LEIYADKLDP VIAYPFLPSN GKSVREAVKD DIAIDQAFIG
     SCTNGRLSDL RIAAEILKGR KVSRKTRLII TPATQKIALA AQKEGLMDIF VEAGAVVSNP
     TCGACLGGYM GILGAGERCV STTNRNFVGR MGDRTSEVYL ANSAVAAASA IAGKIADPRE
     L