ID   LEUC_NAUPA              Reviewed;         425 AA.
AC   B9L6Y8;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 95.
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=NAMH_1751;
OS   Nautilia profundicola (strain ATCC BAA-1463 / DSM 18972 / AmH).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Nautiliales; Nautiliaceae;
OC   Nautilia.
OX   NCBI_TaxID=598659;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1463 / DSM 18972 / AmH;
RX   PubMed=19197347; DOI=10.1371/journal.pgen.1000362;
RA   Campbell B.J., Smith J.L., Hanson T.E., Klotz M.G., Stein L.Y., Lee C.K.,
RA   Wu D., Robinson J.M., Khouri H.M., Eisen J.A., Cary S.C.;
RT   "Adaptations to submarine hydrothermal environments exemplified by the
RT   genome of Nautilia profundicola.";
RL   PLoS Genet. 5:E1000362-E1000362(2009).
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; CP001279; ACM92883.1; -; Genomic_DNA.
DR   RefSeq; WP_015901935.1; NC_012115.1.
DR   AlphaFoldDB; B9L6Y8; -.
DR   SMR; B9L6Y8; -.
DR   STRING; 598659.NAMH_1751; -.
DR   EnsemblBacteria; ACM92883; ACM92883; NAMH_1751.
DR   KEGG; nam:NAMH_1751; -.
DR   eggNOG; COG0065; Bacteria.
DR   HOGENOM; CLU_006714_3_4_7; -.
DR   OMA; GIEHCLL; -.
DR   OrthoDB; 749418at2; -.
DR   UniPathway; UPA00048; UER00071.
DR   Proteomes; UP000000448; 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..425
FT                   /note="3-isopropylmalate dehydratase large subunit"
FT                   /id="PRO_1000149380"
FT   BINDING         306
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01027"
FT   BINDING         366
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01027"
FT   BINDING         369
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01027"
SQ   SEQUENCE   425 AA;  46454 MW;  D64D2551D7861745 CRC64;
     MPMTITEKIF AEHIGREVKP GEIIMCDVDM TIGNDITTPI SIRAFNESGA EKLAKPDNFA
     IVLDHFIPPK DIASANQAKI NRDFAYKHDL KNFFDEKDMG IEHRLLPEKG LVIPGDVIIG
     ADSHTCTHGA LGAFSTGMGS TDIAFCMITG KSWFKIPESI KVVFKGERGE HVYGKDLILE
     LIRRIGVDGA LYKALEFTGE VIENLPMDDR MSLCNMAIEA GAKNGIVAYD KITEAFLEEV
     KKYNPLRSEP KIHYSDPDAN YSQVIEIDVN KLEPLVAYPF LPSNGKPISQ AVKDDIEIDQ
     VYIGSCTNGT LSDLRIAAEI LKGKRVHRRV RLIVTPATQR IYKQAEHEGI LDILIDAGAV
     VANPTCGACL GGYMGILGDG ERAVATTNRN FRGRMGSRSS EVYLSNSAVA AASAIAGKIA
     DPRDL