ID   LEUC1_PYRFU             Reviewed;         424 AA.
AC   Q8U2A1;
DT   26-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 117.
DE   RecName: Full=3-isopropylmalate dehydratase large subunit 1 {ECO:0000255|HAMAP-Rule:MF_01027};
DE            EC=4.2.1.33 {ECO:0000255|HAMAP-Rule:MF_01027};
DE   AltName: Full=Alpha-IPM isomerase 1 {ECO:0000255|HAMAP-Rule:MF_01027};
DE            Short=IPMI 1 {ECO:0000255|HAMAP-Rule:MF_01027};
DE   AltName: Full=Isopropylmalate isomerase 1 {ECO:0000255|HAMAP-Rule:MF_01027};
GN   Name=leuC1 {ECO:0000255|HAMAP-Rule:MF_01027}; OrderedLocusNames=PF0938;
OS   Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Pyrococcus.
OX   NCBI_TaxID=186497;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX   PubMed=10430560; DOI=10.1093/genetics/152.4.1299;
RA   Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M.,
RA   DiRuggiero J., Robb F.T.;
RT   "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P.
RT   horikoshii inferred from complete genomic sequences.";
RL   Genetics 152:1299-1305(1999).
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; AE009950; AAL81062.1; -; Genomic_DNA.
DR   RefSeq; WP_011012074.1; NZ_CP023154.1.
DR   AlphaFoldDB; Q8U2A1; -.
DR   SMR; Q8U2A1; -.
DR   STRING; 186497.PF0938; -.
DR   PRIDE; Q8U2A1; -.
DR   EnsemblBacteria; AAL81062; AAL81062; PF0938.
DR   GeneID; 41712748; -.
DR   KEGG; pfu:PF0938; -.
DR   PATRIC; fig|186497.12.peg.994; -.
DR   eggNOG; arCOG01698; Archaea.
DR   HOGENOM; CLU_006714_3_4_2; -.
DR   OMA; CNMSIEM; -.
DR   OrthoDB; 15714at2157; -.
DR   PhylomeDB; Q8U2A1; -.
DR   UniPathway; UPA00048; UER00071.
DR   Proteomes; UP000001013; 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..424
FT                   /note="3-isopropylmalate dehydratase large subunit 1"
FT                   /id="PRO_0000076880"
FT   BINDING         303
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01027"
FT   BINDING         363
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"
SQ   SEQUENCE   424 AA;  46211 MW;  29BCD223CD24EAED CRC64;
     MGGMTIAEKI LATHAGKEEV KPGEIVLAKV DFMFGNDVTT PLAIKTFRKI GVEKVFDPER
     IAIVLDHFTP NKDIKAAEQC KFSREFAREQ GIKWFFEGGN VGVEHCLLPE LGLVLPGELI
     IGADSHTCTY GALGAFATGV GSTDLAVAMA TGEAWFRVPE TIKFVYEGDL QPWVTSKDLI
     LYTIGDIGVN GALYKVMEFS GEVIEKLSVE QRMTMTNMAI EAGAKTGIIE PDKKTIEYVK
     GRAKREYKIY KSDEDAKYYK VIEYDVSKIE PQVAFPHLPE NTVPISKAAK MNIKIDQVVI
     GSCTNGRLED LRMAAEVLEG QKVAPWVRLI ILPCSPTVYF KAMKEGLLEI FLEAGAVIGP
     PTCGPCLGGH MGILASGERA VSTTNRNFVG RMGHPKSEVY LASPYVAAAS AILGRIASPE
     EVVK