ID   LEUC_PYRIL              Reviewed;         414 AA.
AC   A1RVH3;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   11-JUL-2012, entry version 45.
DE   RecName: Full=3-isopropylmalate dehydratase large subunit;
DE            EC=4.2.1.33;
DE   AltName: Full=Alpha-IPM isomerase;
DE            Short=IPMI;
DE   AltName: Full=Isopropylmalate isomerase;
GN   Name=leuC; OrderedLocusNames=Pisl_1806;
OS   Pyrobaculum islandicum (strain DSM 4184 / JCM 9189).
OC   Archaea; Crenarchaeota; Thermoprotei; Thermoproteales;
OC   Thermoproteaceae; Pyrobaculum.
OX   NCBI_TaxID=384616;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 4184 / JCM 9189;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Dalin E., Tice H., Pitluck S., Meincke L.,
RA   Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Lowe T.,
RA   Richardson P.;
RT   "Complete sequence of Pyrobaculum islandicum DSM 4184.";
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the isomerization between 2-isopropylmalate
CC       and 3-isopropylmalate, via the formation of 2-isopropylmaleate.
CC   -!- CATALYTIC ACTIVITY: (2R,3S)-3-isopropylmalate = (2S)-2-
CC       isopropylmaleate + H(2)O.
CC   -!- CATALYTIC ACTIVITY: (2S)-2-isopropylmaleate + H(2)O = (2S)-2-
CC       isopropylmalate.
CC   -!- COFACTOR: Binds 1 4Fe-4S cluster per subunit (By similarity).
CC   -!- PATHWAY: Amino-acid biosynthesis; L-leucine biosynthesis; L-
CC       leucine from 3-methyl-2-oxobutanoate: step 2/4.
CC   -!- SUBUNIT: Heterodimer of LeuC and LeuD (By similarity).
CC   -!- SIMILARITY: Belongs to the aconitase/IPM isomerase family. LeuC
CC       type 2 subfamily.
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DR   EMBL; CP000504; ABL88955.1; -; Genomic_DNA.
DR   RefSeq; YP_931298.1; NC_008701.1.
DR   STRING; A1RVH3; -.
DR   GeneID; 4616859; -.
DR   GenomeReviews; CP000504_GR; Pisl_1806.
DR   KEGG; pis:Pisl_1806; -.
DR   eggNOG; COG0065; -.
DR   HOGENOM; HOG000226971; -.
DR   KO; K01703; -.
DR   OMA; SMGKVEV; -.
DR   ProtClustDB; PRK00402; -.
DR   BioCyc; PISL384616:PISL_1806-MONOMER; -.
DR   GO; GO:0003861; F:3-isopropylmalate dehydratase activity; IEA:EC.
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-KW.
DR   Gene3D; G3DSA:3.30.499.10; Acnase/IPM_dHydase_lsu_aba_1/3; 2.
DR   Gene3D; G3DSA:3.40.1060.10; Aconitase/IPMdHydase_lsu_aba_2; 1.
DR   HAMAP; MF_01027; LeuC_type2; 1; -.
DR   InterPro; IPR015931; Acnase/IPM_dHydase_lsu_aba_1/3.
DR   InterPro; IPR015937; Acoase/IPM_deHydtase.
DR   InterPro; IPR001030; Acoase/IPM_deHydtase_lsu_aba.
DR   InterPro; IPR015932; Aconitase/IPMdHydase_lsu_aba_2.
DR   InterPro; IPR018136; Aconitase_4Fe-4S_BS.
DR   InterPro; IPR011826; HAcnase/IPMdehydase_lsu_prok.
DR   InterPro; IPR006251; Homoacnase/IPMdehydase_lsu.
DR   PANTHER; PTHR11670; Aconitase-like_core; 1.
DR   PANTHER; PTHR11670:SF16; PTHR11670:SF16; 1.
DR   Pfam; PF00330; Aconitase; 2.
DR   PRINTS; PR00415; ACONITASE.
DR   SUPFAM; SSF53732; Aconitase_N; 1.
DR   TIGRFAMs; TIGR01343; HacA_fam; 1.
DR   TIGRFAMs; TIGR02086; IPMI_arch; 1.
DR   PROSITE; PS00450; ACONITASE_1; FALSE_NEG.
DR   PROSITE; PS01244; ACONITASE_2; 1.
PE   3: Inferred from homology;
KW   4Fe-4S; Amino-acid biosynthesis;
KW   Branched-chain amino acid biosynthesis; Complete proteome; Iron;
KW   Iron-sulfur; Leucine biosynthesis; Lyase; Metal-binding.
FT   CHAIN         1    414       3-isopropylmalate dehydratase large
FT                                subunit.
FT                                /FTId=PRO_1000063654.
FT   METAL       295    295       Iron-sulfur (4Fe-4S) (By similarity).
FT   METAL       353    353       Iron-sulfur (4Fe-4S) (By similarity).
FT   METAL       356    356       Iron-sulfur (4Fe-4S) (By similarity).
SQ   SEQUENCE   414 AA;  45069 MW;  E524DE87B167F3E6 CRC64;
     MPTWTEYIFQ KKLGHTPSPG DVVEVVPDLV GFHDLTGYHV LEVLESMGKV EVFDKERVVV
     AFDHLSPPPT QRAAEIMVYI RKHVKALELP HFYDVGGGIL HQIILEKYAM PEYVIFAADS
     HTNTAGAVGA FAHGMGATDI AAALKLGKTW VVIPAPFRVD MKGEFPPGVM GKDVALHLLK
     QFGAEGFNGY SVEVFVEIPK AFPMDDRATV ANMSTEMGAD ALMFIPDVVT VDYLQRERGV
     SYKPPDLQPG RYVDKYVVEL SKLEPLVAAP YSVDNVKAVR EVEGVEVDQV FIGSCTNGRL
     SDFEIAARIL RRGRVKSRCI AIPASYTIFR KALELGYIDI LTKAGCVVTY GTCGPCLGGH
     FGVAGPGEVV VSTSNRNFKG RMGHPDSKVY LANPATAAAA ALEGKIVDPR PYLL
//