ID LEUC_SHEPA Reviewed; 466 AA.
AC A8H999;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 1.
DT 01-MAY-2013, entry version 47.
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=Spea_3826;
OS Shewanella pealeana (strain ATCC 700345 / ANG-SQ1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=398579;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700345 / ANG-SQ1;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T.,
RA Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D.,
RA Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Kim E., Zhao J.-S.Z., Manno D., Hawari J., Richardson P.;
RT "Complete sequence of Shewanella pealeana ATCC 700345.";
RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the isomerization between 2-isopropylmalate
CC and 3-isopropylmalate, via the formation of 2-isopropylmaleate (By
CC similarity).
CC -!- CATALYTIC ACTIVITY: (2R,3S)-3-isopropylmalate = (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 1 subfamily.
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DR EMBL; CP000851; ABV89136.1; -; Genomic_DNA.
DR RefSeq; YP_001503671.1; NC_009901.1.
DR STRING; 398579.Spea_3826; -.
DR PRIDE; A8H999; -.
DR EnsemblBacteria; ABV89136; ABV89136; Spea_3826.
DR GeneID; 5664210; -.
DR KEGG; spl:Spea_3826; -.
DR PATRIC; 23537853; VBIShePea72822_3993.
DR eggNOG; COG0065; -.
DR HOGENOM; HOG000226972; -.
DR KO; K01703; -.
DR OMA; DIRQGIV; -.
DR ProtClustDB; PRK05478; -.
DR UniPathway; UPA00048; UER00071.
DR GO; GO:0003861; F:3-isopropylmalate dehydratase activity; IEA:HAMAP.
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:HAMAP.
DR Gene3D; 3.30.499.10; -; 3.
DR Gene3D; 3.40.1060.10; -; 1.
DR HAMAP; MF_01026; LeuC_type1; 1; -.
DR InterPro; IPR004430; 3-IsopropMal_deHydase_lsu.
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 PANTHER; PTHR11670; PTHR11670; 1.
DR Pfam; PF00330; Aconitase; 1.
DR PRINTS; PR00415; ACONITASE.
DR SUPFAM; SSF53732; Aconitase_N; 1.
DR TIGRFAMs; TIGR00170; leuC; 1.
DR PROSITE; PS00450; ACONITASE_1; 1.
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 1 466 3-isopropylmalate dehydratase large
FT subunit.
FT /FTId=PRO_1000084227.
FT METAL 347 347 Iron-sulfur (4Fe-4S) (By similarity).
FT METAL 407 407 Iron-sulfur (4Fe-4S) (By similarity).
FT METAL 410 410 Iron-sulfur (4Fe-4S) (By similarity).
SQ SEQUENCE 466 AA; 49636 MW; D34183308D5D3FBC CRC64;
MAKTLYEKVW DSHVVVAPEG EAPIIYVDRH LVHEVTSPQA FSGVKVAGRQ LRAPQKTFAT
MDHNTSTTSA SLDALSPMAR TQVETLEQNC KEFGVRLYDI HHKNQGIVHV MGPELGITLP
GTVIVCGDSH TATHGAFGAL AFGIGTSEVE HVMATQTLRQ LKAKTMKIEV RGHVASGITA
KDIVLAIIGK IGMDGGTGYV VEFCGEAIEA LSMEGRMTVC NMAIEMGAKA GMIAPDATTA
EYLEGREFSP KGESWSQAVA AWEQLKTDEG AVFDASVVLD AIDIAPQLTW GTNPGQVVAI
DQLVPNPLDA TNSTVRSSIE KALEYVDLTA GTLMTDVSIN KVFIGSCTNS RIEDLRAAAV
HAKGRKVADG VKAIVVPGSG LVKEQAEAEG LDKIFTDAGF EWRLPGCSMC LAMNDDKLEA
GDRCASTSNR NFEGRQGRGS RTHLVSPAMA AAAAVAGHFV DIRKPY
//
