ID B3R123_CUPTR Unreviewed; 469 AA.
AC B3R123;
DT 02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 02-SEP-2008, sequence version 1.
DT 01-MAY-2013, entry version 37.
DE RecName: Full=3-isopropylmalate dehydratase large subunit;
DE EC=4.2.1.33;
DE AltName: Full=Alpha-IPM isomerase;
DE AltName: Full=Isopropylmalate isomerase;
GN Name=leuC1; Synonyms=leuC; OrderedLocusNames=RALTA_A2120;
OS Cupriavidus taiwanensis (strain R1 / LMG 19424) (Ralstonia taiwanensis
OS (strain LMG 19424)).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=164546;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R1 / LMG 19424;
RX PubMed=18490699; DOI=10.1101/gr.076448.108;
RA Amadou C., Pascal G., Mangenot S., Glew M., Bontemps C., Capela D.,
RA Carrere S., Cruveiller S., Dossat C., Lajus A., Marchetti M.,
RA Poinsot V., Rouy Z., Servin B., Saad M., Schenowitz C., Barbe V.,
RA Batut J., Medigue C., Masson-Boivin C.;
RT "Genome sequence of the beta-rhizobium Cupriavidus taiwanensis and
RT comparative genomics of rhizobia.";
RL Genome Res. 18:1472-1483(2008).
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; CU633749; CAQ70057.1; -; Genomic_DNA.
DR RefSeq; YP_002006120.1; NC_010528.1.
DR STRING; 164546.RALTA_A2120; -.
DR EnsemblBacteria; CAQ70057; CAQ70057; RALTA_A2120.
DR GeneID; 6454672; -.
DR KEGG; cti:RALTA_A2120; -.
DR PATRIC; 21530864; VBICupTai42494_2076.
DR eggNOG; COG0065; -.
DR HOGENOM; HOG000226972; -.
DR KO; K01703; -.
DR OMA; DIRQGIV; -.
DR ProtClustDB; PRK05478; -.
DR BioCyc; CTAI164546:GJNE-2113-MONOMER; -.
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:0016853; F:isomerase activity; 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; Isomerase; Leucine biosynthesis; Lyase; Metal-binding.
FT METAL 347 347 Iron-sulfur (4Fe-4S) (By similarity).
FT METAL 410 410 Iron-sulfur (4Fe-4S) (By similarity).
FT METAL 413 413 Iron-sulfur (4Fe-4S) (By similarity).
SQ SEQUENCE 469 AA; 50855 MW; CC9582E7D0C2125A CRC64;
MAKTLYDKLW DDHTVHVEED GTTLLYIDRH LLHEVTSPQA FEGLKMAERP VWRISANLAV
SDHNVPTTDR SQGIADPVSK LQVDTLDANC DSYGITQFKM NDHRQGIVHV IGPEQGATLP
GMTVVCGDSH TSTHGAFGAL AHGIGTSEVE HVLATQTLLG KKAKNMLVKV EGKLPRGCTA
KDIVLAVIGK IGTAGGTGYT IEFAGSAIRD LTMEGRMTVC NMAIEAGARA GLVAVDDVTL
EYVKGRPYAP QGVEWEQAVA YWRTLHSDAG AKFDQVVELR AEDVRPQVTW GTSPEMVISI
EDRVPDPEKE KDPNKRNAME RALEYMGLRP NVPVESISID KVFIGSCTNS RIEDMRAAAW
VVQKLGRKIA SNVKLAMVVP GSGLVKEQAE REGLDQIFKA AGFEWREPGC SMCLAMNADR
LDAGERCAST SNRNFEGRQG AGGRTHLVSP AMAAAAAIEG HFVDIRKLG
//
