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Database: UniProt/TrEMBL
Entry: B3R123_CUPTR
LinkDB: B3R123_CUPTR
Original site: B3R123_CUPTR 
ID   B3R123_CUPTR            Unreviewed;       469 AA.
AC   B3R123;
DT   02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   02-SEP-2008, sequence version 1.
DT   11-JUN-2014, entry version 44.
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; APTGVEW; -.
DR   OrthoDB; EOG600DP5; -.
DR   BioCyc; CTAI164546:GJNE-2113-MONOMER; -.
DR   BioCyc; CTAI977880:GLC7-2113-MONOMER; -.
DR   UniPathway; UPA00048; UER00071.
DR   GO; GO:0003861; F:3-isopropylmalate dehydratase activity; IEA:UniProtKB-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:UniProtKB-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; SSF53732; 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
FT                                similarity){EA16}.
FT   METAL       410    410       Iron-sulfur (4Fe-4S) (By
FT                                similarity){EA16}.
FT   METAL       413    413       Iron-sulfur (4Fe-4S) (By
FT                                similarity){EA16}.
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
//
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