ID E8PN40_THESS Unreviewed; 470 AA.
AC E8PN40;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 29-MAY-2013, entry version 18.
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=leuC; OrderedLocusNames=TSC_c07650;
OS Thermus scotoductus (strain ATCC 700910 / SA-01).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae;
OC Thermus.
OX NCBI_TaxID=743525;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700910 / SA-01;
RA Gounder K., Liesegang H., Brzuszkiewicz E., Wollherr A., Daniel R.,
RA Gottschalk G., van Heerden E., Litthauer D.;
RT "The genome sequence of Thermus scotoductus SA-01.";
RL Submitted (MAR-2010) 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; CP001962; ADW21392.1; -; Genomic_DNA.
DR RefSeq; YP_004201940.1; NC_014974.1.
DR EnsemblBacteria; ADW21392; ADW21392; TSC_c07650.
DR GeneID; 10176885; -.
DR KEGG; tsc:TSC_c07650; -.
DR PATRIC; 47044371; VBITheSco147128_0731.
DR HOGENOM; HOG000226972; -.
DR KO; K01703; -.
DR BioCyc; TSCO743525:GCD4-763-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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009098; P:leucine biosynthetic process; IEA:HAMAP.
DR Gene3D; 3.30.499.10; -; 2.
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 METAL 346 346 Iron-sulfur (4Fe-4S) (By similarity).
FT METAL 406 406 Iron-sulfur (4Fe-4S) (By similarity).
FT METAL 409 409 Iron-sulfur (4Fe-4S) (By similarity).
SQ SEQUENCE 470 AA; 51430 MW; 3610A422984EBCAD CRC64;
MGKTLYEKVW EAHEVRKLRS GQSQLFIDLH LLHEVTSPQA FGMLRDLGLK VRYPHRTFAT
VDHIVPTHDR TEPFQDPLAQ SMLEALRQNT REHGITFFDL GSGNQGIVHV IGPQLGLTQP
GMTIACGDSH TSTHGAFGAV AFGIGTSQVR DVLATQTLAA QKLKVRRINI EGKLSPGAYA
KDVILHIIRH LGVKGGLGYA YEYGGSTVEA MDMESRMTLC NMSIEGGARI GYVNPDETTF
AYLEGRPYSP KGAEWEEAKR RWKSFASDPD AHYDDVVTFQ AEEIPPTVTW GINPGQAVPI
DGRIPLLEEL SPEERPVAEE ALAYMGLKPG QPIKGVPIQV AFIGSCTNAR LSDLREVARY
LKGHKVKKGV RALVVPGSEW VARKAEEEGI AEIFREAGFE WRNPGCSMCL AMNPDRLQGD
ELAASSSNRN YKGRMGSPKG RTVLMSPLMV AAAAVAGEIA DAREVFGIGR
//
