LEUC_THET8
ID LEUC_THET8 Reviewed; 472 AA.
AC Q9ZND5; Q5SIY6;
DT 02-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=3-isopropylmalate dehydratase large subunit {ECO:0000255|HAMAP-Rule:MF_01026};
DE EC=4.2.1.33 {ECO:0000255|HAMAP-Rule:MF_01026};
DE AltName: Full=Alpha-IPM isomerase {ECO:0000255|HAMAP-Rule:MF_01026};
DE Short=IPMI {ECO:0000255|HAMAP-Rule:MF_01026};
DE AltName: Full=Isopropylmalate isomerase {ECO:0000255|HAMAP-Rule:MF_01026};
GN Name=leuC {ECO:0000255|HAMAP-Rule:MF_01026}; OrderedLocusNames=TTHA1228;
OS Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=300852;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9813279; DOI=10.1016/s0378-1119(98)00482-x;
RA Tamakoshi M., Yamagishi A., Oshima T.;
RT "The organization of the leuC, leuD and leuB genes of the extreme
RT thermophile, Thermus thermophilus.";
RL Gene 222:125-132(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RA Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T.,
RA Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
RT "Complete genome sequence of Thermus thermophilus HB8.";
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the isomerization between 2-isopropylmalate and 3-
CC isopropylmalate, via the formation of 2-isopropylmaleate.
CC {ECO:0000255|HAMAP-Rule:MF_01026}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R,3S)-3-isopropylmalate = (2S)-2-isopropylmalate;
CC Xref=Rhea:RHEA:32287, ChEBI:CHEBI:1178, ChEBI:CHEBI:35121;
CC EC=4.2.1.33; Evidence={ECO:0000255|HAMAP-Rule:MF_01026};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01026};
CC Note=Binds 1 [4Fe-4S] cluster per subunit. {ECO:0000255|HAMAP-
CC Rule:MF_01026};
CC -!- PATHWAY: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine
CC from 3-methyl-2-oxobutanoate: step 2/4. {ECO:0000255|HAMAP-
CC Rule:MF_01026}.
CC -!- SUBUNIT: Heterodimer of LeuC and LeuD. {ECO:0000255|HAMAP-
CC Rule:MF_01026}.
CC -!- SIMILARITY: Belongs to the aconitase/IPM isomerase family. LeuC type 1
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01026}.
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DR EMBL; AB017135; BAA37138.1; -; Genomic_DNA.
DR EMBL; AP008226; BAD71051.1; -; Genomic_DNA.
DR RefSeq; WP_011173294.1; NC_006461.1.
DR RefSeq; YP_144494.1; NC_006461.1.
DR AlphaFoldDB; Q9ZND5; -.
DR SMR; Q9ZND5; -.
DR STRING; 300852.55772610; -.
DR EnsemblBacteria; BAD71051; BAD71051; BAD71051.
DR GeneID; 3168997; -.
DR KEGG; ttj:TTHA1228; -.
DR PATRIC; fig|300852.9.peg.1207; -.
DR eggNOG; COG0065; Bacteria.
DR HOGENOM; CLU_006714_3_4_0; -.
DR OMA; CNMSIEM; -.
DR PhylomeDB; Q9ZND5; -.
DR UniPathway; UPA00048; UER00071.
DR Proteomes; UP000000532; Chromosome.
DR GO; GO:0003861; F:3-isopropylmalate dehydratase activity; IEA:UniProtKB-UniRule.
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-UniRule.
DR CDD; cd01583; IPMI; 1.
DR Gene3D; 3.30.499.10; -; 2.
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; IPR001030; Acoase/IPM_deHydtase_lsu_aba.
DR InterPro; IPR018136; Aconitase_4Fe-4S_BS.
DR InterPro; IPR036008; Aconitase_4Fe-4S_dom.
DR InterPro; IPR033941; IPMI_cat.
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; Branched-chain amino acid biosynthesis;
KW Iron; Iron-sulfur; Leucine biosynthesis; Lyase; Metal-binding;
KW Reference proteome.
FT CHAIN 1..472
FT /note="3-isopropylmalate dehydratase large subunit"
FT /id="PRO_0000076834"
FT BINDING 346
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01026"
FT BINDING 406
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01026"
FT BINDING 409
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01026"
SQ SEQUENCE 472 AA; 51837 MW; 9ED139146D65B2B5 CRC64;
MGKTLYEKVW EAHEVRKLKN GQSQLFIDLH LLHEVTSPQA FGMLKDLGLR VRYPHRTFAT
VDHIVPTHDR TEPFQDPLAQ SMLEALRANT REHGITFFDL GSGNQGIVHV IGPQLGLTQP
GMTIACGDSH TSTHGAFGAV AFGIGTSQVR DVLATQTLAA QKLKVRRINV EGRLAPGVYA
KDVILHIIRH LGVKGGLGYA YEYGGSAVEA MDMESRMTLC NMSIEGGARI GYVNPDETTF
QYLEGRPYVP KGSEWEEAKR RWLAWRSDPD ASYDDVVTFR AEEIAPTVTW GITPGQAIPI
DGRIPLLEEL PEEERPVAEE ALAYMGFRPG QPIKGVPIQV AFIGSCTNAR LSDLREVARY
LKGHKVKKGV RALVVPGSEW VARKAEEEGI AEVFREAGFE WRMPGCSMCL AMNPDRLEGD
ELCASSSNRN YKGRMGSPRG RTVLMSPLMV AAAAVAGEIA DAREVFGLAG VR
