ID   LEUD_THET8              Reviewed;         201 AA.
AC   Q9ZND4; Q5SIY5;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   25-MAY-2022, entry version 113.
DE   RecName: Full=3-isopropylmalate dehydratase small subunit;
DE            EC=4.2.1.33;
DE   AltName: Full=Alpha-IPM isomerase;
DE            Short=IPMI;
DE   AltName: Full=Isopropylmalate isomerase;
GN   Name=leuD; OrderedLocusNames=TTHA1229;
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:0000250}.
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;
CC   -!- PATHWAY: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine
CC       from 3-methyl-2-oxobutanoate: step 2/4.
CC   -!- SUBUNIT: Heterodimer of LeuC and LeuD.
CC   -!- SIMILARITY: Belongs to the LeuD family. LeuD type 1 subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AB017135; BAA37139.1; -; Genomic_DNA.
DR   EMBL; AP008226; BAD71052.1; -; Genomic_DNA.
DR   RefSeq; WP_011228533.1; NC_006461.1.
DR   RefSeq; YP_144495.1; NC_006461.1.
DR   AlphaFoldDB; Q9ZND4; -.
DR   SMR; Q9ZND4; -.
DR   STRING; 300852.55772611; -.
DR   EnsemblBacteria; BAD71052; BAD71052; BAD71052.
DR   GeneID; 3168995; -.
DR   KEGG; ttj:TTHA1229; -.
DR   PATRIC; fig|300852.9.peg.1208; -.
DR   eggNOG; COG0066; Bacteria.
DR   HOGENOM; CLU_081378_0_0_0; -.
DR   OMA; FEVNGIN; -.
DR   PhylomeDB; Q9ZND4; -.
DR   UniPathway; UPA00048; UER00071.
DR   Proteomes; UP000000532; Chromosome.
DR   GO; GO:0009316; C:3-isopropylmalate dehydratase complex; IEA:InterPro.
DR   GO; GO:0003861; F:3-isopropylmalate dehydratase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0009098; P:leucine biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd01577; IPMI_Swivel; 1.
DR   Gene3D; 3.20.19.10; -; 1.
DR   HAMAP; MF_01031; LeuD_type1; 1.
DR   InterPro; IPR004431; 3-IsopropMal_deHydase_ssu.
DR   InterPro; IPR015928; Aconitase/3IPM_dehydase_swvl.
DR   InterPro; IPR000573; AconitaseA/IPMdHydase_ssu_swvl.
DR   InterPro; IPR033940; IPMI_Swivel.
DR   Pfam; PF00694; Aconitase_C; 1.
DR   TIGRFAMs; TIGR00171; leuD; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Branched-chain amino acid biosynthesis;
KW   Leucine biosynthesis; Lyase; Reference proteome.
FT   CHAIN           1..201
FT                   /note="3-isopropylmalate dehydratase small subunit"
FT                   /id="PRO_0000141903"
SQ   SEQUENCE   201 AA;  22622 MW;  5A72EE20B4CAD172 CRC64;
     MLEKFTVIRG KAVPLRGEDI DTDRILPARF MKVLTFEGLG QYLFYDERFD EKGNPKPHPL
     NDPRYRGATI LLVESGFGSG SSREHAPQAI KRAGFKAIIG ESFAEIFFGN ATAIGLPCVS
     LAPEDLGVLF RSVEENPELE VEIDLVNKEV RFGDRTAPLF IREEAREALV EGLWDPIGEL
     LEAGELLDQF DRKLPYPRRT E