ID   LEUD_BUCAP              Reviewed;         207 AA.
AC   O85066;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   25-MAY-2022, entry version 108.
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=BUsg_PL7;
OS   Buchnera aphidicola subsp. Schizaphis graminum (strain Sg).
OG   Plasmid pLeu-Sg (pBSg1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=198804;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Sg;
RX   PubMed=9873079; DOI=10.1007/pl00006447;
RA   Baumann L., Baumann P., Moran N.A., Sandstroem J.P., Thao M.L.;
RT   "Genetic characterization of plasmids containing genes encoding enzymes of
RT   leucine biosynthesis in endosymbionts (Buchnera) of aphids.";
RL   J. Mol. Evol. 48:77-85(1999).
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. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the LeuD family. LeuD type 1 subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AF041836; AAD12596.1; -; Genomic_DNA.
DR   RefSeq; NP_047183.1; NC_001910.1.
DR   AlphaFoldDB; O85066; -.
DR   SMR; O85066; -.
DR   OMA; KQFMKSI; -.
DR   UniPathway; UPA00048; UER00071.
DR   Proteomes; UP000000416; Plasmid pLeu-Sg.
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; Plasmid.
FT   CHAIN           1..207
FT                   /note="3-isopropylmalate dehydratase small subunit"
FT                   /id="PRO_0000141803"
SQ   SEQUENCE   207 AA;  24229 MW;  0231CC4A8E795753 CRC64;
     MFKFIEHTGV VVPLNISNID TDAIIPKQFL KKVNKIGFGK YLFHDWRFLD KNQLKINPNF
     ILNKSTYKNA SILLTRENFG CGSSREHAVW SLLDYGFKVI IASSFSDIFY SNSFNNKLLL
     IVLENEDIDY LFDLVNTKIG LSFNVSLIHK KITVDNLDIP FQIDDFQRLC LVNNWDNNDL
     TMKIDHKIKL YEKNIFSFLL KREKFTS