ID   LEU1_BUCTS              Reviewed;         375 AA.
AC   O31287;
DT   26-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   25-MAY-2022, entry version 74.
DE   RecName: Full=2-isopropylmalate synthase;
DE            EC=2.3.3.13;
DE   AltName: Full=Alpha-IPM synthase;
DE   AltName: Full=Alpha-isopropylmalate synthase;
DE   Flags: Fragment;
GN   Name=leuA;
OS   Buchnera aphidicola subsp. Thelaxes suberi.
OG   Plasmid pBTs1.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=98797;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9244264; DOI=10.1128/jb.179.15.4768-4777.1997;
RA   van Ham R.C.H.J., Moya A., Latorre A.;
RT   "Putative evolutionary origin of plasmids carrying the genes involved in
RT   leucine biosynthesis in Buchnera aphidicola (endosymbiont of aphids).";
RL   J. Bacteriol. 179:4768-4777(1997).
CC   -!- FUNCTION: Catalyzes the condensation of the acetyl group of acetyl-CoA
CC       with 3-methyl-2-oxobutanoate (2-oxoisovalerate) to form 3-carboxy-3-
CC       hydroxy-4-methylpentanoate (2-isopropylmalate).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3-methyl-2-oxobutanoate + acetyl-CoA + H2O = (2S)-2-
CC         isopropylmalate + CoA + H(+); Xref=Rhea:RHEA:21524, ChEBI:CHEBI:1178,
CC         ChEBI:CHEBI:11851, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57288; EC=2.3.3.13;
CC   -!- PATHWAY: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine
CC       from 3-methyl-2-oxobutanoate: step 1/4.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the alpha-IPM synthase/homocitrate synthase
CC       family. LeuA type 1 subfamily. {ECO:0000305}.
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DR   EMBL; Y11966; CAA72697.1; -; Genomic_DNA.
DR   AlphaFoldDB; O31287; -.
DR   SMR; O31287; -.
DR   UniPathway; UPA00048; UER00070.
DR   GO; GO:0003852; F:2-isopropylmalate synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009098; P:leucine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.20.20.70; -; 1.
DR   Gene3D; 3.30.160.270; -; 1.
DR   InterPro; IPR013709; 2-isopropylmalate_synth_dimer.
DR   InterPro; IPR002034; AIPM/Hcit_synth_CS.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR036230; LeuA_allosteric_dom_sf.
DR   InterPro; IPR000891; PYR_CT.
DR   Pfam; PF00682; HMGL-like; 1.
DR   Pfam; PF08502; LeuA_dimer; 1.
DR   SMART; SM00917; LeuA_dimer; 1.
DR   SUPFAM; SSF110921; SSF110921; 1.
DR   PROSITE; PS00816; AIPM_HOMOCIT_SYNTH_2; 1.
DR   PROSITE; PS50991; PYR_CT; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Branched-chain amino acid biosynthesis;
KW   Leucine biosynthesis; Plasmid; Transferase.
FT   CHAIN           <1..375
FT                   /note="2-isopropylmalate synthase"
FT                   /id="PRO_0000140341"
FT   DOMAIN          <1..124
FT                   /note="Pyruvate carboxyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01151"
FT   NON_TER         1
SQ   SEQUENCE   375 AA;  41208 MW;  3013664DB634C7FC CRC64;
     GRTSIDNLCR IVESAIKAGA TTINIPDTVG YTIPSQFKTI IKNLFNKVPN INNAIISAHC
     HDDLGLAVGN AIASIEAGVR QIEGTISGIG ERAGNTALEE VILTIKLKEE LLNVFTNIKH
     NELYRTSQLI SQLCNTPIPA NKSIIGSNAF AHSSGIHQDG ILKNRANYEI IDPKTIGVKA
     VQLNLTSRSG RAAVKHHMHE MGYQDDDYDL NQLYVNFLKL ADKKGQVFDY DLEALAFISN
     QEDKDQEHFQ LKYFSIHSGS TGVSTASVKL LCGNKILNEI ITTRNGPINS IYQALNNIAG
     LPIVLEKFHL VGKGEGRDAL GQVDIVVKYN NRKFHGIGLA TDIIESSIKA MLNVLNNIWL
     SNKIKSKIKN IKNKK