ID   LEU1_BUCUL              Reviewed;         437 AA.
AC   Q9EVE3;
DT   26-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   25-MAY-2022, entry version 64.
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. Uroleucon rurale.
OG   Plasmid pLeu (pBAp1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=168386;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=11133977; DOI=10.1128/jb.183.2.785-790.2001;
RA   Wernegreen J.J., Moran N.A.;
RT   "Vertical transmission of biosynthetic plasmids in aphid endosymbionts
RT   (Buchnera).";
RL   J. Bacteriol. 183:785-790(2001).
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). {ECO:0000250}.
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; AF200468; AAG31926.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9EVE3; -.
DR   SMR; Q9EVE3; -.
DR   PRIDE; Q9EVE3; -.
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   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; IPR005671; LeuA_bact_synth.
DR   InterPro; IPR000891; PYR_CT.
DR   Pfam; PF00682; HMGL-like; 1.
DR   Pfam; PF08502; LeuA_dimer; 1.
DR   SUPFAM; SSF110921; SSF110921; 1.
DR   TIGRFAMs; TIGR00973; leuA_bact; 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..>437
FT                   /note="2-isopropylmalate synthase"
FT                   /id="PRO_0000140343"
FT   DOMAIN          <1..241
FT                   /note="Pyruvate carboxyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01151"
FT   NON_TER         1
FT   NON_TER         437
SQ   SEQUENCE   437 AA;  48673 MW;  9F28A63674F0B087 CRC64;
     EKLQIALSLE KIGVDIMEVG FPISSPGDFK SVQTISKNIK NSRICSLARC LEKDIDAAGE
     AMSVCDNFRI HIFLATSTLH IESKLRKNFN EIIEMAIFSV KKALRYTNDV EFSCEDASRT
     NIDNLCRIVE KLIKSGVKTI NIPDTVGYST PDELTFIIKN LFERVPNIHK SIISVHCHDD
     LGMAVGNSIA AIQAGARQIE GTINGIGERA GNTALEEVIM AIKVRKNILG VSTNINHKEI
     YRTSQMISRI CNMPIPSNKA IVGSNAFSHS SGIHQDGVLK NRENYEIMDP RSIGLKKVKL
     NLTSRSGRAA VKYYMSEMGY KDSDYNIDEL YTDFLKLADK KGQVFDYDLE SLAFINKQQD
     ELEYFRLQFF SVQSISNNLS TASVKLLCGN KTYTESSTTS NGPVDAIYQA LNRITHFPII
     LQKFQLIAKG KGKDALG