ID   LEU1_BUCRP              Reviewed;         518 AA.
AC   P48571;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   25-MAY-2022, entry version 81.
DE   RecName: Full=2-isopropylmalate synthase;
DE            EC=2.3.3.13;
DE   AltName: Full=Alpha-IPM synthase;
DE   AltName: Full=Alpha-isopropylmalate synthase;
GN   Name=leuA;
OS   Buchnera aphidicola subsp. Rhopalosiphum padi.
OG   Plasmid pRPE.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=98793;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=7608990; DOI=10.1007/bf00174042;
RA   Bracho A.M., Martinez-Torres D., Moya A., Latorre A.;
RT   "Discovery and molecular characterization of a plasmid localized in
RT   Buchnera sp. bacterial endosymbiont of the aphid Rhopalosiphum padi.";
RL   J. Mol. Evol. 41:67-73(1995).
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; X71612; CAA50615.1; -; Genomic_DNA.
DR   AlphaFoldDB; P48571; -.
DR   SMR; P48571; -.
DR   UniPathway; UPA00048; UER00070.
DR   GO; GO:0003852; F:2-isopropylmalate synthase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0009098; P:leucine biosynthetic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.20.20.70; -; 1.
DR   Gene3D; 3.30.160.270; -; 1.
DR   HAMAP; MF_01025; LeuA_type1; 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   SMART; SM00917; LeuA_dimer; 1.
DR   SUPFAM; SSF110921; SSF110921; 1.
DR   TIGRFAMs; TIGR00973; leuA_bact; 1.
DR   PROSITE; PS00815; AIPM_HOMOCIT_SYNTH_1; 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..518
FT                   /note="2-isopropylmalate synthase"
FT                   /id="PRO_0000140340"
FT   DOMAIN          5..267
FT                   /note="Pyruvate carboxyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01151"
SQ   SEQUENCE   518 AA;  57336 MW;  C889C91D5720BA40 CRC64;
     MNSQVIIFDT TLRDGEQALQ ASLSVKQKLQ IALSLENTGI DIIEVGFPIS SPGDFKSVQT
     ISKNIKNSRI CSLARCLDKD IDAAAEAMHS SNAFRIHIFL ATSILHMESK LKKNFDQIID
     MAITSVKRAL RYTDDVEFSC EDASRTTMDN LCRIVEKLIN AGVKTINIPD TVGYTVPNEL
     SSIIHNLFQR VPNIDKSIIS VHCHNDLGMA VGNSISAIQA GARQIEGTIN GIGERAGNTA
     LEEVIIAIKV REDVLGVSTK IKHKEIYRTS QIISQICNLP IPPNKAIVGS NAFAHSSGIH
     QDGVLKNRKN YEIMEPSSIG LKEVKLNLTS RSGRAAVKHY MTEMGYRECD YKIDELYASF
     LKLADKKGQV FDYDLEALAF INQQQEELEH FSLSFFSVQS ISNGLSTASV KLLCGKKTFI
     ESATTSNGPI DAIYQALNRI THFPIILQKY QLIAKGKGKD ALGQVDILVE HKKRKFHGMG
     LATDIIESSA QAMVNVLNNI WKANQVNEKL KKLKKINN