ID   LEU1_BUCUM              Reviewed;         503 AA.
AC   Q9EVH0;
DT   26-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   25-MAY-2022, entry version 69.
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 ambrosiae.
OG   Plasmid pLeu (pBAp1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=118117;
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AF197454; AAG31395.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9EVH0; -.
DR   SMR; Q9EVH0; -.
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   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; 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..503
FT                   /note="2-isopropylmalate synthase"
FT                   /id="PRO_0000140344"
FT   DOMAIN          <1..254
FT                   /note="Pyruvate carboxyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01151"
FT   NON_TER         1
SQ   SEQUENCE   503 AA;  55717 MW;  B372C5BF2C17BA1C CRC64;
     DGEQALQASL SVKEKLQIAL CLEKSGVDIM EVGFPISSPG DFKSVQTISQ KIKNSRVCSL
     ARCIEKDIDV AGEAMSASNS FRIHIFLATS TLHMESKLRK NFNEIIDMAI FSVKRALRYT
     DDIEFSCEDA SRTTIDNLCR IVEKLISCGV KTINIPDTVG YTIPNELSFI IKNLFEKVPN
     IHKSTISVHC HDDLGMAVGN SISAIQAGAR QIEGTINGIG ERAGNTALEE VIMAIKVRED
     ILGVSTNINH KEIYRTSQIV SSICNMPIPS NKAIVGSNAF AHSSGIHQDG VLKNRENYEI
     IDPISIGLKK VKLNLTSRSG RAAVKHYMNE MGYKENDYNI DELYTDFLKL ADKKGQVFDY
     DLEALAFINK QQDESEYFSL KFFSVQSISN NLSTASVTLL CGKKIYTEAS TTSNGPVDAI
     YQALNRITHF PIVLQKFQLV AKGKGKDALG QVDILVEYKK RKFHGVGLAT DIMESSAKAM
     VNVLNNIWKA KQVNKNLKNL KKQ