ID   LEU1_BUCPS              Reviewed;         515 AA.
AC   P58898;
DT   26-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT   26-JUL-2002, sequence version 1.
DT   23-FEB-2022, entry version 62.
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. Pemphigus spyrothecae.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=98799;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=11976137; DOI=10.1128/aem.68.5.2572-2575.2002;
RA   Sabater-Munoz B., Gomez-Valero L., van Ham R.C.H.J., Silva F.J.,
RA   Latorre A.;
RT   "Molecular characterization of the leucine cluster in Buchnera sp. strain
RT   PSY, a primary endosymbiont of the aphid Pemphigus spyrothecae.";
RL   Appl. Environ. Microbiol. 68:2572-2575(2002).
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}.
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; AJ426489; CAD20137.1; -; Genomic_DNA.
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; 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   TIGRFAMs; TIGR00973; leuA_bact; 1.
DR   PROSITE; PS00815; AIPM_HOMOCIT_SYNTH_1; 1.
DR   PROSITE; PS50991; PYR_CT; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Branched-chain amino acid biosynthesis;
KW   Leucine biosynthesis; Transferase.
FT   CHAIN           1..515
FT                   /note="2-isopropylmalate synthase"
FT                   /id="PRO_0000140339"
FT   DOMAIN          5..267
FT                   /note="Pyruvate carboxyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01151"
SQ   SEQUENCE   515 AA;  57966 MW;  A0CC8FB5B33648DF CRC64;
     MGEKIIIFDT TLRDGEQALQ ASLTTKKKLK IALSLEEMGI DIIEAGFPIS SPGDFKSVET
     ISKEFKSSII CSLARCVEKD IDIAAEAMRF AKHFRIHIFL GTSPLHVKSK LKKNFSEIID
     MAIFAIKKAK RYTBDIEFSC EDAGRTPINQ LCYIVENVIK AGATTINIPD TVGFTIPYEF
     NQIIKSLYNK VPNIDKVILS VHCHNGLGMA TANSITAIQA GARQIEXTMN GMGERAGNTA
     LEEVIIAIKL KKNNLNLHTN IKHKKIYKTR KLISEICNTV IPSNKAIIGT NAFSHSSGIH
     QDGILKNRKN YEIITPKSIG LKPIKLNLTS RSGRAAVKYH MTEMGYDEKL YKLDILYNSF
     LKLADRKGQV FDYELESLAF IDQKENTTEH FRLKKFNVQH QSTGITISSI ELYCGKKIKT
     ANTRTKKGLV NSIYITLNKI TNLPIYLKNI QLITQKKPIN IIISIKVQIE YKKRQFYGIG
     NSKDIVESTA QAMIHILNNI WKANKVNILL KNIKT