ID   LEU1_BUCDN              Reviewed;         516 AA.
AC   O85070;
DT   26-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=2-isopropylmalate synthase {ECO:0000255|HAMAP-Rule:MF_01025};
DE            EC=2.3.3.13 {ECO:0000255|HAMAP-Rule:MF_01025};
DE   AltName: Full=Alpha-IPM synthase {ECO:0000255|HAMAP-Rule:MF_01025};
DE   AltName: Full=Alpha-isopropylmalate synthase {ECO:0000255|HAMAP-Rule:MF_01025};
GN   Name=leuA {ECO:0000255|HAMAP-Rule:MF_01025};
OS   Buchnera aphidicola subsp. Diuraphis noxia.
OG   Plasmid pLeu-Dn (pBDn1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=118101;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9873079; DOI=10.1007/pl00006447;
RA   Baumann L., Baumann P., Moran N.A., Sandstroem J.P., Thao M.L.;
RT   "Genetic characterization of plasmids containing genes encoding enzymes of
RT   leucine biosynthesis in endosymbionts (Buchnera) of aphids.";
RL   J. Mol. Evol. 48:77-85(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-13.
RX   PubMed=9812361; DOI=10.1111/j.1574-6968.1998.tb13253.x;
RA   Silva F.J., van Ham R.C.H.J., Sabater B., Latorre A.;
RT   "Structure and evolution of the leucine plasmids carried by the
RT   endosymbiont (Buchnera aphidicola) from aphids of the family Aphididae.";
RL   FEMS Microbiol. Lett. 168:43-49(1998).
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         Evidence={ECO:0000255|HAMAP-Rule:MF_01025};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine
CC       from 3-methyl-2-oxobutanoate: step 1/4. {ECO:0000255|HAMAP-
CC       Rule:MF_01025}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_01025}.
CC   -!- SIMILARITY: Belongs to the alpha-IPM synthase/homocitrate synthase
CC       family. LeuA type 1 subfamily. {ECO:0000255|HAMAP-Rule:MF_01025}.
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DR   EMBL; AF041837; AAD12600.1; -; Genomic_DNA.
DR   EMBL; AJ006880; CAA07311.1; -; Genomic_DNA.
DR   RefSeq; NP_047187.1; NC_001911.1.
DR   AlphaFoldDB; O85070; -.
DR   SMR; O85070; -.
DR   PRIDE; O85070; -.
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..516
FT                   /note="2-isopropylmalate synthase"
FT                   /id="PRO_0000140337"
FT   DOMAIN          5..267
FT                   /note="Pyruvate carboxyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01151"
SQ   SEQUENCE   516 AA;  57259 MW;  2A053D9ADB68E862 CRC64;
     MSSKVIIFDT TLRDGEQALQ ASLSVKEKLQ IALSLEKCGI DIIEVGFPIS SPGDFKSVQT
     ISKKIKNSRI CSLARCVEKD IEVAGDAMSS SDFFRIHIFL ATSTLHMESK LRKNFDEIID
     MAVSSVKKAL RYTDDVEFSC EDASRTTMDN LCRIVEKLIK AGVKTINIPD TVGYTIPNEL
     SNIIKNLFER VPNIHKSIIS VHCHNDLGMA VGNSISAIQA GARQIEGTIN GIGERAGNTA
     LEEIIMAIKV REDILGVSTN IVHKEIYRTS QIISQICNMP IPANKAIVGS NAFAHSSGIH
     QDGVLKNRKN YEIMEPNTIG VKEVKLNLTS RSGRAAVKYY MDKMGYKDDD YDIDELYSAF
     LKLADKKGQV FDYDLEALAI FSKKQENAEY FYLKFFSVQS ISNGLSTASV KLKCGKKVYT
     ESSTTSNGPV DATYQALNKI INFPITLQKF QLVAKGKGKD ALGQVDILVK YENRQFHGIG
     LATDIIESSA QAMINVLNNI WKSQQVNKKL KNLKKY