ID   LEU1_BUCAI              Reviewed;         519 AA.
AC   Q9ZEY8; Q9EVG1; Q9KGQ0;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2000, sequence version 3.
DT   25-MAY-2022, entry version 125.
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; OrderedLocusNames=BUpL04;
OS   Buchnera aphidicola subsp. Acyrthosiphon pisum (strain APS) (Acyrthosiphon
OS   pisum symbiotic bacterium).
OG   Plasmid pLeu (pBAp1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=107806;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=APS;
RX   PubMed=10993077; DOI=10.1038/35024074;
RA   Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H.;
RT   "Genome sequence of the endocellular bacterial symbiont of aphids Buchnera
RT   sp. APS.";
RL   Nature 407:81-86(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 14-519.
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; AJ006878; CAA07305.2; -; Genomic_DNA.
DR   EMBL; AP001071; BAA95423.1; -; Genomic_DNA.
DR   EMBL; AF197457; AAG31404.1; -; Genomic_DNA.
DR   RefSeq; NP_057968.1; NC_002253.1.
DR   RefSeq; WP_010892294.1; NC_002253.1.
DR   AlphaFoldDB; Q9ZEY8; -.
DR   SMR; Q9ZEY8; -.
DR   EnsemblBacteria; BAA95423; BAA95423; BAA95423.
DR   KEGG; buc:BUpL04; -.
DR   PATRIC; fig|107806.10.peg.10; -.
DR   HOGENOM; CLU_022158_0_1_6; -.
DR   OMA; NTMRMLV; -.
DR   UniPathway; UPA00048; UER00070.
DR   Proteomes; UP000001806; Plasmid pLeu.
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; Reference proteome; Transferase.
FT   CHAIN           1..519
FT                   /note="2-isopropylmalate synthase"
FT                   /id="PRO_0000140334"
FT   DOMAIN          5..267
FT                   /note="Pyruvate carboxyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01151"
FT   CONFLICT        188
FT                   /note="F -> L (in Ref. 1; CAA07305)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        358
FT                   /note="T -> I (in Ref. 1; CAA07305 and 3; AAG31404)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   519 AA;  57592 MW;  5044AC1D617E072A CRC64;
     MKSKVVIFDT TLRDGEQALQ ASLSVKEKLQ IALSLEKCGI DILEIGFPVS SPGDFKSVQT
     ISKNIKNSRI CSLARCIEKD IDAAGEAMSS SDSFRIHIFL ATSTLHMESK LKKNFNEIID
     MAVFSVKKAL RYTDDIEFSC EDATRTTMDN LCRIVETLIK SGVKTINIPD TVGYTVPNEL
     SCIIKNLFER VPNIHKSIIS VHCHDDLGMA VGNSISAIQA GARQIEGTIN GIGERAGNTA
     LEEIIMAIKV REDILSVSTN INYKEIYRTS KIVSQICNMP IPSNKAIVGS NAFAHSSGIH
     QDGVLKNRKN YEIMEPSSIG LKEVKLNLTS RSGRAAVKHY MDEMGYNNSD YNIDELYTAF
     LKLADKKGQV FDYDLEALAF INKQQDEWEY FSLKFFSVQS ISNSLSTASV KLLCGKKTYT
     ESSTTSNGPV DAIYQALNRI ACFPIILQKF QLVAKGKGKD ALGQVDILVE HKKRKFHGVG
     LATDIIEASA QAMINVLNNI WKAKQVNKKL KILKDFKKK