ID   LEU1_BUCCC              Reviewed;         516 AA.
AC   Q5WQ01;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 97.
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=BCc_PL1;
OS   Buchnera aphidicola subsp. Cinara cedri (strain Cc).
OG   Plasmid pLeu-BCc.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=372461;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Cc;
RX   PubMed=16413149; DOI=10.1016/j.gene.2005.10.043;
RA   Gil R., Sabater-Munoz B., Perez-Brocal V., Silva F.J., Latorre A.;
RT   "Plasmids in the aphid endosymbiont Buchnera aphidicola with the smallest
RT   genomes. A puzzling evolutionary story.";
RL   Gene 370:17-25(2006).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Cc;
RX   PubMed=17038625; DOI=10.1126/science.1130441;
RA   Perez-Brocal V., Gil R., Ramos S., Lamelas A., Postigo M., Michelena J.M.,
RA   Silva F.J., Moya A., Latorre A.;
RT   "A small microbial genome: the end of a long symbiotic relationship?";
RL   Science 314:312-313(2006).
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; AY438025; AAR99732.1; -; Genomic_DNA.
DR   RefSeq; WP_012622901.1; NC_011878.1.
DR   AlphaFoldDB; Q5WQ01; -.
DR   SMR; Q5WQ01; -.
DR   STRING; 372461.41323035; -.
DR   PRIDE; Q5WQ01; -.
DR   EnsemblBacteria; AAR99732; AAR99732; AAR99732.
DR   KEGG; bcc:leuA; -.
DR   eggNOG; COG0119; Bacteria.
DR   HOGENOM; CLU_022158_0_1_6; -.
DR   OMA; NTMRMLV; -.
DR   OrthoDB; 840579at2; -.
DR   UniPathway; UPA00048; UER00070.
DR   Proteomes; UP000000669; Plasmid pLeu-BCc.
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..516
FT                   /note="2-isopropylmalate synthase"
FT                   /id="PRO_0000274186"
FT   DOMAIN          5..267
FT                   /note="Pyruvate carboxyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01151"
SQ   SEQUENCE   516 AA;  57461 MW;  DD2F016A3902CC06 CRC64;
     MNEKIIIFDT TLRDGEQALL TSLTSNEKIQ IALALERLGV DVIEVGFPVS SPGDFKSVQM
     LSKIIKNSKI CSLARCLPND ITIAADAMQF SKNFRIHLFL GTSDLHVSSK LKKNFNEIIE
     MAVASVKQAK KFTNDIEFSC EDAGRTTLQN LYCIIEAVIK AGATTVNIPD TVGYTTPTQF
     KKIITMLFNH VKNIHQAIIS VHCHNDLGMA VANSISAVEA GVRQIEGTMN GLGERAGNAA
     LEEVIMTLNV HKNSLKVSTD INIKEIHRTS KIVSQFCNTP IPLNKAIIGK NVFSHSSGIH
     QDGVLKNRKN YEIIDPNSIG FTDYCSLNLT SRSGRAAVKH HMKKMGYENS DYNLNELYID
     FLKLADKKGR IFDYDLEALA FFKKQQNTEE YYKLEYFDVQ SKLSGLSTAY IVLICGSQTN
     IQKATTYNGP VDAIYQALNK ATLYSIVLKK FHLEANGEGK DALGKVNIIV QYKLRNFHGV
     GLATDIIEAS AQAMVNVLNY IWKSQQVNKE LERLQK