ID   LEU11_RALSO             Reviewed;         513 AA.
AC   Q8XXP1;
DT   26-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   25-MAY-2022, entry version 107.
DE   RecName: Full=2-isopropylmalate synthase 1;
DE            EC=2.3.3.13;
DE   AltName: Full=Alpha-IPM synthase 1;
DE   AltName: Full=Alpha-isopropylmalate synthase 1;
GN   Name=leuA1; OrderedLocusNames=RSc2072; ORFNames=RS03637;
OS   Ralstonia solanacearum (strain GMI1000) (Pseudomonas solanacearum).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Ralstonia.
OX   NCBI_TaxID=267608;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GMI1000;
RX   PubMed=11823852; DOI=10.1038/415497a;
RA   Salanoubat M., Genin S., Artiguenave F., Gouzy J., Mangenot S., Arlat M.,
RA   Billault A., Brottier P., Camus J.-C., Cattolico L., Chandler M.,
RA   Choisne N., Claudel-Renard C., Cunnac S., Demange N., Gaspin C., Lavie M.,
RA   Moisan A., Robert C., Saurin W., Schiex T., Siguier P., Thebault P.,
RA   Whalen M., Wincker P., Levy M., Weissenbach J., Boucher C.A.;
RT   "Genome sequence of the plant pathogen Ralstonia solanacearum.";
RL   Nature 415:497-502(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). {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; AL646052; CAD15779.1; -; Genomic_DNA.
DR   RefSeq; WP_011002004.1; NC_003295.1.
DR   AlphaFoldDB; Q8XXP1; -.
DR   SMR; Q8XXP1; -.
DR   STRING; 267608.RSc2072; -.
DR   EnsemblBacteria; CAD15779; CAD15779; RSc2072.
DR   GeneID; 60501584; -.
DR   KEGG; rso:RSc2072; -.
DR   eggNOG; COG0119; Bacteria.
DR   HOGENOM; CLU_022158_0_1_4; -.
DR   OMA; NTMRMLV; -.
DR   UniPathway; UPA00048; UER00070.
DR   Proteomes; UP000001436; Chromosome.
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; Reference proteome; Transferase.
FT   CHAIN           1..513
FT                   /note="2-isopropylmalate synthase 1"
FT                   /id="PRO_0000140372"
FT   DOMAIN          5..268
FT                   /note="Pyruvate carboxyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01151"
SQ   SEQUENCE   513 AA;  55573 MW;  62A68CAE3E66C0C2 CRC64;
     MSDKLIIFDT TLRDGEQSPG ASMTKEEKIR IAKQLERLKV DVIEAGFAAS SNGDFEAIRA
     IAQSVKDSRI CSLARANDRD ISRAAEALKP AGQFRIHTFI ATSALHMEKK LRMTPDQVYE
     QARLAVRFAR QFTDDIEFSP EDGSRSDMDF LCRVLEGVIA EGATTINLPD TVGYAVPEGY
     AALIRSVRER IPNSDKAIWS VHCHNDLGMA VANSLAAVKL GGARQIECTI NGLGERAGNT
     SLEEVVMAVK TRRDYFNLDV GVDTTQIVPA SKLVSQITGF VVQPNKAVVG ANAFAHASGI
     HQDGVLKARD TYEIMRAEDV GWTANKIVLG KLSGRNAFKQ RLQELGIELD SEAELNAAFT
     RFKELADQKA EIFDEDIVAI VSNEAQHAEG EHFRFVSLSQ RSETGERPHA RIVFVADGKE
     VTGEAEGNGP VDATLNAIES KVASGAEQLL YSVNAITTGT QAQGEVTVRL SKSGRIVNGV
     GTDPDIVAAS AKAYLAALNK LQDKSSEKLN PQI