ID   LEU12_RALSO             Reviewed;         576 AA.
AC   Q8XSZ5;
DT   26-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   25-MAY-2022, entry version 111.
DE   RecName: Full=2-isopropylmalate synthase 2;
DE            EC=2.3.3.13;
DE   AltName: Full=Alpha-IPM synthase 2;
DE   AltName: Full=Alpha-isopropylmalate synthase 2;
GN   Name=leuA2; OrderedLocusNames=RSp0322; ORFNames=RS05445;
OS   Ralstonia solanacearum (strain GMI1000) (Pseudomonas solanacearum).
OG   Plasmid megaplasmid Rsp.
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 2 subfamily. {ECO:0000305}.
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DR   EMBL; AL646053; CAD17473.1; -; Genomic_DNA.
DR   RefSeq; WP_011003634.1; NC_003296.1.
DR   AlphaFoldDB; Q8XSZ5; -.
DR   SMR; Q8XSZ5; -.
DR   STRING; 267608.RSp0322; -.
DR   EnsemblBacteria; CAD17473; CAD17473; RSp0322.
DR   GeneID; 60503254; -.
DR   KEGG; rso:RSp0322; -.
DR   PATRIC; fig|267608.8.peg.3797; -.
DR   eggNOG; COG0119; Bacteria.
DR   HOGENOM; CLU_004588_3_0_4; -.
DR   OMA; FGQGERT; -.
DR   UniPathway; UPA00048; UER00070.
DR   Proteomes; UP000001436; Plasmid megaplasmid Rsp.
DR   GO; GO:0003852; F:2-isopropylmalate synthase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0009098; P:leucine biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd07942; DRE_TIM_LeuA; 1.
DR   Gene3D; 3.20.20.70; -; 1.
DR   Gene3D; 3.30.160.270; -; 1.
DR   HAMAP; MF_00572; LeuA_type2; 1.
DR   InterPro; IPR013709; 2-isopropylmalate_synth_dimer.
DR   InterPro; IPR002034; AIPM/Hcit_synth_CS.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR005668; IPM_Synthase.
DR   InterPro; IPR036230; LeuA_allosteric_dom_sf.
DR   InterPro; IPR039371; LeuA_N_DRE-TIM.
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; TIGR00970; leuA_yeast; 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..576
FT                   /note="2-isopropylmalate synthase 2"
FT                   /id="PRO_0000140440"
FT   DOMAIN          31..305
FT                   /note="Pyruvate carboxyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01151"
SQ   SEQUENCE   576 AA;  63150 MW;  BBCB0A9A66BA332B CRC64;
     MLKHPATKYR PFPPIALPDR TWPSKTLTRA PIWMSTDLRD GNQALFEPMN AERKMRMFKM
     LVQIGFKEIE AAFPAASQTD YDFVRELIEG GHIPDDVTIE VLTQAREDLI RRTMESLRGA
     RRAIIHVYNA TSPVFRRTVF NTDREGVKRI AVESAKLIRE IAESMPETQW TYQYSPEVFS
     GTELDFALEV CNAVTEAWDP TPAHKIIFNL PATVEMATPN VYADQIEWMH RHLARRDSIL
     LSVHPHNDRG TAVAAAELAV MAGADRVEGC LFGNGERTGN VDLVTLALNL YSQGIDPGLD
     FSHVNDVART CEDCTQLPVH PRHPYVGDLV FTAFSGSHQD AIKKGFAVQK PDAIWEMPYL
     PIDPADVGRT YDSIIRVNSQ SGKGGVAYLL ESGYGIAMPR RLQVEFSSTV QQLTDASGRE
     ATAADIWALF QETYLRADGP IGYVSHRLAE RDDGSQHIRL VVNIADREHV CEGVGNGPLD
     ALVQALAAVL AAPVSIHHYE ERALGQGANA DAIAFAELAA PGVAGSVFGV GIDANLTTAS
     IRAVVGGVNR LAARHAQAQP GQSLLRRGMA PSMELA