ID   LEU1_PARXL              Reviewed;         572 AA.
AC   Q13WM0;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2006, sequence version 1.
DT   25-MAY-2022, entry version 94.
DE   RecName: Full=2-isopropylmalate synthase {ECO:0000255|HAMAP-Rule:MF_00572};
DE            EC=2.3.3.13 {ECO:0000255|HAMAP-Rule:MF_00572};
DE   AltName: Full=Alpha-IPM synthase {ECO:0000255|HAMAP-Rule:MF_00572};
DE   AltName: Full=Alpha-isopropylmalate synthase {ECO:0000255|HAMAP-Rule:MF_00572};
GN   Name=leuA {ECO:0000255|HAMAP-Rule:MF_00572}; OrderedLocusNames=Bxeno_A2981;
GN   ORFNames=Bxe_A1435;
OS   Paraburkholderia xenovorans (strain LB400).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=266265;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LB400;
RX   PubMed=17030797; DOI=10.1073/pnas.0606924103;
RA   Chain P.S.G., Denef V.J., Konstantinidis K.T., Vergez L.M., Agullo L.,
RA   Reyes V.L., Hauser L., Cordova M., Gomez L., Gonzalez M., Land M., Lao V.,
RA   Larimer F., LiPuma J.J., Mahenthiralingam E., Malfatti S.A., Marx C.J.,
RA   Parnell J.J., Ramette A., Richardson P., Seeger M., Smith D., Spilker T.,
RA   Sul W.J., Tsoi T.V., Ulrich L.E., Zhulin I.B., Tiedje J.M.;
RT   "Burkholderia xenovorans LB400 harbors a multi-replicon, 9.73-Mbp genome
RT   shaped for versatility.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15280-15287(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:0000255|HAMAP-
CC       Rule:MF_00572}.
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_00572};
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_00572}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_00572}.
CC   -!- SIMILARITY: Belongs to the alpha-IPM synthase/homocitrate synthase
CC       family. LeuA type 2 subfamily. {ECO:0000255|HAMAP-Rule:MF_00572}.
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DR   EMBL; CP000270; ABE31519.1; -; Genomic_DNA.
DR   RefSeq; WP_011489091.1; NZ_CP008760.1.
DR   AlphaFoldDB; Q13WM0; -.
DR   SMR; Q13WM0; -.
DR   STRING; 266265.Bxe_A1435; -.
DR   EnsemblBacteria; ABE31519; ABE31519; Bxe_A1435.
DR   KEGG; bxb:DR64_3600; -.
DR   KEGG; bxe:Bxe_A1435; -.
DR   PATRIC; fig|266265.5.peg.3134; -.
DR   eggNOG; COG0119; Bacteria.
DR   OMA; FGQGERT; -.
DR   OrthoDB; 840579at2; -.
DR   UniPathway; UPA00048; UER00070.
DR   Proteomes; UP000001817; Chromosome 1.
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; Reference proteome; Transferase.
FT   CHAIN           1..572
FT                   /note="2-isopropylmalate synthase"
FT                   /id="PRO_1000129501"
FT   DOMAIN          31..305
FT                   /note="Pyruvate carboxyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01151"
SQ   SEQUENCE   572 AA;  63382 MW;  041FFF8CC83C993D CRC64;
     MLKNPATKYR SFKPIDLTDR QWPSRTITRP PIWMSTDLRD GNQSLFEPMD AQRKMRMFKT
     LVQIGFKEIE VAFPSASQTD FNFVRELIEG GHIPDDVTIE VLTQARDDLI ERTFESLRGV
     PRAIVHLYNA TAPEFRKIVF NLEKSGVKEL AQNAARTMKR IAATMPETQF TFQYSPEVFS
     GTEIEFAKEV CDAVFDIWEP TPEHKAIVNL PATVEMSTPN IYADQIEWMH RNLKRRDSLV
     ISVHPHNDRG TAVAAAELAV MAGADRIEGC LFGNGERTGN VDLVTLALNL YTQGVDPGLD
     FSNINEVART AEECTQLPIH PRHPYVGDLV FTAFSGSHQD AIKKGFAVQK PDAMWEVPYM
     PIDPADLGRT YDSVIRVNSQ SGKGGIAYLL EQGYGVVLPR RLQVDFSSAV QRFTDDSGQE
     VTSAQIWELF QQEYVQNATP VHYVGHSLSE RDGREHIKLT VDINGTRRVL NGAGNGPLDA
     LMHAIGVPVR IQHYEERALT QGADARAVAV AEMAGADVTG SAFGVGIDAN LVTASIRAVI
     SGVNRAYARV NAQAKERFFE AAMNDATESV GV