ID   LEU1_CORGB              Reviewed;         616 AA.
AC   A4QAP0;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-MAY-2007, sequence version 1.
DT   25-MAY-2022, entry version 88.
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=cgR_0323;
OS   Corynebacterium glutamicum (strain R).
OC   Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC   Corynebacterium.
OX   NCBI_TaxID=340322;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R;
RX   PubMed=17379713; DOI=10.1099/mic.0.2006/003657-0;
RA   Yukawa H., Omumasaba C.A., Nonaka H., Kos P., Okai N., Suzuki N., Suda M.,
RA   Tsuge Y., Watanabe J., Ikeda Y., Vertes A.A., Inui M.;
RT   "Comparative analysis of the Corynebacterium glutamicum group and complete
RT   genome sequence of strain R.";
RL   Microbiology 153:1042-1058(2007).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AP009044; BAF53287.1; -; Genomic_DNA.
DR   RefSeq; WP_011896569.1; NC_009342.1.
DR   AlphaFoldDB; A4QAP0; -.
DR   SMR; A4QAP0; -.
DR   EnsemblBacteria; BAF53287; BAF53287; cgR_0323.
DR   KEGG; cgt:cgR_0323; -.
DR   HOGENOM; CLU_004588_3_2_11; -.
DR   OMA; WPDKVID; -.
DR   PhylomeDB; A4QAP0; -.
DR   UniPathway; UPA00048; UER00070.
DR   Proteomes; UP000006698; 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   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; Transferase.
FT   CHAIN           1..616
FT                   /note="2-isopropylmalate synthase"
FT                   /id="PRO_1000025029"
FT   DOMAIN          67..341
FT                   /note="Pyruvate carboxyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01151"
FT   REGION          1..34
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   616 AA;  68227 MW;  306AD922D425A636 CRC64;
     MSPNDAFISA PAKIETPVGP RNEGQPAWNK QRGSSMPVNR YMPFEVEVED ISLPDRTWPD
     KKITVAPQWC AVDLRDGNQA LIDPMSPERK RRMFELLVQM GFKEIEVGFP SASQTDFDFV
     REIIEKDMIP DDVTIQVLVQ AREHLIRRTF EACEGAKNVI VHFYNSTSIL QRNVVFRMDK
     DQVKKLATDA AELIKTIAQD YPDTNWRWQY SPESFTGTEV EYAKEVVDAV VEVMDPTPEN
     PMIINLPSTV EMITPNVYAD SIEWMHRNVN RRDSIILSLH PHNDRGTGVG AAELGYMAGA
     DRIEGCLFGN GERTGNVCLV TLALNMLTQG VDPQLDFTDI RQIRSTVEYC NQLRVPERHP
     YAGDLVFTAF SGSHQDAVNK GLDAMAAKVK PGANSTDVSW EELRDTEWEV PYLPIDPKDV
     GRDYEAVIRV NSQSGKGGVA YIMKTDHGLQ IPRSMQVEFS AVVQNVTDAE GGEVNSKAMW
     DIFATEYLER TAPVEQIALR VENAQTENED ASITAELIHN GKDVTVDGHG NGPLAAYANA
     LEKLGIDVEI QEYNQHARTS GDDAEAAAYV LAEVNGRKVW GVGIAGSITY ASLKAVTSAV
     NRALDVNHEA VLAGGV