ID   LEU1_KOCRD              Reviewed;         584 AA.
AC   B2GHT7;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 1.
DT   25-MAY-2022, entry version 76.
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=KRH_12930;
OS   Kocuria rhizophila (strain ATCC 9341 / DSM 348 / NBRC 103217 / DC2201).
OC   Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; Kocuria.
OX   NCBI_TaxID=378753;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 9341 / DSM 348 / NBRC 103217 / DC2201;
RX   PubMed=18408034; DOI=10.1128/jb.01853-07;
RA   Takarada H., Sekine M., Kosugi H., Matsuo Y., Fujisawa T., Omata S.,
RA   Kishi E., Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.;
RT   "Complete genome sequence of the soil actinomycete Kocuria rhizophila.";
RL   J. Bacteriol. 190:4139-4146(2008).
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; AP009152; BAG29640.1; -; Genomic_DNA.
DR   RefSeq; WP_012398361.1; NC_010617.1.
DR   AlphaFoldDB; B2GHT7; -.
DR   SMR; B2GHT7; -.
DR   STRING; 378753.KRH_12930; -.
DR   EnsemblBacteria; BAG29640; BAG29640; KRH_12930.
DR   KEGG; krh:KRH_12930; -.
DR   eggNOG; COG0119; Bacteria.
DR   HOGENOM; CLU_004588_3_1_11; -.
DR   OMA; WPDKVID; -.
DR   OrthoDB; 840579at2; -.
DR   UniPathway; UPA00048; UER00070.
DR   Proteomes; UP000008838; 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; Reference proteome; Transferase.
FT   CHAIN           1..584
FT                   /note="2-isopropylmalate synthase"
FT                   /id="PRO_1000129506"
FT   DOMAIN          40..314
FT                   /note="Pyruvate carboxyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01151"
SQ   SEQUENCE   584 AA;  64634 MW;  EEDDA8C29946F4AB CRC64;
     MKNLQRPSGM PAHKYTPYHQ NFPFDMSDRT WPDKVATTAP RWCAVDLRDG NQALIDPMDS
     ERKLRMFQLL VGMGYKEIEV GFPSASQTDF DFVRTLVEGG HIPEDVSIQV LTQSREHLIE
     RTYEAIDGAP NAIVHLYNST STLQRRVVFH QDMDGIVDIA LTGARLCRKY EEQLSGTAVT
     YEYSPESYTG TELEFAARIC NEVAETFEIG NGRKMIVNLP ATVEMATPNV YADSIEWMGR
     HLYQREDIIL SLHPHNDRGT GVAAAELGYL AGADRIEGCL FGNGERTGNV DLVTLGLNLL
     TQGVDPQIDF SDIEEIRRTV EYCNQLPVPE RSPYGGDLVF TAFSGSHQDA IKKGFEAMER
     DAEQQGVGVD ELEWAVPYLP IDPKDVGRSY EAVIRVNSQS GKGGVAYLLK SEYGIDLPRR
     AQIEFSGVVQ KFTETSGSEV SAQQLWTIFR DEYLPSRDGS GSTWGHYRIT SISTHAEDQA
     NTVLEIGLDV GGEHKERTAQ GTGPIDALIN LFNREGMDVR LLDYTEHTLS ASANAQAASY
     VELAVGDRVL WGAGMDSNTT RASLKAVISA VNRAVRDAQE AAQD