ID   LEU1_BRASO              Reviewed;         525 AA.
AC   A4YZ76;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=2-isopropylmalate synthase {ECO:0000255|HAMAP-Rule:MF_01025};
DE            EC=2.3.3.13 {ECO:0000255|HAMAP-Rule:MF_01025};
DE   AltName: Full=Alpha-IPM synthase {ECO:0000255|HAMAP-Rule:MF_01025};
DE   AltName: Full=Alpha-isopropylmalate synthase {ECO:0000255|HAMAP-Rule:MF_01025};
GN   Name=leuA {ECO:0000255|HAMAP-Rule:MF_01025}; OrderedLocusNames=BRADO5528;
OS   Bradyrhizobium sp. (strain ORS 278).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Bradyrhizobiaceae; Bradyrhizobium; unclassified Bradyrhizobium.
OX   NCBI_TaxID=114615;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ORS 278;
RX   PubMed=17540897; DOI=10.1126/science.1139548;
RA   Giraud E., Moulin L., Vallenet D., Barbe V., Cytryn E., Avarre J.-C.,
RA   Jaubert M., Simon D., Cartieaux F., Prin Y., Bena G., Hannibal L.,
RA   Fardoux J., Kojadinovic M., Vuillet L., Lajus A., Cruveiller S., Rouy Z.,
RA   Mangenot S., Segurens B., Dossat C., Franck W.L., Chang W.-S., Saunders E.,
RA   Bruce D., Richardson P., Normand P., Dreyfus B., Pignol D., Stacey G.,
RA   Emerich D., Vermeglio A., Medigue C., Sadowsky M.;
RT   "Legumes symbioses: absence of nod genes in photosynthetic bradyrhizobia.";
RL   Science 316:1307-1312(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_01025}.
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_01025};
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_01025}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_01025}.
CC   -!- SIMILARITY: Belongs to the alpha-IPM synthase/homocitrate synthase
CC       family. LeuA type 1 subfamily. {ECO:0000255|HAMAP-Rule:MF_01025}.
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DR   EMBL; CU234118; CAL79202.1; -; Genomic_DNA.
DR   RefSeq; WP_012029114.1; NC_009445.1.
DR   AlphaFoldDB; A4YZ76; -.
DR   SMR; A4YZ76; -.
DR   STRING; 114615.BRADO5528; -.
DR   EnsemblBacteria; CAL79202; CAL79202; BRADO5528.
DR   KEGG; bra:BRADO5528; -.
DR   eggNOG; COG0119; Bacteria.
DR   HOGENOM; CLU_022158_0_1_5; -.
DR   OMA; NTMRMLV; -.
DR   OrthoDB; 840579at2; -.
DR   BioCyc; BSP114615:BRADO_RS25705-MON; -.
DR   UniPathway; UPA00048; UER00070.
DR   Proteomes; UP000001994; 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..525
FT                   /note="2-isopropylmalate synthase"
FT                   /id="PRO_1000149142"
FT   DOMAIN          12..274
FT                   /note="Pyruvate carboxyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01151"
SQ   SEQUENCE   525 AA;  57274 MW;  5F5FF331894AB3DC CRC64;
     MSNPVQSDKD RVVIFDTTLR DGEQCPGATM TFEEKLNIAA MLDDMGVDII EAGFPIASDG
     DFEAVNEIAK RSKNAVICGL SRAGAKDIDR CAEAIRPAKR GRIHTFLSTS PVHMKYKLQM
     DPQQVFELVI SSVTRARNHT DDVEWSSEDG TRTEFDFLCR CVEAAIKAGA STINIPDTVG
     YAVPEEYYDL FKRVRETVPN SDKAVFSVHC HNDLGMAVAN SMAGVRAGAR QIECTINGIG
     ERAGNAALEE VVMAMRVRND KLPFWNKIDT TQLTHASKVV SAATSFPVQY NKAIVGRNAF
     AHESGIHQDG MLKNAQTYEI MLPETVGVKQ TSLVMGKHSG RHAFIHKLEE MGHKLSSNQV
     EDAFVRFKAL ADRKKQIYDE DIEALIDEGM VSAHDRIKLL SLSVIAGTRG PQRATMKLDI
     DGVTRIEESE GNGPVDAVFN CIKSLVPHEA KLELYQVHAV TEGTDAQAEV SVRLSQDGRS
     MTARAADPDT LVASAKAYLG ALNKLVMKRQ RDVAPGHGAS AAAAS