ID   LEU1_MICAE              Reviewed;         533 AA.
AC   P94907;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   25-MAY-2022, entry version 81.
DE   RecName: Full=2-isopropylmalate synthase;
DE            EC=2.3.3.13;
DE   AltName: Full=Alpha-IPM synthase;
DE   AltName: Full=Alpha-isopropylmalate synthase;
GN   Name=leuA;
OS   Microcystis aeruginosa.
OC   Bacteria; Cyanobacteria; Oscillatoriophycideae; Chroococcales;
OC   Microcystaceae; Microcystis.
OX   NCBI_TaxID=1126;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=K-81;
RX   PubMed=9003451; DOI=10.1016/s0167-4781(96)00191-1;
RA   Asayama M., Kabasawa M., Shirai M.;
RT   "A novel genetic organization: the leuA-rpoD1 locus in the cyanobacterium
RT   Microcystis aeruginosa K-81.";
RL   Biochim. Biophys. Acta 1350:15-20(1997).
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 1 subfamily. {ECO:0000305}.
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DR   EMBL; D85684; BAA12849.1; -; Genomic_DNA.
DR   AlphaFoldDB; P94907; -.
DR   SMR; P94907; -.
DR   UniPathway; UPA00048; UER00070.
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; Transferase.
FT   CHAIN           1..533
FT                   /note="2-isopropylmalate synthase"
FT                   /id="PRO_0000140362"
FT   DOMAIN          8..270
FT                   /note="Pyruvate carboxyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01151"
SQ   SEQUENCE   533 AA;  57989 MW;  16E69B5431803C8D CRC64;
     MNTSPDRVII FDTTLRDGEQ SPGAALNVDE KLTIARALAR LGVDVIEAGF PHASPGDFEA
     VQKIAGSVGS EADSPIICGL ARATQKDIKS AADALRPAAK PRIHTFLATS DIHLQYKLKK
     TRQEVLEIVP EMVAYAKSFL NDVEFSPEDA GRSDPEFLYQ VLERAIAAGA TTVNIPDTVG
     YTTPSEFGAL IRGIKENVPN IDQAIISVHG HDDLGLAVAN FLEAVKNGAR QLECTINGIG
     ERAGNASLEE LVMALHVRRS YFNPFLGRPA ESTEPLTKIN TKEIYRTSRL VSNLTGMIVQ
     PNKAIVGANA FAHESGIHQD GVLKHKLTYE IMDAESIGLT NNQIVLGKLS GRNAFRSRLQ
     ELGFELSETE LNNAFIQFKE MADRKKEITD RDLEAIVNDE IDTVPDHFRL ELVQVSCGNN
     ARPTATVTIR TPDGSELSDA AIGTGPVDAL CKAIDRVVQI PNELISFSVR EVTEGIDALG
     EVTIRLRYAG RTYSARAADT DIIVASARAY VSALNRLHVA LQQKEKTPEM LQV