ID   LEU1_MICAN              Reviewed;         533 AA.
AC   B0JGK2;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   18-MAR-2008, sequence version 1.
DT   03-AUG-2022, entry version 85.
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=MAE_54460;
OS   Microcystis aeruginosa (strain NIES-843 / IAM M-2473).
OC   Bacteria; Cyanobacteria; Oscillatoriophycideae; Chroococcales;
OC   Microcystaceae; Microcystis.
OX   NCBI_TaxID=449447;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIES-843 / IAM M-247;
RX   PubMed=18192279; DOI=10.1093/dnares/dsm026;
RA   Kaneko T., Nakajima N., Okamoto S., Suzuki I., Tanabe Y., Tamaoki M.,
RA   Nakamura Y., Kasai F., Watanabe A., Kawashima K., Kishida Y., Ono A.,
RA   Shimizu Y., Takahashi C., Minami C., Fujishiro T., Kohara M., Katoh M.,
RA   Nakazaki N., Nakayama S., Yamada M., Tabata S., Watanabe M.M.;
RT   "Complete genomic structure of the bloom-forming toxic cyanobacterium
RT   Microcystis aeruginosa NIES-843.";
RL   DNA Res. 14:247-256(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; AP009552; BAG05268.1; -; Genomic_DNA.
DR   RefSeq; WP_012267775.1; NC_010296.1.
DR   AlphaFoldDB; B0JGK2; -.
DR   SMR; B0JGK2; -.
DR   STRING; 449447.MAE_54460; -.
DR   PaxDb; B0JGK2; -.
DR   EnsemblBacteria; BAG05268; BAG05268; MAE_54460.
DR   KEGG; mar:MAE_54460; -.
DR   PATRIC; fig|449447.4.peg.4965; -.
DR   eggNOG; COG0119; Bacteria.
DR   HOGENOM; CLU_022158_0_1_3; -.
DR   OMA; NTMRMLV; -.
DR   OrthoDB; 840579at2; -.
DR   BioCyc; MAER449447:MAE_RS23655-MON; -.
DR   UniPathway; UPA00048; UER00070.
DR   Proteomes; UP000001510; 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..533
FT                   /note="2-isopropylmalate synthase"
FT                   /id="PRO_1000149224"
FT   DOMAIN          8..270
FT                   /note="Pyruvate carboxyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01151"
SQ   SEQUENCE   533 AA;  58027 MW;  FE30CDFE6A305EB4 CRC64;
     MNTSPDRVII FDTTLRDGEQ SPGAALNVDE KLTIARALAR LGVDVIEAGF PHASPGDFDA
     VQKIAASVGS EADSPIICGL ARTTQKDIKS AADALRPAAK PRIHTFLATS DIHLQYKLKK
     TRQEVLEIVP EMVAYAKSFV DDVEFSPEDA GRSDPDFLYQ VLERAIAAGA TTVNIPDTVG
     YTTPSEFGAL IRGIKENVPN IDQAIISVHG HDDLGLAVAN FLEAVKNGAR QLECTINGIG
     ERAGNASLEE LVMALHVRRS YFNPFLGRPA ESTEPLTKIN TKEIYRTSRL VSNLTGMIVQ
     PNKAIVGANA FAHESGIHQD GVLKHKLTYE IMDAESIGLT HNQIVLGKLS GRNAFRSRLQ
     ELGFELSETE LNNAFIQFKE MADRKKEITD RDLEAIVNDE IDTVPDHFRL ELVQVSCGNS
     ARPTATVTIR TPDGSELSDA AIGTGPVDAL CKAIDRVVKI PNELISFSVR EVTEGIDALG
     EVTIRLRYEG RTYSAHAADT DIIVASARAY VSALNRLHVA LQQKEKTPEM LQV