ID   LEU1_SYNPW              Reviewed;         540 AA.
AC   A5GM47;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 1.
DT   25-MAY-2022, entry version 80.
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};
GN   OrderedLocusNames=SynWH7803_1586;
OS   Synechococcus sp. (strain WH7803).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC   unclassified Synechococcus.
OX   NCBI_TaxID=32051;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WH7803;
RG   Genoscope;
RL   Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
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; CT971583; CAK24012.1; -; Genomic_DNA.
DR   RefSeq; WP_011933489.1; NC_009481.1.
DR   AlphaFoldDB; A5GM47; -.
DR   SMR; A5GM47; -.
DR   STRING; 32051.SynWH7803_1586; -.
DR   EnsemblBacteria; CAK24012; CAK24012; SynWH7803_1586.
DR   KEGG; syx:SynWH7803_1586; -.
DR   eggNOG; COG0119; Bacteria.
DR   HOGENOM; CLU_022158_0_1_3; -.
DR   OMA; NTMRMLV; -.
DR   OrthoDB; 840579at2; -.
DR   UniPathway; UPA00048; UER00070.
DR   Proteomes; UP000001566; 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..540
FT                   /note="2-isopropylmalate synthase"
FT                   /id="PRO_1000149314"
FT   DOMAIN          8..269
FT                   /note="Pyruvate carboxyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01151"
SQ   SEQUENCE   540 AA;  57925 MW;  8DBE07D553E61739 CRC64;
     MAHDPGRVLI FDTTLRDGEQ SPGASLNLEE KLAIAQQLAR LGVDVIEAGF PFASPGDFNA
     VQRIAQQVGG EQGPIICGLA RASRGDIKAC ADAVAPAPRR RIHTFIATSD IHLEHKLRKS
     RQEVLAIVPE MVAYARSLVD DVEFSCEDAG RSDPEFLYAV IEAAINAGAS TINIPDTVGY
     TTPAEFGALI AGIDQHVPNI SEAVLSVHGH NDLGLAVANF LEAVKNGARQ LECTINGIGE
     RAGNAALEEL VMALHVRRRY FNPFFGRAED SPTPLTGVRT EEITKTSRLV SNLTGMVVQP
     NKAIVGANAF AHESGIHQDG VLKNRLTYEI VDARTVGLTD NRISLGKLSG RSAVRARLEE
     LGYDLSREDL DDAFARFKEL ADRKRDITDR DLEAIVSEQV QQPDARYQLK LVQVSCGSSL
     QPTATVTLLD EEGQEQSEAA IGTGPVDAVC RALNALAGEP NELVEFSVKS VTEGIDAMGE
     VTIRLRRDGQ LFSGHAADTD VVVAAAQAFV NALNRLVAGS LNPTLHPQRD ATPLDASPTL