ID   LEU1_PSEA7              Reviewed;         556 AA.
AC   A6V0X2;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   03-AUG-2022, entry version 78.
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=PSPA7_1323;
OS   Pseudomonas aeruginosa (strain PA7).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=381754;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PA7;
RA   Dodson R.J., Harkins D., Paulsen I.T.;
RL   Submitted (JUN-2007) 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_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; CP000744; ABR86416.1; -; Genomic_DNA.
DR   RefSeq; WP_012074569.1; NC_009656.1.
DR   AlphaFoldDB; A6V0X2; -.
DR   SMR; A6V0X2; -.
DR   PRIDE; A6V0X2; -.
DR   EnsemblBacteria; ABR86416; ABR86416; PSPA7_1323.
DR   KEGG; pap:PSPA7_1323; -.
DR   HOGENOM; CLU_004588_3_0_6; -.
DR   OMA; DQIEYMH; -.
DR   UniPathway; UPA00048; UER00070.
DR   Proteomes; UP000001582; 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; Transferase.
FT   CHAIN           1..556
FT                   /note="2-isopropylmalate synthase"
FT                   /id="PRO_1000025032"
FT   DOMAIN          33..307
FT                   /note="Pyruvate carboxyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01151"
SQ   SEQUENCE   556 AA;  61829 MW;  EDB899397AD5C1F3 CRC64;
     MSMLKDPSQK YRPFPAINLP DRTWPSKTIT EVPIWCSSDL RDGNQSLIEP MDAAKKMRFF
     KTLVQVGLKQ IEVAFPSASD TDFNFVRELI EGNHIPDDVT IQVLTQARED LITRTFESLR
     GAKKAIVHVY NATAPSFRRI VFNQDKQGVV DIATNAAKLI RKLAAEQPDT QWSFQYSPEI
     FSSTELEFSV EVCNAVIDVW QPTPEHKIIL NLPATVECAT PNVYADQIEW FGRHVNRRDS
     VIISLHTHND RGTGVAATEL GLMAGADRVE GCLFGNGERT GNVDLVTLAL NMYTQGLHPQ
     LDFSDIDAVR KVVEECNQLP VHPRHPYVGD LVHTAFSGSH QDAIRKGFAQ QKEDAIWEVP
     YLPIDPADIG RDYEAVIRVN SQSGKGGITF LLEQEYGISL PRRMQIEFSQ VVQGETDRLG
     LEMTAQQIYS LLENEYLKAT SPYALASHRL QEENGTSAVD LEVTFDGEKQ HWRGIGKGPL
     EALVAALPVK AEIMDYHEHA IGAGANARAA AYIEIRLEGQ RPLHGIGIDE NITTASFRAL
     FSALNRAVTQ AEAKAA