ID   LEU1_PSEU2              Reviewed;         556 AA.
AC   Q4ZX14;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2005, sequence version 1.
DT   25-MAY-2022, entry version 93.
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=Psyr_1257;
OS   Pseudomonas syringae pv. syringae (strain B728a).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas; Pseudomonas syringae.
OX   NCBI_TaxID=205918;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B728a;
RX   PubMed=16043691; DOI=10.1073/pnas.0504930102;
RA   Feil H., Feil W.S., Chain P., Larimer F., Dibartolo G., Copeland A.,
RA   Lykidis A., Trong S., Nolan M., Goltsman E., Thiel J., Malfatti S.,
RA   Loper J.E., Lapidus A., Detter J.C., Land M., Richardson P.M.,
RA   Kyrpides N.C., Ivanova N., Lindow S.E.;
RT   "Comparison of the complete genome sequences of Pseudomonas syringae pv.
RT   syringae B728a and pv. tomato DC3000.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:11064-11069(2005).
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; CP000075; AAY36308.1; -; Genomic_DNA.
DR   RefSeq; WP_004406457.1; NC_007005.1.
DR   RefSeq; YP_234346.1; NC_007005.1.
DR   AlphaFoldDB; Q4ZX14; -.
DR   SMR; Q4ZX14; -.
DR   STRING; 205918.Psyr_1257; -.
DR   EnsemblBacteria; AAY36308; AAY36308; Psyr_1257.
DR   KEGG; psb:Psyr_1257; -.
DR   PATRIC; fig|205918.7.peg.1289; -.
DR   eggNOG; COG0119; Bacteria.
DR   HOGENOM; CLU_004588_3_0_6; -.
DR   OMA; WPDKVID; -.
DR   UniPathway; UPA00048; UER00070.
DR   Proteomes; UP000000426; 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_1000025038"
FT   DOMAIN          33..307
FT                   /note="Pyruvate carboxyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01151"
SQ   SEQUENCE   556 AA;  61508 MW;  55FC3A752EC0DE6E CRC64;
     MTMLKDPSKK YRAFPTIDLP DRTWPSKTID AVPIWCSSDL RDGNQSLIEP MDAAKKLRFW
     KTLVSVGVKE IEASFPSASQ TDFDFVRTLI EDGHIPDDTT IQVLTQARED LIARTFESLR
     GAKKAIVHLY NATCPSFRRI VFNQDKAGVK EIAVNAAKLF VKYAAQQPET QWTFQYSPET
     FSATELEFAK EVCDAVIEVW NPTPENKVIL NLPATVEVAT PNIYADQIEW FGRNITRRDS
     VLISLHTHND RGTGVAATEL GLMAGADRVE GCLFGNGERT GNVDLVTVAL NLYTQGINPG
     LDFSDIDGVR KVVEECNQIP VHPRHPYVGD LVHTAFSGSH QDAIRKGFTQ QKEGELWEVP
     YLPIDPADIG RSYEAVIRVN SQSGKGGIAY LLEQEYGISL PRRMQIEFSQ VVQGETDRLG
     LEMTAEQIHS LLRREYLQAN VPYALISHKL QEENGNSSVD AEVHVDGETQ HWRGKGKGAL
     EALVAGLPVA VEIMDYNEHA IGSGTTAKAA AYIELRVNGE RAVHGVGIDE NITTASFRAL
     FSALNRSLSQ TQAKAA