ID   LEU1_XANOP              Reviewed;         491 AA.
AC   B2SNG9;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 1.
DT   25-MAY-2022, entry version 76.
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; OrderedLocusNames=PXO_02609;
OS   Xanthomonas oryzae pv. oryzae (strain PXO99A).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=360094;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PXO99A;
RX   PubMed=18452608; DOI=10.1186/1471-2164-9-204;
RA   Salzberg S.L., Sommer D.D., Schatz M.C., Phillippy A.M., Rabinowicz P.D.,
RA   Tsuge S., Furutani A., Ochiai H., Delcher A.L., Kelley D., Madupu R.,
RA   Puiu D., Radune D., Shumway M., Trapnell C., Aparna G., Jha G., Pandey A.,
RA   Patil P.B., Ishihara H., Meyer D.F., Szurek B., Verdier V., Koebnik R.,
RA   Dow J.M., Ryan R.P., Hirata H., Tsuyumu S., Won Lee S., Seo Y.-S.,
RA   Sriariyanum M., Ronald P.C., Sonti R.V., Van Sluys M.-A., Leach J.E.,
RA   White F.F., Bogdanove A.J.;
RT   "Genome sequence and rapid evolution of the rice pathogen Xanthomonas
RT   oryzae pv. oryzae PXO99A.";
RL   BMC Genomics 9:204-204(2008).
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; CP000967; ACD60891.1; -; Genomic_DNA.
DR   AlphaFoldDB; B2SNG9; -.
DR   SMR; B2SNG9; -.
DR   STRING; 360094.PXO_02609; -.
DR   EnsemblBacteria; ACD60891; ACD60891; PXO_02609.
DR   KEGG; xop:PXO_02609; -.
DR   eggNOG; COG0119; Bacteria.
DR   HOGENOM; CLU_022158_0_1_6; -.
DR   OMA; NTMRMLV; -.
DR   UniPathway; UPA00048; UER00070.
DR   Proteomes; UP000001740; Chromosome.
DR   GO; GO:0003852; F:2-isopropylmalate synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009098; P:leucine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.20.20.70; -; 1.
DR   Gene3D; 3.30.160.270; -; 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; 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..491
FT                   /note="2-isopropylmalate synthase"
FT                   /id="PRO_0000406901"
FT   DOMAIN          1..245
FT                   /note="Pyruvate carboxyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01151"
SQ   SEQUENCE   491 AA;  53169 MW;  56D7083ECB31375D CRC64;
     MTPQQKLVMA RALDELGVDI IETGFPASSH SDREAVAMMG RELRRPTLAV LSRCLQADIE
     TSAKALETAA NPRLHVFLST SPLHREHKLR MSREQVLESV HRHVTLARGY IDDVEFSAED
     ATRTEEDFLA EVTRVAVAAG ATTINLPDTV GFTTPEEIRG MFSRLIASVE GADKVIFSAH
     CHNDLGLAVA NSLAAIEGGA RQVECTINGI GERAGNCALE EITMALKVRG AFYNIDSAIN
     TPRIVSTSQL LQRLVGMPVQ RNKAVVGGNA FAHESGIHQH GMLRHRGTYE IMRPEDVGWE
     SSQMVLGRHS GRAAVERRLR ALGYLLEEEE VKLMFEQFKA LCEKQRLVTD ADLQALMQDA
     TVQEGYRLAS MTISDVGSRA NALVELSDPE GNRVAETAQG NGPVDALFGA LASATGVKLE
     LDSYQVHSVG IGADARGEAS LSVRHDGVEY EGTGTSKDII EASALAWLDV ANRLLRQRER
     GVIAGKTAAV A