ID   LEU1_ALISL              Reviewed;         515 AA.
AC   B6ELK0;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 1.
DT   25-MAY-2022, entry version 77.
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=VSAL_I0377;
OS   Aliivibrio salmonicida (strain LFI1238) (Vibrio salmonicida (strain
OS   LFI1238)).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Aliivibrio.
OX   NCBI_TaxID=316275;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LFI1238;
RX   PubMed=19099551; DOI=10.1186/1471-2164-9-616;
RA   Hjerde E., Lorentzen M.S., Holden M.T., Seeger K., Paulsen S., Bason N.,
RA   Churcher C., Harris D., Norbertczak H., Quail M.A., Sanders S.,
RA   Thurston S., Parkhill J., Willassen N.P., Thomson N.R.;
RT   "The genome sequence of the fish pathogen Aliivibrio salmonicida strain
RT   LFI1238 shows extensive evidence of gene decay.";
RL   BMC Genomics 9:616-616(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: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; FM178379; CAQ78062.1; -; Genomic_DNA.
DR   RefSeq; WP_012549204.1; NC_011312.1.
DR   AlphaFoldDB; B6ELK0; -.
DR   SMR; B6ELK0; -.
DR   STRING; 316275.VSAL_I0377; -.
DR   EnsemblBacteria; CAQ78062; CAQ78062; VSAL_I0377.
DR   KEGG; vsa:VSAL_I0377; -.
DR   eggNOG; COG0119; Bacteria.
DR   HOGENOM; CLU_022158_0_1_6; -.
DR   OMA; NTMRMLV; -.
DR   OrthoDB; 840579at2; -.
DR   UniPathway; UPA00048; UER00070.
DR   Proteomes; UP000001730; Chromosome 1.
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; Transferase.
FT   CHAIN           1..515
FT                   /note="2-isopropylmalate synthase"
FT                   /id="PRO_1000149120"
FT   DOMAIN          5..267
FT                   /note="Pyruvate carboxyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01151"
SQ   SEQUENCE   515 AA;  56211 MW;  0ED47FE45B66FEC6 CRC64;
     MSDQVIIFDT TLRDGEQALS ASLTVKEKLQ IAFALERLGV DVIEAGFPIS SPGDFESVRT
     IAKHIKNSRI CALSRAVTKD IDVAADALKV AEAFRIHTFI STSTVHVQDK LRRSYDDVVE
     MGVKAVQRAR KYTDDVEFSC EDAGRTPIDN LCRMVEAAIN AGANTINIPD TVGYTIPGEF
     GGIIQTLFNR VPNIDKAIIS VHCHDDLGMS VANSIAAVQA GARQVEGTIN GIGERAGNCS
     LEEIAMILQT RSEYLGVHTS LKNDEIHRTS KLVSQLCNMP IQSNKAIVGA NAFSHSSGIH
     QDGMLKNKNT YEIMTPESIG LKNKALNLTS RSGRAAVKSH MDSMGYKAEE YNLDTLYADF
     VKLADRKGQV FDYDLEALMH FANLRDEDDF YKLNYLSVQS GSVMATTSIK LLCGDEEKCE
     AAVGNGPVDA LYQCIYKLTG YEIVLDKFDL TAKGEGEDGL GQADIIANYK GRKYHGTGLA
     TDIIEASGQA LLHVINSIHR ADQIAEIKQN KITTV