ID   LEU1_LISMF              Reviewed;         512 AA.
AC   Q71Y35;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 94.
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=LMOf2365_2010;
OS   Listeria monocytogenes serotype 4b (strain F2365).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=265669;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F2365;
RX   PubMed=15115801; DOI=10.1093/nar/gkh562;
RA   Nelson K.E., Fouts D.E., Mongodin E.F., Ravel J., DeBoy R.T., Kolonay J.F.,
RA   Rasko D.A., Angiuoli S.V., Gill S.R., Paulsen I.T., Peterson J.D.,
RA   White O., Nelson W.C., Nierman W.C., Beanan M.J., Brinkac L.M.,
RA   Daugherty S.C., Dodson R.J., Durkin A.S., Madupu R., Haft D.H.,
RA   Selengut J., Van Aken S.E., Khouri H.M., Fedorova N., Forberger H.A.,
RA   Tran B., Kathariou S., Wonderling L.D., Uhlich G.A., Bayles D.O.,
RA   Luchansky J.B., Fraser C.M.;
RT   "Whole genome comparisons of serotype 4b and 1/2a strains of the food-borne
RT   pathogen Listeria monocytogenes reveal new insights into the core genome
RT   components of this species.";
RL   Nucleic Acids Res. 32:2386-2395(2004).
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; AE017262; AAT04780.1; -; Genomic_DNA.
DR   RefSeq; WP_003725876.1; NC_002973.6.
DR   PDB; 3EWB; X-ray; 2.10 A; X=2-283.
DR   PDBsum; 3EWB; -.
DR   AlphaFoldDB; Q71Y35; -.
DR   SMR; Q71Y35; -.
DR   KEGG; lmf:LMOf2365_2010; -.
DR   HOGENOM; CLU_022158_0_1_9; -.
DR   OMA; NTMRMLV; -.
DR   UniPathway; UPA00048; UER00070.
DR   EvolutionaryTrace; Q71Y35; -.
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   1: Evidence at protein level;
KW   3D-structure; Amino-acid biosynthesis;
KW   Branched-chain amino acid biosynthesis; Leucine biosynthesis; Transferase.
FT   CHAIN           1..512
FT                   /note="2-isopropylmalate synthase"
FT                   /id="PRO_0000140360"
FT   DOMAIN          4..266
FT                   /note="Pyruvate carboxyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01151"
FT   STRAND          2..8
FT                   /evidence="ECO:0007829|PDB:3EWB"
FT   TURN            10..12
FT                   /evidence="ECO:0007829|PDB:3EWB"
FT   HELIX           24..37
FT                   /evidence="ECO:0007829|PDB:3EWB"
FT   STRAND          40..45
FT                   /evidence="ECO:0007829|PDB:3EWB"
FT   HELIX           47..49
FT                   /evidence="ECO:0007829|PDB:3EWB"
FT   HELIX           51..63
FT                   /evidence="ECO:0007829|PDB:3EWB"
FT   STRAND          66..76
FT                   /evidence="ECO:0007829|PDB:3EWB"
FT   HELIX           77..87
FT                   /evidence="ECO:0007829|PDB:3EWB"
FT   STRAND          91..100
FT                   /evidence="ECO:0007829|PDB:3EWB"
FT   HELIX           103..108
FT                   /evidence="ECO:0007829|PDB:3EWB"
FT   HELIX           114..129
FT                   /evidence="ECO:0007829|PDB:3EWB"
FT   STRAND          135..140
FT                   /evidence="ECO:0007829|PDB:3EWB"
FT   HELIX           142..144
FT                   /evidence="ECO:0007829|PDB:3EWB"
FT   HELIX           147..159
FT                   /evidence="ECO:0007829|PDB:3EWB"
FT   STRAND          164..168
FT                   /evidence="ECO:0007829|PDB:3EWB"
FT   STRAND          170..172
FT                   /evidence="ECO:0007829|PDB:3EWB"
FT   HELIX           176..189
FT                   /evidence="ECO:0007829|PDB:3EWB"
FT   HELIX           193..195
FT                   /evidence="ECO:0007829|PDB:3EWB"
FT   STRAND          196..201
FT                   /evidence="ECO:0007829|PDB:3EWB"
FT   HELIX           209..218
FT                   /evidence="ECO:0007829|PDB:3EWB"
FT   STRAND          223..227
FT                   /evidence="ECO:0007829|PDB:3EWB"
FT   HELIX           228..230
FT                   /evidence="ECO:0007829|PDB:3EWB"
FT   TURN            233..235
FT                   /evidence="ECO:0007829|PDB:3EWB"
FT   HELIX           240..249
FT                   /evidence="ECO:0007829|PDB:3EWB"
FT   HELIX           251..254
FT                   /evidence="ECO:0007829|PDB:3EWB"
FT   STRAND          256..258
FT                   /evidence="ECO:0007829|PDB:3EWB"
FT   HELIX           262..264
FT                   /evidence="ECO:0007829|PDB:3EWB"
FT   HELIX           265..274
FT                   /evidence="ECO:0007829|PDB:3EWB"
SQ   SEQUENCE   512 AA;  56064 MW;  475D88C6E46318FF CRC64;
     MKKIQFFDTT LRDGEQTPGV NFDVKEKIQI ALQLEKLGID VIEAGFPISS PGDFECVKAI
     AKAIKHCSVT GLARCVEGDI DRAEEALKDA VSPQIHIFLA TSDVHMEYKL KMSRAEVLAS
     IKHHISYARQ KFDVVQFSPE DATRSDRAFL IEAVQTAIDA GATVINIPDT VGYTNPTEFG
     QLFQDLRREI KQFDDIIFAS HCHDDLGMAT ANALAAIENG ARRVEGTING IGERAGNTAL
     EEVAVALHIR KDFYQAETNI VLNQFKNSSD LISRLSGMPV PRNKAVIGGN AYAHESGIHQ
     DGVLKNPDTY EIITPALVGV DKNSLPLGKL SGKHAFNTRM EEMGYTLTEQ EQKDAFKRFK
     QLADAKKEVT EEDLHALILG QSSESADDFE LKHLQVQYVT GGVQGAIVRI EERDGALVED
     AATGSGSIEA IYNTINRLMK QDIELTDYRI QAITAGQDAQ AEVHVVIKND KGAVFHGIGI
     DFDVLTASAK AYLQASGKSK TASKQADFEE VK