ID   LEU1_GEOS4              Reviewed;         518 AA.
AC   D3EBC1;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   23-MAR-2010, sequence version 1.
DT   25-MAY-2022, entry version 65.
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=GYMC10_4749;
OS   Geobacillus sp. (strain Y412MC10).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=481743;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Y412MC10;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Saunders E., Brettin T., Detter J.C.,
RA   Han C., Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G.,
RA   Brumm P., Mead D.;
RT   "Complete sequence of Geobacillus sp. Y412MC10.";
RL   Submitted (OCT-2009) 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_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; CP001793; ACX66967.1; -; Genomic_DNA.
DR   RefSeq; WP_015736822.1; NC_013406.1.
DR   AlphaFoldDB; D3EBC1; -.
DR   SMR; D3EBC1; -.
DR   STRING; 481743.GYMC10_4749; -.
DR   PRIDE; D3EBC1; -.
DR   EnsemblBacteria; ACX66967; ACX66967; GYMC10_4749.
DR   KEGG; gym:GYMC10_4749; -.
DR   HOGENOM; CLU_022158_0_1_9; -.
DR   OMA; GVYEEGH; -.
DR   OrthoDB; 840579at2; -.
DR   UniPathway; UPA00048; UER00070.
DR   Proteomes; UP000002381; 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   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; Reference proteome; Transferase.
FT   CHAIN           1..518
FT                   /note="2-isopropylmalate synthase"
FT                   /id="PRO_0000406895"
FT   DOMAIN          5..269
FT                   /note="Pyruvate carboxyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01151"
SQ   SEQUENCE   518 AA;  56944 MW;  389D58EE173F8DF1 CRC64;
     MERNIIVLDT TLRDGEQVPG AKLNVQQKIE FAQQLKRLNV DIIEAGFPAS SAGDFQAVQE
     IARTVGDSVS ITALARAVKG DIDAVYESIK LAQNPLIHIV LGTSNIHVEK KFNRSKDAVL
     QMGVDAVKYA KTLLPQVQYS TEDASRSDFE YLWKTIEAVV KAGATMINVP DTVGYAVPDE
     FGELIRKINE RLKNLNDQVI LSVHCHNDLG LATANTLSAV RNGAEKVECT INGLGERAGN
     TSLEEVVMGL KVRENHFKAS TNVRLKELIR TSRLLTHLTG LDVQVNKAIT GENAFAHSSG
     IHQDGLLKDK QVYEIMSPEE VGADSMELIL TARSGRHAFK NAVEKLGFET GEGDDFEALF
     EKFLLLADAK KEVYDHDVFY LVTQHRTHEE VSSHLYELDS FQVVTNDMYP TATVKLKKGS
     ETFRDSMVGD GPIDALYSAI KALVGLDVQL KDYKINSLSR GKEAIGRVNI RIEYQGKIYS
     GRAMDTDIIK ASALAFLNGI NAVLLDAGHD SQAPVSAR