ID   LEU1_STRG3              Reviewed;         520 AA.
AC   D3HCJ2;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   23-MAR-2010, sequence version 1.
DT   03-AUG-2022, entry version 60.
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=GALLO_0758;
OS   Streptococcus gallolyticus (strain UCN34).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=637909;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCN34;
RX   PubMed=20139183; DOI=10.1128/jb.01659-09;
RA   Rusniok C., Couve E., Da Cunha V., El Gana R., Zidane N., Bouchier C.,
RA   Poyart C., Leclercq R., Trieu-Cuot P., Glaser P.;
RT   "Genome sequence of Streptococcus gallolyticus: insights into its
RT   adaptation to the bovine rumen and its ability to cause endocarditis.";
RL   J. Bacteriol. 192:2266-2276(2010).
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; FN597254; CBI13250.1; -; Genomic_DNA.
DR   RefSeq; WP_012961740.1; NC_013798.1.
DR   AlphaFoldDB; D3HCJ2; -.
DR   SMR; D3HCJ2; -.
DR   PRIDE; D3HCJ2; -.
DR   KEGG; sga:GALLO_0758; -.
DR   HOGENOM; CLU_022158_0_1_9; -.
DR   OMA; NTMRMLV; -.
DR   UniPathway; UPA00048; UER00070.
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..520
FT                   /note="2-isopropylmalate synthase"
FT                   /id="PRO_0000406900"
FT   DOMAIN          4..266
FT                   /note="Pyruvate carboxyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01151"
SQ   SEQUENCE   520 AA;  56573 MW;  1DD9881CFE9027C4 CRC64;
     MRKVEFLDTT LRDGEQTPGV NFSIKEKVAI AKQLEKWGIA SIEAGFPAAS PDSFEAVRQI
     SAAMTTTAVS GLARSVKSDI DACYEALKDA KYPQCHVFIA TSPIHREYKL KKTKEEILDI
     IKEHVTYARS KFDVVEFSPE DATRTELDYL LQVVQTAVDA GATYINIPDT VGFTTPEEYG
     NIFKYLIENT KSDREIIFSP HCHDDLGMAT ANTLAAIKNG AGRVEGTVNG IGERAGNVAL
     EEIAVALNIR EDYYQATSDI VLNETVNTSE LISRFSGISI PKNKAVVGGN AFSHESGIHQ
     DGVLKNPLTY EIITPELVGV KHNSLPLGKL SGRHAFVEKL KELELAFEES EIATLFGKFK
     KLADKKHEIT DADIRALVAG TEIENPEGFH FGDLKLTSNA DDTVTAEVLM VNADGEEVEV
     IANGKGSVEA IYNAVDKFFN QTVRLLSYTM DAVTDGIDSQ ARVSVSIENV DTGTIFNASG
     IDFDVLKAGA IAYVNANAFV QKENAGEIGK AVSFRDVPTN