ID   LEU1_NOCFA              Reviewed;         580 AA.
AC   Q5YVA5;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=2-isopropylmalate synthase {ECO:0000255|HAMAP-Rule:MF_00572};
DE            EC=2.3.3.13 {ECO:0000255|HAMAP-Rule:MF_00572};
DE   AltName: Full=Alpha-IPM synthase {ECO:0000255|HAMAP-Rule:MF_00572};
DE   AltName: Full=Alpha-isopropylmalate synthase {ECO:0000255|HAMAP-Rule:MF_00572};
GN   Name=leuA {ECO:0000255|HAMAP-Rule:MF_00572}; OrderedLocusNames=NFA_30390;
OS   Nocardia farcinica (strain IFM 10152).
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Nocardia.
OX   NCBI_TaxID=247156;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IFM 10152;
RX   PubMed=15466710; DOI=10.1073/pnas.0406410101;
RA   Ishikawa J., Yamashita A., Mikami Y., Hoshino Y., Kurita H., Hotta K.,
RA   Shiba T., Hattori M.;
RT   "The complete genomic sequence of Nocardia farcinica IFM 10152.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:14925-14930(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_00572}.
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_00572};
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_00572}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_00572}.
CC   -!- SIMILARITY: Belongs to the alpha-IPM synthase/homocitrate synthase
CC       family. LeuA type 2 subfamily. {ECO:0000255|HAMAP-Rule:MF_00572}.
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DR   EMBL; AP006618; BAD57886.1; -; Genomic_DNA.
DR   RefSeq; WP_041560172.1; NC_006361.1.
DR   AlphaFoldDB; Q5YVA5; -.
DR   SMR; Q5YVA5; -.
DR   STRING; 247156.NFA_30390; -.
DR   PRIDE; Q5YVA5; -.
DR   EnsemblBacteria; BAD57886; BAD57886; NFA_30390.
DR   GeneID; 61133756; -.
DR   KEGG; nfa:NFA_30390; -.
DR   eggNOG; COG0119; Bacteria.
DR   HOGENOM; CLU_004588_3_2_11; -.
DR   OMA; DQIEYMH; -.
DR   BioCyc; NFAR247156:NFA_RS15175-MON; -.
DR   UniPathway; UPA00048; UER00070.
DR   Proteomes; UP000006820; 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   CDD; cd07942; DRE_TIM_LeuA; 1.
DR   Gene3D; 3.20.20.70; -; 1.
DR   Gene3D; 3.30.160.270; -; 1.
DR   HAMAP; MF_00572; LeuA_type2; 1.
DR   InterPro; IPR002034; AIPM/Hcit_synth_CS.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR005668; IPM_Synthase.
DR   InterPro; IPR036230; LeuA_allosteric_dom_sf.
DR   InterPro; IPR039371; LeuA_N_DRE-TIM.
DR   InterPro; IPR000891; PYR_CT.
DR   Pfam; PF00682; HMGL-like; 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..580
FT                   /note="2-isopropylmalate synthase"
FT                   /id="PRO_0000406878"
FT   DOMAIN          61..334
FT                   /note="Pyruvate carboxyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01151"
FT   REGION          1..37
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   580 AA;  63442 MW;  D99E0B0830F6E309 CRC64;
     MSATAFPTLS TPAGEIPATA PAWNRQRRSQ MPSHRYRDVH SRVAVPLTDR QWPTRRLTEA
     PLWVPVDLRD GNQALAEPMD PARKRRFFEL LVAMGYKEIE VGYPSASQTD FDFVRLLADT
     DLAPDDVTVV VFTPARRDLI ERTVESIRGI TNPVVVHMYT ATAPTWREVV LGHDRAALRA
     LILDGGREVL RCAGDLPTVR FEFSPEVFNL TEPDFVLEIC DAMTELWQAT PQRPVILNLP
     ATVEVATPNV YADQIEYMHR NLARRDSVIL SVHPHNDRGT GIACAELAVL AGAQRVEGCV
     FGNGERTGNV DIATLALNLH AQGVDPMIDF SDIDEIRRTV EYCNRVEIHA RHPYVGDLVH
     TAFSGTHQDA IKKGLAEHRA RAAARGVPER EIDWRVPYLP IDPADIGRSY DAVIRVNSQS
     GKGGIAYLLE SEYGTVLPRR LQIDFARHVQ QHTDDTGREV TAAELWSLFS AVYLREGEAD
     APQADLGNRL GIDGVVASGA SAAELGAALR RHGVELEVLA VHHTTVTGEL LALVEYRDGA
     GVRWSAGRGR TAGEAVGNAV AAAVGPATAP ARAVAEVRPG