ID   LEU1_SALRM              Reviewed;         546 AA.
AC   D5HB86;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   15-JUN-2010, sequence version 1.
DT   25-MAY-2022, entry version 63.
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=SRM_02370;
OS   Salinibacter ruber (strain M8).
OC   Bacteria; Bacteroidetes; Bacteroidetes Order II. Incertae sedis;
OC   Rhodothermaceae; Salinibacter.
OX   NCBI_TaxID=761659;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M8;
RG   Genoscope;
RT   "Genome sequence of Salinibacter ruber M8.";
RL   Submitted (APR-2010) 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; FP565814; CBH25291.1; -; Genomic_DNA.
DR   RefSeq; WP_011404875.1; NC_014032.1.
DR   AlphaFoldDB; D5HB86; -.
DR   SMR; D5HB86; -.
DR   EnsemblBacteria; CBH25291; CBH25291; SRM_02370.
DR   KEGG; srm:SRM_02370; -.
DR   PATRIC; fig|761659.10.peg.2580; -.
DR   HOGENOM; CLU_022158_0_1_10; -.
DR   OMA; NTMRMLV; -.
DR   OrthoDB; 840579at2; -.
DR   UniPathway; UPA00048; UER00070.
DR   Proteomes; UP000000933; 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; Transferase.
FT   CHAIN           1..546
FT                   /note="2-isopropylmalate synthase"
FT                   /id="PRO_0000406898"
FT   DOMAIN          5..274
FT                   /note="Pyruvate carboxyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01151"
SQ   SEQUENCE   546 AA;  58464 MW;  D4F8389A6B644ABF CRC64;
     MSDSITIFDT TLRDGEQAPG ASMTVPEKVH IAHKLADLNV DVIEAGFPIS SPAQTEAVTR
     IATEVDGPVT CALARTKEDD IDAAGEALAD GTDTRLHTFI ATSDVHIEAK FDKLGNTMAE
     KREAIIQRAV RAIEQALTYT DNVEFSAEDA GRTDPEFLCE VVQAAAEAGA TTINIPDTTG
     YCAPSEYTDL LETVVDCLPD PDAVTLSTHC HDDLGLATAN TLAGIRAGAR QVECTINGIG
     ERAGNAALEE IVMALTVRAD AFDVTADVHT EHLTPTSQTV SAATGFPVQP NKAIVGSNAF
     SHEAGIHQHG VLEERTTYEI MSATDVGQDA EQIRLGRHSG RHGLFNRLEA MGYAVPEGHR
     DALYDRFLDL ADRKKEVFEE DLEQMMNDFG GDAVAAATGL PDNGVALNGG TPAYRLDQFS
     VHLSSDDEAK VSVRLQRDDG SAREEQATGE GPVDALYRAL DHAVDAPHTL VDYSIRSISE
     GADAQGEVEV TIRYGENQFA GTARNTDVIR ASAEAYVDAL NRLVAAQEHA ESVEFVQNGI
     MHTYGE