ID   LEU1_AFIC5              Reviewed;         519 AA.
AC   B6JB87; F8BUL6;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 1.
DT   25-MAY-2022, entry version 74.
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=OCAR_5296, OCA5_c26790;
OS   Afipia carboxidovorans (strain ATCC 49405 / DSM 1227 / KCTC 32145 / OM5)
OS   (Oligotropha carboxidovorans).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Bradyrhizobiaceae; Afipia.
OX   NCBI_TaxID=504832;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49405 / DSM 1227 / KCTC 32145 / OM5;
RX   PubMed=18539730; DOI=10.1128/jb.00614-08;
RA   Paul D., Bridges S., Burgess S.C., Dandass Y., Lawrence M.L.;
RT   "Genome sequence of the chemolithoautotrophic bacterium Oligotropha
RT   carboxidovorans OM5T.";
RL   J. Bacteriol. 190:5531-5532(2008).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49405 / DSM 1227 / KCTC 32145 / OM5;
RX   PubMed=21742883; DOI=10.1128/jb.05619-11;
RA   Volland S., Rachinger M., Strittmatter A., Daniel R., Gottschalk G.,
RA   Meyer O.;
RT   "Complete genome sequences of the chemolithoautotrophic Oligotropha
RT   carboxidovorans strains OM4 and OM5.";
RL   J. Bacteriol. 193:5043-5043(2011).
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; CP001196; ACI92428.1; -; Genomic_DNA.
DR   EMBL; CP002826; AEI07373.1; -; Genomic_DNA.
DR   RefSeq; WP_012562457.1; NC_015684.1.
DR   AlphaFoldDB; B6JB87; -.
DR   SMR; B6JB87; -.
DR   STRING; 504832.OCAR_5296; -.
DR   EnsemblBacteria; AEI07373; AEI07373; OCA5_c26790.
DR   KEGG; oca:OCAR_5296; -.
DR   KEGG; ocg:OCA5_c26790; -.
DR   PATRIC; fig|504832.7.peg.2829; -.
DR   eggNOG; COG0119; Bacteria.
DR   HOGENOM; CLU_022158_0_1_5; -.
DR   OMA; NTMRMLV; -.
DR   OrthoDB; 840579at2; -.
DR   UniPathway; UPA00048; UER00070.
DR   Proteomes; UP000007730; 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..519
FT                   /note="2-isopropylmalate synthase"
FT                   /id="PRO_1000149233"
FT   DOMAIN          12..274
FT                   /note="Pyruvate carboxyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01151"
SQ   SEQUENCE   519 AA;  56157 MW;  7879EF4F881AD2FF CRC64;
     MTSPSTSDKD RVVIFDTTLR DGEQCPGATM THEEKLEVAE MLDTMGVDII EAGFPIASVG
     DFEAVAEIAK RANNAVIAGL ARAIPADIVR AGEAVRHAKR GRIHTFVSTS PIHLAHQMRK
     SEEDVLGIIT ATVAQARNLV DDVEWSAMDS TRTPIDYLCR CVETAIAAGA TTINLPDTVG
     YAVPEEYRRM FKVIRERVPN ADKAVFSVHC HDDLGLAVAN SLAGVEGGAR QIECTINGIG
     ERAGNAALEE VVMAIKTRGD VMPYWCNVES TTLTRASKVV SAATSFPVQY NKAIVGRNAF
     AHESGIHQDG VLKNAQTYEI MTPESVGVKQ TSLVMGKHSG RHAFQHKLRE LGYELADNQL
     QDAFVRFKAL ADRKKDIYDE DIEALVDQEL AQTHDRLRLV SLTVIAGTHG PQRATMKVEV
     DGKVRIDEAE GNGPVDAVFN AVKTLVPHEA KLELYQVHAV TAGTDAQAEV SVRLSQDGRS
     VTARSSDPDT LVASAKAYLS ALNKIISRQQ REAPVAAAS