ID   LEU1_CAUVN              Reviewed;         524 AA.
AC   B8H607;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 79.
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=CCNA_01610;
OS   Caulobacter vibrioides (strain NA1000 / CB15N) (Caulobacter crescentus).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales;
OC   Caulobacteraceae; Caulobacter.
OX   NCBI_TaxID=565050;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NA1000 / CB15N;
RX   PubMed=20472802; DOI=10.1128/jb.00255-10;
RA   Marks M.E., Castro-Rojas C.M., Teiling C., Du L., Kapatral V.,
RA   Walunas T.L., Crosson S.;
RT   "The genetic basis of laboratory adaptation in Caulobacter crescentus.";
RL   J. Bacteriol. 192:3678-3688(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; CP001340; ACL95075.1; -; Genomic_DNA.
DR   RefSeq; WP_010919415.1; NC_011916.1.
DR   RefSeq; YP_002516983.1; NC_011916.1.
DR   AlphaFoldDB; B8H607; -.
DR   SMR; B8H607; -.
DR   PRIDE; B8H607; -.
DR   EnsemblBacteria; ACL95075; ACL95075; CCNA_01610.
DR   GeneID; 7331588; -.
DR   KEGG; ccs:CCNA_01610; -.
DR   PATRIC; fig|565050.3.peg.1588; -.
DR   HOGENOM; CLU_022158_0_1_5; -.
DR   OMA; NTMRMLV; -.
DR   OrthoDB; 840579at2; -.
DR   PhylomeDB; B8H607; -.
DR   UniPathway; UPA00048; UER00070.
DR   Proteomes; UP000001364; 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; 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..524
FT                   /note="2-isopropylmalate synthase"
FT                   /id="PRO_1000149166"
FT   DOMAIN          15..275
FT                   /note="Pyruvate carboxyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01151"
SQ   SEQUENCE   524 AA;  55990 MW;  F8DBEA6B2AAD8B57 CRC64;
     MTSVPAGAIS KRDNVVVFDT TMRDGEQSPG ASMSLEEKLE LAKILEEMGV DVIEAGFPIA
     SNGDFEAVRQ IAELITESTV CGLARAAAGD IDRCAEAVRR AKRGRIHTFI STSPVHMKYK
     LQMEPDAVLE AITRSVSHAR NLVGDVEWSA EDATRTERDF LKRCVEAAIK AGATTINLPD
     TVGYSYPSEY GELFRDVITS VPGADKAIFS AHCHNDLGLA VANSIAAIEG GARQVEVAIN
     GIGERAGNAA LEEIVMALRV RGDHLPYGTS VDPVHITRAS RYVSAITGFP VQFNKAIVGK
     NAFAHESGIH QDGMLKNAET YEIMKPEDVG QGATNLVMGK HSGRHAFREK LKALGYELGQ
     NALNDAFGRF KELADKKKHV FDDDIVALVD DALARGSEKI RVSRLRVVAG TDGQSAELTL
     DIDGVASTAE ATGDGPVDAV FNAIHKIVPH SAALRLFQVH AVTEGTDAQA QVSVRLEEDG
     RIATGAAADT DTLTASAKAY VNALNNLFAR KEKSRPEAAI ASGF