ID   LEU1_ACIFD              Reviewed;         516 AA.
AC   C7M0E4;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   13-OCT-2009, sequence version 1.
DT   25-MAY-2022, entry version 71.
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=Afer_1529;
OS   Acidimicrobium ferrooxidans (strain DSM 10331 / JCM 15462 / NBRC 103882 /
OS   ICP).
OC   Bacteria; Actinobacteria; Acidimicrobiia; Acidimicrobiales;
OC   Acidimicrobiaceae; Acidimicrobium.
OX   NCBI_TaxID=525909;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 10331 / JCM 15462 / NBRC 103882 / ICP;
RX   PubMed=21304635; DOI=10.4056/sigs.1463;
RA   Clum A., Nolan M., Lang E., Glavina Del Rio T., Tice H., Copeland A.,
RA   Cheng J.F., Lucas S., Chen F., Bruce D., Goodwin L., Pitluck S.,
RA   Ivanova N., Mavrommatis K., Mikhailova N., Pati A., Chen A.,
RA   Palaniappan K., Goker M., Spring S., Land M., Hauser L., Chang Y.J.,
RA   Jeffries C.C., Chain P., Bristow J., Eisen J.A., Markowitz V.,
RA   Hugenholtz P., Kyrpides N.C., Klenk H.P., Lapidus A.;
RT   "Complete genome sequence of Acidimicrobium ferrooxidans type strain
RT   (ICP).";
RL   Stand. Genomic Sci. 1:38-45(2009).
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; CP001631; ACU54452.1; -; Genomic_DNA.
DR   AlphaFoldDB; C7M0E4; -.
DR   SMR; C7M0E4; -.
DR   STRING; 525909.Afer_1529; -.
DR   EnsemblBacteria; ACU54452; ACU54452; Afer_1529.
DR   KEGG; afo:Afer_1529; -.
DR   eggNOG; COG0119; Bacteria.
DR   HOGENOM; CLU_022158_0_1_11; -.
DR   OMA; SNMFAHE; -.
DR   UniPathway; UPA00048; UER00070.
DR   Proteomes; UP000000771; 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..516
FT                   /note="2-isopropylmalate synthase"
FT                   /id="PRO_0000406892"
FT   DOMAIN          10..271
FT                   /note="Pyruvate carboxyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01151"
SQ   SEQUENCE   516 AA;  55125 MW;  FB52F6D0F5A26BC6 CRC64;
     MDEVGTQERI RIFDTTLRDG EQAPGISLDP LEKLEIAEQL ARLGVDIIEA GFPVASQGDF
     DAVRQIARQV HGPVICGLSR THVADIERCY EAVRDAEHHR IHVFISTSPS HLEHMLRMSE
     DQVVEAVRRA IARARELVDD VEFSPQDATR TPLPFLYRVL QVAVDEGAST LNIPDTVGYG
     IPWDFARMVE SVRREVAGSY VISCHCHNDL GLATANSLAA VAAGARQVEC CINGIGERAG
     NAALEEVVMG LAIRSDVIGD VTTGIDTREL ARTSRLVSRL TGYPVQYNKA VVGRNAFAHE
     SGIHQHGVLT DRSTYEVIDA ASVGQEAAQI VLGKHSGRHA FQEALARMGI ALEGDALNAT
     FQRFKELADR KVELSEADLE AIVAEELGTT LADRFELVSF RVEAGTGREA VASATVLVDG
     TPVEASASGN GMVDALGRVL AEATALEARL TGFSVTSVTG GADALGSVAV TVDVGGHEVS
     GRGVSTDIVE ASARALLNAL NRAARVREKA SNRETP