ID   LEU1_OLSUV              Reviewed;         511 AA.
AC   E1QWZ1;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   30-NOV-2010, sequence version 1.
DT   03-AUG-2022, entry version 58.
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=Olsu_1545;
OS   Olsenella uli (strain ATCC 49627 / DSM 7084 / CIP 109912 / JCM 12494 /
OS   NCIMB 702895 / VPI D76D-27C) (Lactobacillus uli).
OC   Bacteria; Actinobacteria; Coriobacteriia; Coriobacteriales; Atopobiaceae;
OC   Olsenella.
OX   NCBI_TaxID=633147;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49627 / DSM 7084 / CIP 109912 / JCM 12494 / NCIMB 702895 / VPI
RC   D76D-27C;
RX   PubMed=21304694; DOI=10.4056/sigs.1082860;
RA   Goker M., Held B., Lucas S., Nolan M., Yasawong M., Glavina Del Rio T.,
RA   Tice H., Cheng J.F., Bruce D., Detter J.C., Tapia R., Han C., Goodwin L.,
RA   Pitluck S., Liolios K., Ivanova N., Mavromatis K., Mikhailova N., Pati A.,
RA   Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D.,
RA   Rohde M., Sikorski J., Pukall R., Woyke T., Bristow J., Eisen J.A.,
RA   Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P., Lapidus A.;
RT   "Complete genome sequence of Olsenella uli type strain (VPI D76D-27C).";
RL   Stand. Genomic Sci. 3:76-84(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; CP002106; ADK68644.1; -; Genomic_DNA.
DR   RefSeq; WP_013252396.1; NZ_JQCO01000002.1.
DR   AlphaFoldDB; E1QWZ1; -.
DR   SMR; E1QWZ1; -.
DR   STRING; 633147.Olsu_1545; -.
DR   PRIDE; E1QWZ1; -.
DR   EnsemblBacteria; ADK68644; ADK68644; Olsu_1545.
DR   KEGG; ols:Olsu_1545; -.
DR   PATRIC; fig|633147.7.peg.1242; -.
DR   eggNOG; COG0119; Bacteria.
DR   HOGENOM; CLU_022158_0_1_11; -.
DR   OMA; SNMFAHE; -.
DR   OrthoDB; 840579at2; -.
DR   UniPathway; UPA00048; UER00070.
DR   Proteomes; UP000000333; 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..511
FT                   /note="2-isopropylmalate synthase"
FT                   /id="PRO_0000406896"
FT   DOMAIN          5..268
FT                   /note="Pyruvate carboxyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01151"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   511 AA;  54966 MW;  3C20B3D7146B66D2 CRC64;
     MTRKIDIFDT TLRDGEQSPG ASMNTEEKLI VAQQLLRMHV DVIEAGFPIS SPGDFRSVQE
     IGRLAGDDAV VVGLTRAVDK DIDRAAEALS CAKRPRIHTG LGVSPQHLAD KLRISEDECV
     ERAIRCVRYA KRYVEDVQFY AEDAGRADQG FLERVIQAVI EAGATVVNIP DTTGYQMPAA
     FGARIKGLCD NVRGIENVTI AVHTHNDLGM ATALALAGVE NGATQIECTI NGLGERAGNT
     ALEEVVMALR MHGDELDGHT DVVTQELTRA SRLVSRITGM QVQANKAIVG ANAFAHSSGI
     HQDGVLKSRG TYEIIDPADV GAAGSEIILS ARSGHAALRH RLSELGYSFP ESEFDDVYQR
     FLEIADQKKE VFDEDLESMV QERQRDVTAI YALESVQVVC GDAAIPTATV HITDEVGGEH
     VVACTGTGPV DAAYKAIDKV VSVHGDLQEF AVKAITRGID AIGEVTVRIV AGDGRLYTGR
     GSDTDIVVSS AKAYVNAINR MIQTTRSKQG K