ID   LEU1_SEDSS              Reviewed;         505 AA.
AC   E1R5X1;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   30-NOV-2010, sequence version 1.
DT   25-MAY-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=Spirs_1609;
OS   Sediminispirochaeta smaragdinae (strain DSM 11293 / JCM 15392 / SEBR 4228)
OS   (Spirochaeta smaragdinae).
OC   Bacteria; Spirochaetes; Spirochaetales; Spirochaetaceae;
OC   Sediminispirochaeta.
OX   NCBI_TaxID=573413;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 11293 / JCM 15392 / SEBR 4228;
RX   PubMed=21304743; DOI=10.4056/sigs.1143106;
RA   Mavromatis K., Yasawong M., Chertkov O., Lapidus A., Lucas S., Nolan M.,
RA   Del Rio T.G., Tice H., Cheng J.F., Pitluck S., Liolios K., Ivanova N.,
RA   Tapia R., Han C., Bruce D., Goodwin L., Pati A., Chen A., Palaniappan K.,
RA   Land M., Hauser L., Chang Y.J., Jeffries C.D., Detter J.C., Rohde M.,
RA   Brambilla E., Spring S., Goker M., Sikorski J., Woyke T., Bristow J.,
RA   Eisen J.A., Markowitz V., Hugenholtz P., Klenk H.P., Kyrpides N.C.;
RT   "Complete genome sequence of Spirochaeta smaragdinae type strain (SEBR
RT   4228).";
RL   Stand. Genomic Sci. 3:136-144(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; CP002116; ADK80736.1; -; Genomic_DNA.
DR   RefSeq; WP_013254200.1; NC_014364.1.
DR   AlphaFoldDB; E1R5X1; -.
DR   SMR; E1R5X1; -.
DR   STRING; 573413.Spirs_1609; -.
DR   EnsemblBacteria; ADK80736; ADK80736; Spirs_1609.
DR   KEGG; ssm:Spirs_1609; -.
DR   eggNOG; COG0119; Bacteria.
DR   HOGENOM; CLU_022158_0_1_12; -.
DR   OMA; NTMRMLV; -.
DR   OrthoDB; 840579at2; -.
DR   UniPathway; UPA00048; UER00070.
DR   Proteomes; UP000002318; 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..505
FT                   /note="2-isopropylmalate synthase"
FT                   /id="PRO_0000406899"
FT   DOMAIN          5..269
FT                   /note="Pyruvate carboxyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01151"
SQ   SEQUENCE   505 AA;  55377 MW;  14717CBA6393F195 CRC64;
     MPRRIKIFDT TLRDGEQSPG ASMSLEQKIK MASALERLGV DRIEAGFPVS SPVQFEAVQR
     VSATVKKAEV VGLARCVQRD IDAAYDALRD AAHPMLHIFI ATSPLHREYK LKKSKEEILD
     TVRECLNYGG KGFSRMEFSP EDASRTEPDY LVEVVKTAIE CGATSINIPD TVGYAVPKEF
     GQLISFLVEQ VPQFSDGSVD LSVHCHNDLG LALANSLAAV RSGASQVEVT LNGIGERAGN
     CPMEELIMSL DVRKDMFDVE TGIHTEYLYP TGKLLQSITG LLIPRNKPIF GDNVFVHESG
     IHQHGVLNKR ETYEIMKPER IGRSSETIIM GRHSGKHALE DKLSQYNIKL TRQQFEDVFA
     RFTAIADKKK EVYDEDLFSI VGTVLGGVVK GFSLLYFHTF TGNSLIPGAT VKVRSEAGEK
     VASATGDGPV DAVFNAIDEC VGINARLKEY IIHAIGSGKD AQGEVKLEVE IEGATYGGKA
     SSTDIIEASA MAYLNAVNRF ELRKR