ID   LEU1_STRRD              Reviewed;         579 AA.
AC   D2ATJ4;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   09-FEB-2010, sequence version 1.
DT   25-MAY-2022, entry version 66.
DE   RecName: Full=2-isopropylmalate synthase {ECO:0000255|HAMAP-Rule:MF_00572};
DE            EC=2.3.3.13 {ECO:0000255|HAMAP-Rule:MF_00572};
DE   AltName: Full=Alpha-IPM synthase {ECO:0000255|HAMAP-Rule:MF_00572};
DE   AltName: Full=Alpha-isopropylmalate synthase {ECO:0000255|HAMAP-Rule:MF_00572};
GN   Name=leuA {ECO:0000255|HAMAP-Rule:MF_00572}; OrderedLocusNames=Sros_3794;
OS   Streptosporangium roseum (strain ATCC 12428 / DSM 43021 / JCM 3005 / NI
OS   9100).
OC   Bacteria; Actinobacteria; Streptosporangiales; Streptosporangiaceae;
OC   Streptosporangium.
OX   NCBI_TaxID=479432;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 12428 / DSM 43021 / JCM 3005 / NI 9100;
RX   PubMed=21304675; DOI=10.4056/sigs.631049;
RA   Nolan M., Sikorski J., Jando M., Lucas S., Lapidus A., Glavina Del Rio T.,
RA   Chen F., Tice H., Pitluck S., Cheng J.F., Chertkov O., Sims D., Meincke L.,
RA   Brettin T., Han C., Detter J.C., Bruce D., Goodwin L., Land M., Hauser L.,
RA   Chang Y.J., Jeffries C.D., Ivanova N., Mavromatis K., Mikhailova N.,
RA   Chen A., Palaniappan K., Chain P., Rohde M., Goker M., Bristow J.,
RA   Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Streptosporangium roseum type strain (NI
RT   9100).";
RL   Stand. Genomic Sci. 2:29-37(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_00572}.
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_00572};
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_00572}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_00572}.
CC   -!- SIMILARITY: Belongs to the alpha-IPM synthase/homocitrate synthase
CC       family. LeuA type 2 subfamily. {ECO:0000255|HAMAP-Rule:MF_00572}.
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DR   EMBL; CP001814; ACZ86714.1; -; Genomic_DNA.
DR   RefSeq; WP_012890457.1; NC_013595.1.
DR   AlphaFoldDB; D2ATJ4; -.
DR   SMR; D2ATJ4; -.
DR   STRING; 479432.Sros_3794; -.
DR   EnsemblBacteria; ACZ86714; ACZ86714; Sros_3794.
DR   KEGG; sro:Sros_3794; -.
DR   eggNOG; COG0119; Bacteria.
DR   HOGENOM; CLU_004588_3_0_11; -.
DR   OMA; FGQGERT; -.
DR   OrthoDB; 840579at2; -.
DR   UniPathway; UPA00048; UER00070.
DR   Proteomes; UP000002029; 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   CDD; cd07942; DRE_TIM_LeuA; 1.
DR   Gene3D; 3.20.20.70; -; 1.
DR   Gene3D; 3.30.160.270; -; 1.
DR   HAMAP; MF_00572; LeuA_type2; 1.
DR   InterPro; IPR013709; 2-isopropylmalate_synth_dimer.
DR   InterPro; IPR002034; AIPM/Hcit_synth_CS.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR005668; IPM_Synthase.
DR   InterPro; IPR036230; LeuA_allosteric_dom_sf.
DR   InterPro; IPR039371; LeuA_N_DRE-TIM.
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; TIGR00970; leuA_yeast; 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..579
FT                   /note="2-isopropylmalate synthase"
FT                   /id="PRO_0000406879"
FT   DOMAIN          33..308
FT                   /note="Pyruvate carboxyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01151"
SQ   SEQUENCE   579 AA;  63689 MW;  0428BEE670F038A9 CRC64;
     MKTTTRQTGR YGAFTPVPLP GRTWPNNIIG SAPRWLSTDL RDGNQSLATP MSPDRKLAMF
     ELLVSMGYKE IEVGFPVASQ DDFDFLRVLI EQERIPEDVR ISVLVQARDE LIRRTVESLE
     GAPRATIHLY NATSPLFRRV VFGMSRNECK DLAVQGTRLM MKYAEKTLGD CDLGFQYSPE
     LFSDTELDFS LEVCEAVMDV WQPEPGRGII LNFPTTVERS LPNVFADQIE WLSRNLSRRE
     HVCLSIHPHN DRGTAVASAE LALLAGAERI EGCLFGNGER AGNVCLVTLG LNMFTHGVDP
     GIDFSDINEI RRTVERCNGL AVHPRHPYGG DLVYTSFSGS HQDAIKKGFD ALEREAAHRG
     AAVGDLPWEM PYLPLDPEDV GRTYEAVVRI NSQSGKGGVA YVMSAWHGLN LPRDLQIDFA
     HVVQSQADAE GGEITPDRVK RLFEREYLSS SDLPVPLASG TELVTTSLHI DGERFDVGAD
     RADTVQAVRA TLTRWGFDVR AVHRTGIAGQ DRGPDADVAV YAECRVEGRV SWGVGIDRDI
     EAASLAAVRS AVIRARLKRL PARGGEATGI VAPLVAAGR