ID   LEU1_CYCRE              Reviewed;           9 AA.
AC   P85362;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 1.
DT   23-FEB-2022, entry version 24.
DE   RecName: Full=2-isopropylmalate synthase;
DE            EC=2.3.3.13;
DE   AltName: Full=Alpha-IPM synthase;
DE   AltName: Full=Alpha-isopropylmalate synthase;
DE   Flags: Fragment;
OS   Cycas revoluta (Sago palm).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Cycadidae; Cycadales; Cycadaceae; Cycas.
OX   NCBI_TaxID=3396;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, AND SUBCELLULAR LOCATION.
RC   TISSUE=Callus {ECO:0000269|PubMed:19157640};
RX   PubMed=19157640; DOI=10.1016/j.jplph.2008.11.009;
RA   Uzal E.N., Gomez-Ros L.V., Hernandez J.A., Pedreno M.A., Cuello J.,
RA   Ros Barcelo A.;
RT   "Analysis of the soluble cell wall proteome of gymnosperms.";
RL   J. Plant Physiol. 166:831-843(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).
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   -!- PATHWAY: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine
CC       from 3-methyl-2-oxobutanoate: step 1/4.
CC   -!- SUBCELLULAR LOCATION: Secreted, cell wall
CC       {ECO:0000269|PubMed:19157640}.
CC   -!- SIMILARITY: Belongs to the alpha-IPM synthase/homocitrate synthase
CC       family. LeuA type 1 subfamily. {ECO:0000305}.
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DR   UniPathway; UPA00048; UER00070.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0003852; F:2-isopropylmalate synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009098; P:leucine biosynthetic process; IEA:UniProtKB-UniPathway.
PE   1: Evidence at protein level;
KW   Amino-acid biosynthesis; Branched-chain amino acid biosynthesis; Cell wall;
KW   Direct protein sequencing; Leucine biosynthesis; Secreted; Transferase.
FT   CHAIN           <1..>9
FT                   /note="2-isopropylmalate synthase"
FT                   /id="PRO_0000315942"
FT   UNSURE          4
FT                   /note="L or I"
FT                   /evidence="ECO:0000269|PubMed:19157640"
FT   UNSURE          5
FT                   /note="L or I"
FT                   /evidence="ECO:0000269|PubMed:19157640"
FT   UNSURE          8
FT                   /note="L or I"
FT                   /evidence="ECO:0000269|PubMed:19157640"
FT   UNSURE          9
FT                   /note="K or Q"
FT                   /evidence="ECO:0000269|PubMed:19157640"
FT   NON_TER         1
FT                   /evidence="ECO:0000303|PubMed:19157640"
FT   NON_TER         9
FT                   /evidence="ECO:0000303|PubMed:19157640"
SQ   SEQUENCE   9 AA;  1061 MW;  C0E92AA4472736DD CRC64;
     FAQLLNDLK