ID   LEU1_SOYBN              Reviewed;         565 AA.
AC   Q39891;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=Probable 2-isopropylmalate synthase;
DE            EC=2.3.3.13;
DE   AltName: Full=Alpha-IPM synthase;
DE   AltName: Full=Alpha-isopropylmalate synthase;
DE   AltName: Full=Late nodulin-56;
DE            Short=N-56;
GN   Name=GMN56;
OS   Glycine max (Soybean) (Glycine hispida).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Glycine;
OC   Glycine subgen. Soja.
OX   NCBI_TaxID=3847;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Akisengoku; TISSUE=Root nodule;
RX   PubMed=7539640; DOI=10.1094/mpmi-8-0172;
RA   Kouchi H., Hata S.;
RT   "GmN56, a novel nodule-specific cDNA from soybean root nodules encodes a
RT   protein homologous to isopropylmalate synthase and homocitrate synthase.";
RL   Mol. Plant Microbe Interact. 8:172-176(1995).
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). May play an important
CC       role in symbiotic nitrogen fixation.
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   -!- TISSUE SPECIFICITY: Exclusively expressed in mature nodules.
CC   -!- INDUCTION: At the same time as leghemoglobin; after completion of
CC       nodule organogenesis and just before the onset of nitrogen-fixation
CC       activity.
CC   -!- SIMILARITY: Belongs to the alpha-IPM synthase/homocitrate synthase
CC       family. LeuA type 1 subfamily. {ECO:0000305}.
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DR   EMBL; D38015; BAA07212.1; -; mRNA.
DR   PIR; T08590; T08590.
DR   RefSeq; NP_001237749.1; NM_001250820.1.
DR   AlphaFoldDB; Q39891; -.
DR   SMR; Q39891; -.
DR   STRING; 3847.GLYMA13G12484.1; -.
DR   PRIDE; Q39891; -.
DR   GeneID; 547778; -.
DR   KEGG; gmx:547778; -.
DR   eggNOG; KOG2367; Eukaryota.
DR   InParanoid; Q39891; -.
DR   OrthoDB; 928619at2759; -.
DR   Proteomes; UP000008827; Unplaced.
DR   GO; GO:0009507; C:chloroplast; IBA:GO_Central.
DR   GO; GO:0003852; F:2-isopropylmalate synthase activity; IBA:GO_Central.
DR   GO; GO:0009098; P:leucine biosynthetic process; IBA:GO_Central.
DR   GO; GO:0009877; P:nodulation; IEA:UniProtKB-KW.
DR   Gene3D; 3.20.20.70; -; 1.
DR   Gene3D; 3.30.160.270; -; 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; 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   PROSITE; PS00815; AIPM_HOMOCIT_SYNTH_1; 1.
DR   PROSITE; PS00816; AIPM_HOMOCIT_SYNTH_2; 1.
DR   PROSITE; PS50991; PYR_CT; 1.
PE   2: Evidence at transcript level;
KW   Amino-acid biosynthesis; Branched-chain amino acid biosynthesis;
KW   Leucine biosynthesis; Nitrogen fixation; Nodulation; Reference proteome;
KW   Transferase.
FT   CHAIN           1..565
FT                   /note="Probable 2-isopropylmalate synthase"
FT                   /id="PRO_0000140448"
FT   DOMAIN          33..306
FT                   /note="Pyruvate carboxyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01151"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..18
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   565 AA;  61580 MW;  1B01B63239D1F62B CRC64;
     MPTKTSTPSS QSPKLSHLRP QYIPNHIPDS SYVRILDTTL RDGEQSPGAT MTAKEKLDIA
     RQLVKLGVDI IQPGFPSASN SDFMAVKMIA QEVGNAVDDD GYVPVIAGFC RCVEKDISTA
     WEAVKYAKRP RLCTSIATSP IHMEHKLRKS KDQVIQIARD MVKFARSLGC NDIQFGAEDA
     TRSDREFLYE ILGVVIEAGA TTVNIADTVG IVMPLELGKL IVDIKDNTPG IANVIISTHC
     HNDLGLATAN TIEGARTGAR QLEVTINGIG ERAGNASLEE VVMALASKGD HALNGLYTRI
     NTRHILETSK MVEEYSGMHL QPHKPLVGAN AFVHASGIHQ DGMLKHKGTY ETISPEEIGH
     KRTTRIGIVL GKLSGSQALR KRLEELGYDL KEDEVDSVFW QFKAMAEKKK VVTDVDLKAL
     VSYKAFHAES IWKLGDLQVT CGTIGLSTAT VKLVNIDGST HVACSIGIGA VDSTYKAINL
     IVKEPTKLLD YSLNSVTEGI GVNVTARVVI CRENNHTSTY AFTEDANYPT FSGIAAEMDV
     VVSTVKAYLV ALNKLLRWKE SFRCA