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-APR-2013, entry version 66.
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; Magnoliophyta; eudicotyledons; core eudicotyledons;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; Phaseoleae;
OC Glycine.
OX NCBI_TaxID=3847;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Akisengoku; TISSUE=Root nodule;
RX PubMed=7539640;
RA Kouchi H., Hata S.;
RT "GmN56, a novel nodule-specific cDNA from soybean root nodules encodes
RT a protein homologous to isopropylmalate synthase and homocitrate
RT synthase.";
RL Mol. Plant Microbe Interact. 8:172-176(1995).
CC -!- FUNCTION: Catalyzes the condensation of the acetyl group of
CC acetyl-CoA with 3-methyl-2-oxobutanoate (2-oxoisovalerate) to form
CC 3-carboxy-3-hydroxy-4-methylpentanoate (2-isopropylmalate). May
CC play an important role in symbiotic nitrogen fixation.
CC -!- CATALYTIC ACTIVITY: Acetyl-CoA + 3-methyl-2-oxobutanoate + H(2)O =
CC (2S)-2-isopropylmalate + CoA.
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-
CC fixation activity.
CC -!- SIMILARITY: Belongs to the alpha-IPM synthase/homocitrate synthase
CC family. LeuA type 1 subfamily.
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DR EMBL; D38015; BAA07212.1; -; mRNA.
DR PIR; T08590; T08590.
DR RefSeq; NP_001237749.1; NM_001250820.1.
DR UniGene; Gma.29860; -.
DR ProteinModelPortal; Q39891; -.
DR GeneID; 547778; -.
DR KEGG; gmx:547778; -.
DR Genevestigator; Q39891; -.
DR GO; GO:0003852; F:2-isopropylmalate synthase activity; IEA:EC.
DR GO; GO:0009098; P:leucine biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0009399; P:nitrogen fixation; IEA:UniProtKB-KW.
DR GO; GO:0009877; P:nodulation; IEA:UniProtKB-KW.
DR Gene3D; 3.20.20.70; -; 1.
DR InterPro; IPR013709; 2-isopropylmalate_synth_dimer.
DR InterPro; IPR002034; AIPM/Hcit_synth_CS.
DR InterPro; IPR013785; Aldolase_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; 2-isopropylmalate_synth_dimer; 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 Complete proteome; Leucine biosynthesis; Nitrogen fixation;
KW Nodulation; Reference proteome; Transferase.
FT CHAIN 1 565 Probable 2-isopropylmalate synthase.
FT /FTId=PRO_0000140448.
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
//
