ID LEU1_SALDC Reviewed; 523 AA.
AC B5FI58;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 1.
DT 01-MAY-2013, entry version 40.
DE RecName: Full=2-isopropylmalate synthase;
DE EC=2.3.3.13;
DE AltName: Full=Alpha-IPM synthase;
DE AltName: Full=Alpha-isopropylmalate synthase;
GN Name=leuA; OrderedLocusNames=SeD_A0122;
OS Salmonella dublin (strain CT_02021853).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=439851;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CT_02021853;
RA Ravel J., Fricke W.F., White D., McDermott P., Mammel M., Rosovitz M.,
RA Leclerc J., Cebula T., Sebastian Y.;
RT "Complete genome of Salmonella dublin strain CT_02021853.";
RL Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases.
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) (By
CC similarity).
CC -!- CATALYTIC ACTIVITY: Acetyl-CoA + 3-methyl-2-oxobutanoate + H(2)O =
CC (2S)-2-isopropylmalate + CoA.
CC -!- PATHWAY: Amino-acid biosynthesis; L-leucine biosynthesis; L-
CC leucine from 3-methyl-2-oxobutanoate: step 1/4.
CC -!- SUBUNIT: Homotetramer (By similarity).
CC -!- SIMILARITY: Belongs to the alpha-IPM synthase/homocitrate synthase
CC family. LeuA type 1 subfamily.
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DR EMBL; CP001144; ACH76469.1; -; Genomic_DNA.
DR RefSeq; YP_002214066.1; NC_011205.1.
DR ProteinModelPortal; B5FI58; -.
DR STRING; 439851.SeD_A0122; -.
DR PRIDE; B5FI58; -.
DR EnsemblBacteria; ACH76469; ACH76469; SeD_A0122.
DR GeneID; 6873686; -.
DR KEGG; sed:SeD_A0122; -.
DR PATRIC; 18488469; VBISalEnt111443_0211.
DR eggNOG; COG0119; -.
DR HOGENOM; HOG000046859; -.
DR KO; K01649; -.
DR OMA; VWSVHCH; -.
DR ProtClustDB; PRK00915; -.
DR BioCyc; SENT439851:GH2Z-3069-MONOMER; -.
DR UniPathway; UPA00048; UER00070.
DR GO; GO:0003852; F:2-isopropylmalate synthase activity; IEA:HAMAP.
DR GO; GO:0009098; P:leucine biosynthetic process; IEA:HAMAP.
DR Gene3D; 3.20.20.70; -; 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; 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; 2-isopropylmalate_synth_dimer; 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 Complete proteome; Leucine biosynthesis; Transferase.
FT CHAIN 1 523 2-isopropylmalate synthase.
FT /FTId=PRO_1000149266.
SQ SEQUENCE 523 AA; 57431 MW; 0F5271BC488E7671 CRC64;
MSQQVIIFDT TLRDGEQALQ ASLSAKEKLQ IALALERMGV DVMEVGFPVS SPGDFESVQT
IARTIKNSRV CALARCVEKD IDVAAQALKV ADAFRIHTFI ATSPMHIATK LRSTLDEVIE
RAVYMVKRAR NYTDDVEFSC EDAGRTPVDD LARVVEAAIN AGARTINIPD TVGYTMPFEF
AGIISGLYER VPNIDKAIIS VHTHDDLGIA VGNSLAAVHA GARQVEGAMN GIGERAGNCA
LEEVIMAIKV RKDIMNVHTN INHHEIWRTS QTVSQICNMP IPANKAIVGS GAFAHSSGIH
QDGVLKNREN YEIMTPESIG LNQIQLNLTS RSGRAAVKHR MEEMGYKDTD YNMDHLYDAF
LKLADKKGQV FDYDLEALAF INKQQEEPEH FRLDYFSVQS GSSDIATASV KLACGEEIKA
EAANGNGPVD AIYQAINRIT GYDVELVKYD LNAKGQGKDA LGQVDIVVNH HGRRFHGVGL
ATDIVESSAK AMVHVLNNIW RAAEVEKELQ RKAQNKENNK ETV
//
