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Database: UniProt
Entry: B5FI58
LinkDB: B5FI58
Original site: B5FI58 
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   09-JUL-2014, entry version 47.
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;
RX   PubMed=21602358; DOI=10.1128/JB.00297-11;
RA   Fricke W.F., Mammel M.K., McDermott P.F., Tartera C., White D.G.,
RA   Leclerc J.E., Ravel J., Cebula T.A.;
RT   "Comparative genomics of 28 Salmonella enterica isolates: evidence for
RT   CRISPR-mediated adaptive sublineage evolution.";
RL   J. Bacteriol. 193:3556-3568(2011).
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   PATRIC; 18488469; VBISalEnt111443_0211.
DR   eggNOG; COG0119; -.
DR   HOGENOM; HOG000046859; -.
DR   OMA; EGQNALG; -.
DR   OrthoDB; EOG6CGCF3; -.
DR   BioCyc; SENT439851:GH2Z-119-MONOMER; -.
DR   UniPathway; UPA00048; UER00070.
DR   GO; GO:0003852; F:2-isopropylmalate synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009098; P:leucine biosynthetic process; IEA:UniProtKB-UniPathway.
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; SSF110921; 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
//
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