ID LEU1_SHEPC Reviewed; 522 AA.
AC A4Y2M0;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 1.
DT 01-MAY-2013, entry version 46.
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=Sputcn32_0471;
OS Shewanella putrefaciens (strain CN-32 / ATCC BAA-453).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=319224;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CN-32 / ATCC BAA-453;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA Romine M.F., Fredrickson J., Tiedje J., Richardson P.;
RT "Complete sequence of Shewanella putrefaciens CN-32.";
RL Submitted (APR-2007) 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; CP000681; ABP74203.1; -; Genomic_DNA.
DR RefSeq; YP_001182002.1; NC_009438.1.
DR ProteinModelPortal; A4Y2M0; -.
DR STRING; 319224.Sputcn32_0471; -.
DR EnsemblBacteria; ABP74203; ABP74203; Sputcn32_0471.
DR GeneID; 5080726; -.
DR KEGG; spc:Sputcn32_0471; -.
DR PATRIC; 23549494; VBIShePut135485_0476.
DR eggNOG; COG0119; -.
DR HOGENOM; HOG000046859; -.
DR KO; K01649; -.
DR OMA; VWSVHCH; -.
DR ProtClustDB; PRK00915; -.
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 1 522 2-isopropylmalate synthase.
FT /FTId=PRO_1000149287.
SQ SEQUENCE 522 AA; 56939 MW; BD179AC4101C6F53 CRC64;
MSNRVIIFDT TLRDGEQALA ASLSVKEKLQ IAMALERLGV DVMEVGFPVS SPGDFESVQT
IARTIKNSRV CALSRALEKD IDAAAQALSV ADQFRIHTFI STSTIHVESK LKRSFDQVLE
MAVGAVKYAR RFTDDVEFSC EDAGRTPIDN LCRMVEAAIL AGARTINIPD TVGYTVPSEF
GNIIQTLFNR VPNIDQAVIS VHCHDDLGLS VANSITAVQH GARQIECTIN GIGERAGNCS
LEEIAMILAT RKGMLGLETG INAKEIHRTS NLVSQLCNMP VQANKAIVGA NAFTHSSGIH
QDGMLKAQNT YEIMTPESIG LNRNNLNMTS RSGRHVIKHR MEEMGYSEHD YNMDTLYEEF
LKLADKKGQV FDYDLEALAF MEAQAEEDNH YQLQQLVVQS DSTEGVATAT VRIEVGGEIK
TEAATGNGPV DAAYNAIARA TDRRIDIISY KLGAKGVGQN ALGQVDITAV YHEQNFHGVG
LATDVVEASA RALVHVMNLT CRADKVADYK QSMQKNRELG GV
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