ID LEU1_EDWI9 Reviewed; 526 AA.
AC C5B7R4;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 1.
DT 29-MAY-2013, entry version 34.
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=NT01EI_0720;
OS Edwardsiella ictaluri (strain 93-146).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC Enterobacteriaceae; Edwardsiella.
OX NCBI_TaxID=634503;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=93-146;
RA Williams M.L., Gillaspy A.F., Dyer D.W., Thune R.L., Waldbieser G.C.,
RA Schuster S.C., Gipson J., Zaitshik J., Landry C., Lawrence M.L.;
RT "Complete genome sequence of Edwardsiella ictaluri 93-146.";
RL Submitted (MAR-2009) 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; CP001600; ACR67941.1; -; Genomic_DNA.
DR RefSeq; YP_002932176.1; NC_012779.2.
DR ProteinModelPortal; C5B7R4; -.
DR STRING; 634503.NT01EI_0720; -.
DR PRIDE; C5B7R4; -.
DR EnsemblBacteria; ACR67941; ACR67941; NT01EI_0720.
DR GeneID; 7962053; -.
DR KEGG; eic:NT01EI_0720; -.
DR PATRIC; 21834658; VBIEdwIct114273_0649.
DR eggNOG; COG0119; -.
DR HOGENOM; HOG000046859; -.
DR KO; K01649; -.
DR OMA; TKEYPAT; -.
DR ProtClustDB; PRK00915; -.
DR BioCyc; EICT634503:GCMY-714-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 1 526 2-isopropylmalate synthase.
FT /FTId=PRO_1000213313.
SQ SEQUENCE 526 AA; 57806 MW; 87A4FAF34990581F CRC64;
MKQQVIIFDT TLRDGEQALQ ASLSVKEKLQ IALALERMGV DVMEVGFPIS SPGDFASVRA
IAQRVKQSRV CALARCVDAD IDAAAEALRA ADAFRIHTFL ATSTLHLESK LRRSFDDAIA
MARHAILRAR RYTDDVEFSC EDAGRTPIDN LCRIVEAAID AGAKTVNIPD TVGYTTPYQF
GGIIHTLFER VPNIDKAVIS VHCHDDLGMA CANSISAIQS GARQVEGTLN GIGERAGNCA
LEEVIMAIRT RQDLLRVHTG IRHQEIYRTS QLVSQLCNMP IPANKAVVGA NAFAHSSGIH
QDGVLKNREN YEIMTPESIG LPQTQLNLTS RSGRAAVKHR MEEMGYCEGN DFDLERLYQA
FLRLADKKGQ VFDYDLEALA FIDRQQEEAD HFRLEYFSVQ SGSSVMATAS VRLICGAETR
AEAATGNGPV DAVYQAISRI TDISVDIVKY QLSAKGQGRD ALGQVDIVAE HQGRRFHGVG
LTTDIVESSA QALIHVLNHI WRARQVEQER QRLHSPVPSI STSSTH
//
