LEU1_ECOLI
ID LEU1_ECOLI Reviewed; 523 AA.
AC P09151; P78044;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 5.
DT 03-AUG-2022, entry version 166.
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=b0074, JW0073;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=1630901; DOI=10.1093/nar/20.13.3305;
RA Yura T., Mori H., Nagai H., Nagata T., Ishihama A., Fujita N., Isono K.,
RA Mizobuchi K., Nakata A.;
RT "Systematic sequencing of the Escherichia coli genome: analysis of the 0-
RT 2.4 min region.";
RL Nucleic Acids Res. 20:3305-3308(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND SEQUENCE REVISION TO 192
RP AND 194.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-21.
RC STRAIN=K12;
RX PubMed=6171647; DOI=10.1016/0022-2836(81)90348-x;
RA Wessler S.R., Calvo J.M.;
RT "Control of leu operon expression in Escherichia coli by a transcription
RT attenuation mechanism.";
RL J. Mol. Biol. 149:579-597(1981).
RN [5]
RP PROTEIN SEQUENCE OF 2-13.
RC STRAIN=K12 / EMG2;
RX PubMed=9298646; DOI=10.1002/elps.1150180807;
RA Link A.J., Robison K., Church G.M.;
RT "Comparing the predicted and observed properties of proteins encoded in the
RT genome of Escherichia coli K-12.";
RL Electrophoresis 18:1259-1313(1997).
CC -!- FUNCTION: Catalyzes the condensation of the acetyl group of acetyl-CoA
CC with 3-methyl-2-oxobutanoate (2-oxoisovalerate) to form 3-carboxy-3-
CC hydroxy-4-methylpentanoate (2-isopropylmalate).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-methyl-2-oxobutanoate + acetyl-CoA + H2O = (2S)-2-
CC isopropylmalate + CoA + H(+); Xref=Rhea:RHEA:21524, ChEBI:CHEBI:1178,
CC ChEBI:CHEBI:11851, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288; EC=2.3.3.13;
CC -!- PATHWAY: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine
CC from 3-methyl-2-oxobutanoate: step 1/4.
CC -!- SUBUNIT: Homotetramer.
CC -!- SIMILARITY: Belongs to the alpha-IPM synthase/homocitrate synthase
CC family. LeuA type 1 subfamily. {ECO:0000305}.
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DR EMBL; U00096; AAC73185.1; -; Genomic_DNA.
DR EMBL; AP009048; BAB96643.2; -; Genomic_DNA.
DR EMBL; J01642; AAA24066.1; -; Genomic_DNA.
DR EMBL; X55034; CAA38851.1; -; Genomic_DNA.
DR PIR; B64729; B64729.
DR RefSeq; NP_414616.1; NC_000913.3.
DR RefSeq; WP_000082850.1; NZ_SSZK01000004.1.
DR AlphaFoldDB; P09151; -.
DR SMR; P09151; -.
DR BioGRID; 4259516; 9.
DR DIP; DIP-6851N; -.
DR IntAct; P09151; 6.
DR STRING; 511145.b0074; -.
DR PaxDb; P09151; -.
DR PRIDE; P09151; -.
DR DNASU; 947465; -.
DR EnsemblBacteria; AAC73185; AAC73185; b0074.
DR EnsemblBacteria; BAB96643; BAB96643; BAB96643.
DR GeneID; 947465; -.
DR KEGG; ecj:JW0073; -.
DR KEGG; eco:b0074; -.
DR PATRIC; fig|1411691.4.peg.2207; -.
DR EchoBASE; EB1208; -.
DR eggNOG; COG0119; Bacteria.
DR HOGENOM; CLU_022158_0_1_6; -.
DR InParanoid; P09151; -.
DR OMA; NTMRMLV; -.
DR PhylomeDB; P09151; -.
DR BioCyc; EcoCyc:2-ISOPROPYLMALATESYN-MON; -.
DR BioCyc; MetaCyc:2-ISOPROPYLMALATESYN-MON; -.
DR UniPathway; UPA00048; UER00070.
DR PRO; PR:P09151; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0003852; F:2-isopropylmalate synthase activity; IMP:EcoCyc.
DR GO; GO:0003985; F:acetyl-CoA C-acetyltransferase activity; IDA:EcoCyc.
DR GO; GO:0009098; P:leucine biosynthetic process; IDA:EcoCyc.
DR Gene3D; 3.20.20.70; -; 1.
DR Gene3D; 3.30.160.270; -; 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; IPR036230; LeuA_allosteric_dom_sf.
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 1: Evidence at protein level;
KW Amino-acid biosynthesis; Branched-chain amino acid biosynthesis;
KW Direct protein sequencing; Leucine biosynthesis; Reference proteome;
KW Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:9298646"
FT CHAIN 2..523
FT /note="2-isopropylmalate synthase"
FT /id="PRO_0000140351"
FT DOMAIN 5..267
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01151"
SQ SEQUENCE 523 AA; 57298 MW; 9F6DE8C007F85FB1 CRC64;
MSQQVIIFDT TLRDGEQALQ ASLSVKEKLQ IALALERMGV DVMEVGFPVS SPGDFESVQT
IARQVKNSRV CALARCVEKD IDVAAESLKV AEAFRIHTFI ATSPMHIATK LRSTLDEVIE
RAIYMVKRAR NYTDDVEFSC EDAGRTPIAD LARVVEAAIN AGATTINIPD TVGYTMPFEF
AGIISGLYER VPNIDKAIIS VHTHDDLGLA VGNSLAAVHA GARQVEGAMN GIGERAGNCS
LEEVIMAIKV RKDILNVHTA INHQEIWRTS QLVSQICNMP IPANKAIVGS GAFAHSSGIH
QDGVLKNREN YEIMTPESIG LNQIQLNLTS RSGRAAVKHR MDEMGYKESE YNLDNLYDAF
LKLADKKGQV FDYDLEALAF IGKQQEEPEH FRLDYFSVQS GSNDIATAAV KLACGEEVKA
EAANGNGPVD AVYQAINRIT EYNVELVKYS LTAKGHGKDA LGQVDIVANY NGRRFHGVGL
ATDIVESSAK AMVHVLNNIW RAAEVEKELQ RKAQHNENNK ETV
