(data stored in SCRATCH zone)

SWISSPROT: C8U1E6_ECO10

ID   C8U1E6_ECO10            Unreviewed;       523 AA.
AC   C8U1E6;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   08-MAY-2019, entry version 74.
DE   RecName: Full=2-isopropylmalate synthase {ECO:0000256|HAMAP-Rule:MF_01025, ECO:0000256|SAAS:SAAS00362855};
DE            EC=2.3.3.13 {ECO:0000256|HAMAP-Rule:MF_01025, ECO:0000256|SAAS:SAAS00085331};
DE   AltName: Full=Alpha-IPM synthase {ECO:0000256|HAMAP-Rule:MF_01025};
DE   AltName: Full=Alpha-isopropylmalate synthase {ECO:0000256|HAMAP-Rule:MF_01025};
GN   Name=leuA {ECO:0000256|HAMAP-Rule:MF_01025,
GN   ECO:0000313|EMBL:BAI28954.1};
GN   OrderedLocusNames=ECO103_0076 {ECO:0000313|EMBL:BAI28954.1};
OS   Escherichia coli O103:H2 (strain 12009 / EHEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585395 {ECO:0000313|EMBL:BAI28954.1, ECO:0000313|Proteomes:UP000000959};
RN   [1] {ECO:0000313|EMBL:BAI28954.1, ECO:0000313|Proteomes:UP000000959}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=12009 / EHEC {ECO:0000313|Proteomes:UP000000959};
RX   PubMed=19815525; DOI=10.1073/pnas.0903585106;
RA   Ogura Y., Ooka T., Iguchi A., Toh H., Asadulghani M., Oshima K.,
RA   Kodama T., Abe H., Nakayama K., Kurokawa K., Tobe T., Hattori M.,
RA   Hayashi T.;
RT   "Comparative genomics reveal the mechanism of the parallel evolution
RT   of O157 and non-O157 enterohemorrhagic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:17939-17944(2009).
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).
CC       {ECO:0000256|HAMAP-Rule:MF_01025, ECO:0000256|SAAS:SAAS00570112}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3-methyl-2-oxobutanoate + acetyl-CoA + H2O = (2S)-2-
CC         isopropylmalate + CoA + H(+); Xref=Rhea:RHEA:21524,
CC         ChEBI:CHEBI:1178, ChEBI:CHEBI:11851, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288;
CC         EC=2.3.3.13; Evidence={ECO:0000256|HAMAP-Rule:MF_01025,
CC         ECO:0000256|SAAS:SAAS01124331};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-leucine biosynthesis; L-
CC       leucine from 3-methyl-2-oxobutanoate: step 1/4.
CC       {ECO:0000256|HAMAP-Rule:MF_01025, ECO:0000256|SAAS:SAAS00085321}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_01025,
CC       ECO:0000256|SAAS:SAAS00362821}.
CC   -!- SIMILARITY: Belongs to the alpha-IPM synthase/homocitrate synthase
CC       family. LeuA type 1 subfamily. {ECO:0000256|HAMAP-Rule:MF_01025,
CC       ECO:0000256|SAAS:SAAS00570119}.
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DR   EMBL; AP010958; BAI28954.1; -; Genomic_DNA.
DR   RefSeq; WP_000082846.1; NC_013353.1.
DR   SMR; C8U1E6; -.
DR   EnsemblBacteria; BAI28954; BAI28954; ECO103_0076.
DR   KEGG; eoh:ECO103_0076; -.
DR   HOGENOM; HOG000046859; -.
DR   KO; K01649; -.
DR   OMA; NDTGMAI; -.
DR   BioCyc; ECOL585395:ECO103_RS00385-MONOMER; -.
DR   UniPathway; UPA00048; UER00070.
DR   Proteomes; UP000000959; Chromosome.
DR   GO; GO:0003852; F:2-isopropylmalate synthase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0009098; P:leucine biosynthetic process; IEA:UniProtKB-UniRule.
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; 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   3: Inferred from homology;
DR   PRODOM; C8U1E6.
DR   SWISS-2DPAGE; C8U1E6.
KW   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01025,
KW   ECO:0000256|SAAS:SAAS00161459};
KW   Branched-chain amino acid biosynthesis {ECO:0000256|HAMAP-
KW   Rule:MF_01025, ECO:0000256|SAAS:SAAS00160591};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000959};
KW   Leucine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01025,
KW   ECO:0000256|SAAS:SAAS00459347};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01025,
KW   ECO:0000256|SAAS:SAAS00131367}.
FT   DOMAIN        5    267       Pyruvate carboxyltransferase.
FT                                {ECO:0000259|PROSITE:PS50991}.
FT   COILED      502    522       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   523 AA;  57284 MW;  DE6DE91AAC89851A 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 DYNVELVKYS LTAKGHGKDA LGQVDIVANY NGRRFHGVGL
     ATDIVESSAK AMVHVLNNIW RAAEVEKELQ RKAQHNENNK ETV
//

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