(data stored in ACNUC7421 zone)

SWISSPROT: LEU1_SHESH

ID   LEU1_SHESH              Reviewed;         523 AA.
AC   A8FQ83;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 1.
DT   07-JUN-2017, entry version 66.
DE   RecName: Full=2-isopropylmalate synthase {ECO:0000255|HAMAP-Rule:MF_01025};
DE            EC=2.3.3.13 {ECO:0000255|HAMAP-Rule:MF_01025};
DE   AltName: Full=Alpha-IPM synthase {ECO:0000255|HAMAP-Rule:MF_01025};
DE   AltName: Full=Alpha-isopropylmalate synthase {ECO:0000255|HAMAP-Rule:MF_01025};
GN   Name=leuA {ECO:0000255|HAMAP-Rule:MF_01025};
GN   OrderedLocusNames=Ssed_0393;
OS   Shewanella sediminis (strain HAW-EB3).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=425104;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HAW-EB3;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T.,
RA   Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D.,
RA   Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Kim E., Zhao J.-S., Richardson P.;
RT   "Complete sequence of Shewanella sediminis HAW-EB3.";
RL   Submitted (AUG-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).
CC       {ECO:0000255|HAMAP-Rule:MF_01025}.
CC   -!- CATALYTIC ACTIVITY: Acetyl-CoA + 3-methyl-2-oxobutanoate + H(2)O =
CC       (2S)-2-isopropylmalate + CoA. {ECO:0000255|HAMAP-Rule:MF_01025}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-leucine biosynthesis; L-
CC       leucine from 3-methyl-2-oxobutanoate: step 1/4.
CC       {ECO:0000255|HAMAP-Rule:MF_01025}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_01025}.
CC   -!- SIMILARITY: Belongs to the alpha-IPM synthase/homocitrate synthase
CC       family. LeuA type 1 subfamily. {ECO:0000255|HAMAP-Rule:MF_01025}.
DR   EMBL; CP000821; ABV35006.1; -; Genomic_DNA.
DR   RefSeq; WP_012140743.1; NC_009831.1.
DR   ProteinModelPortal; A8FQ83; -.
DR   SMR; A8FQ83; -.
DR   STRING; 425104.Ssed_0393; -.
DR   EnsemblBacteria; ABV35006; ABV35006; Ssed_0393.
DR   KEGG; sse:Ssed_0393; -.
DR   eggNOG; ENOG4105CYQ; Bacteria.
DR   eggNOG; COG0119; LUCA.
DR   HOGENOM; HOG000046859; -.
DR   KO; K01649; -.
DR   OMA; KFHGVGL; -.
DR   OrthoDB; POG091H05O8; -.
DR   UniPathway; UPA00048; UER00070.
DR   Proteomes; UP000002015; Chromosome.
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;
DR   PRODOM; A8FQ83.
DR   SWISS-2DPAGE; A8FQ83.
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_1000149290.
FT   DOMAIN        5    267       Pyruvate carboxyltransferase.
FT                                {ECO:0000255|PROSITE-ProRule:PRU01151}.
SQ   SEQUENCE   523 AA;  56773 MW;  150D248BDBAEF711 CRC64;
     MSNRVIIFDT TLRDGEQALA ASLTVKEKLQ IALSLERLGV DVMEVGFPVS SPGDFNSVQT
     IANTVKNSRV CALARALEKD IDAAAQSLSV ADQFRIHTFI STSTIHVESK LKRSFDQVLE
     MAVGAVKYAR RFTDDVEFSC EDAGRTPIDN LCRMVEEAIK AGARTINIPD TVGYTIPSEF
     GGIIETLFNR VPNIDQAIIS VHCHDDLGLS VANSITAVQQ GARQIECTVN GIGERAGNCS
     LEEIAMILST RKDSLGLETG INAKEIHRTS NLVSQLCNMP VQANKAIVGA NAFTHSSGIH
     QDGMLKSQNT YEIMTPESIG LHRNNLNMTS RSGRHVIKHR MEEMGYGNKD YDMDTLYEAF
     LQLADKKGQV FDYDLEALAF MEAQVDEEAD YKLAQLVVHS DSTEGNATAT VKLEIDGKTV
     TEAATGNGPV DAAYNAIARA SQCEVNITSY KLSAKGEGQN ALGQVDIEAN YNEQSFHGVG
     LATDVVEASV QALVHVMNLT SRADKVADCK EKIQKDRSEL GGV
//

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