Database: RefSeq
Entry: YP_001461509
LinkDB: YP_001461509
Original site: YP_001461509 
LOCUS       YP_001461509             389 aa            linear   CON 16-DEC-2014
DEFINITION  methylcitrate synthase [Escherichia coli E24377A].
ACCESSION   YP_001461509
VERSION     YP_001461509.1  GI:157157579
DBLINK      BioProject: PRJNA58395
DBSOURCE    REFSEQ: accession NC_009801.1
SOURCE      Escherichia coli E24377A
  ORGANISM  Escherichia coli E24377A
            Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
            Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 389)
  AUTHORS   Rasko,D.A., Rosovitz,M.J., Myers,G.S., Mongodin,E.F., Fricke,W.F.,
            Gajer,P., Crabtree,J., Sebaihia,M., Thomson,N.R., Chaudhuri,R.,
            Henderson,I.R., Sperandio,V. and Ravel,J.
  TITLE     The pangenome structure of Escherichia coli: comparative genomic
            analysis of E. coli commensal and pathogenic isolates
  JOURNAL   J. Bacteriol. 190 (20), 6881-6893 (2008)
   PUBMED   18676672
REFERENCE   2  (residues 1 to 389)
  CONSRTM   NCBI Genome Project
  TITLE     Direct Submission
  JOURNAL   Submitted (13-SEP-2007) National Center for Biotechnology
            Information, NIH, Bethesda, MD 20894, USA
REFERENCE   3  (residues 1 to 389)
  AUTHORS   Rasko,D.A., Rosovitz,M.J., Brinkley,C., Myers,G.S.A., Seshadri,R.,
            Cer,R.Z., Jiang,L. and Ravel,J.
  TITLE     Direct Submission
  JOURNAL   Submitted (13-AUG-2007) The Institute for Genomic Research, 9712
            Medical Center Dr., Rockville, MD 20850, USA
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from ABV19317.
            Source DNA and bacteria available from Jacques Ravel
            Method: conceptual translation.
FEATURES             Location/Qualifiers
     source          1..389
                     /organism="Escherichia coli E24377A"
     Protein         1..389
                     /product="methylcitrate synthase"
     Region          10..388
                     /note="Citrate synthase [Energy production and
                     conversion]; COG0372"
     Region          20..385
                     /note="Subgroup of Escherichia coli (Ec) 2-methylcitrate
                     synthase (2MCS)_like. 2MCS catalyzes the condensation of
                     propionyl-coenzyme A (PrCoA) and oxalacetate (OAA) to form
                     2-methylcitrate and coenzyme A (CoA) during propionate
                     metabolism. Citrate synthase (CS)...; cd06117"
     Site            order(20..22,25..29,91..92,95..96,104,108,112,115,163,
                     /note="dimer interface [polypeptide binding]"
     Site            order(23,200,203,234..236,238,241,268..275,278,283,318,
     Site            order(23,200,203,234..235,268..269,271..275,283,323,350)
                     /note="citrylCoA binding site [chemical binding]"
     Site            order(200,203,235..236,274,283,325,346,350,369)
                     /note="oxalacetate/citrate binding site [chemical
     Site            order(234..235,238,241,268..273,275,278,318,320,323,325,
                     /note="coenzyme A binding site [chemical binding]"
     Site            order(235,274,325)
                     /note="catalytic triad [active]"
     CDS             1..389
                     /note="catalyzes the synthesis of 2-methylcitrate from
                     propionyl-CoA and oxaloacetate; also catalyzes the
                     condensation of oxaloacetate with acetyl-CoA but with a
                     lower specificity"
CONTIG      join(WP_001285909.1:1..389)
        1 msdttilqns thvikpkksv alsgvpagnt alctvgksgn dlhyrgydil dlaehcefee
       61 vahllihgkl ptrdelaayk tklkalrglp anvrtvleal paashpmdvm rtgvsalgct
      121 lpekeghtvs gardiadkll aslssillyw yhyshngeri qpetdddsig ghflhllhge
      181 kpsqswekam hislvlyaeh efnastftsr viagtgsdmy saiigaigal rgpkhggane
      241 vsleiqqrye tpdeaeadir krvenkevvi gfghpvytia dprhqvikrv akqlsqeggs
      301 lkmyniadrl etvmweskkm fpnldwfsav synmmgvpte mftplfviar vtgwaahiie
      361 qrqdnkiirp sanyvgpedr qfvaldkrq
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