2-ketobutyrate formate-lyase/pyruvate formate-lyase [Escherichia

LOCUS       WP_000861740             764 aa            linear   BCT 11-FEB-2021
            coli].
ACCESSION   WP_000861740
VERSION     WP_000861740.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 764)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: BlastRule
            Evidence Accession :: NBR007592
            Evidence Source    :: NCBI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..764
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     gene            1..764
                     /gene="tdcE"
     Protein         1..764
                     /product="2-ketobutyrate formate-lyase/pyruvate
                     formate-lyase"
                     /EC_number="2.3.1.-"
                     /EC_number="2.3.1.54"
                     /calculated_mol_wt=85804
     Region          15..760
                     /region_name="PFL1"
                     /note="Pyruvate formate lyase 1; cd01678"
                     /db_xref="CDD:153087"
     Site            order(121..122,150..151,154..155,157,162,165..166)
                     /site_type="other"
                     /note="coenzyme A binding site [chemical binding]"
                     /db_xref="CDD:153087"
     Site            order(181,277..278,332,338,423,437,440,609,611)
                     /site_type="active"
                     /db_xref="CDD:153087"
     Site            order(423..424,739)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:153087"
     Site            736..740
                     /site_type="active"
                     /note="glycine loop [active]"
                     /db_xref="CDD:153087"
ORIGIN      
        1 mkvdidtsdk lyadawlgfk gtdwkneinv rdfiqhnytp yegdesflae atpattelwe
       61 kvmegirien athapvdfdt niattitahd agyinqplek ivglqtdapl kralhpfggi
      121 nmikssfhay gremdsefey lftdlrkthn qgvfdvyspd mlrcrksgvl tglpdgygrg
      181 riigdyrrva lygisylvre relqfadlqs rlekgedlea tirlreelae hrhallqiqe
      241 maakygfdis rpaqnaqeav qwlyfaylaa vksqnggams lgrtasfldi yierdfkagv
      301 lneqqaqeli dhfimkirmv rflrtpefds lfsgdpiwat eviggmgldg rtlvtknsfr
      361 ylhtlhtmgp apepnltilw seelpiafkk yaaqvsivts slqyenddlm rtdfnsddya
      421 iaccvspmvi gkqmqffgar anlaktllya inggvdeklk iqvgpktapl mddvldydkv
      481 mdsldhfmdw lavqyisaln iihymhdkys yeaslmalhd rdvyrtmacg iaglsvatds
      541 lsaikyarvk pirdknglav dfeidgeypq ygnndervds iacdlverfm kkikalptyr
      601 navptqsilt itsnvvygqk tgntpdgrra gtpfapganp mhgrdrkgav asltsvaklp
      661 ftyakdgisy tfsivpaalg kedpvrktnl vglldgyfhh eadveggqhl nvnvmnreml
      721 ldaiehpeky pnltirvsgy avrfnaltre qqqdvisrtf tqal