NADPH-dependent aldehyde reductase YahK [Escherichia coli].

LOCUS       WP_000692767             349 aa            linear   BCT 10-JUL-2019
ACCESSION   WP_000692767
VERSION     WP_000692767.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 349)
  AUTHORS   Pick,A., Ruhmann,B., Schmid,J. and Sieber,V.
  TITLE     Novel CAD-like enzymes from Escherichia coli K-12 as additional
            tools in chemical production
  JOURNAL   Appl. Microbiol. Biotechnol. 97 (13), 5815-5824 (2013)
   PUBMED   23093176
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 :: NBR007570
            Evidence Source    :: NCBI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..349
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     gene            1..349
                     /gene="yahK"
     Protein         1..349
                     /product="NADPH-dependent aldehyde reductase YahK"
                     /EC_number="1.1.1.2"
                     /calculated_mol_wt=37837
     Region          10..343
                     /region_name="CAD1"
                     /note="Cinnamyl alcohol dehydrogenases (CAD); cd05283"
                     /db_xref="CDD:176186"
     Site            order(40..42,45,158,162,182..187,205..206,210,225,
                     244..245,247,267..268,292..294)
                     /site_type="other"
                     /note="putative NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:176186"
     Site            order(40,42,62,88,158,294)
                     /site_type="other"
                     /note="putative substrate binding site [chemical binding]"
                     /db_xref="CDD:176186"
     Site            order(40,62,158)
                     /site_type="other"
                     /note="catalytic Zn binding site [ion binding]"
                     /db_xref="CDD:176186"
     Site            order(93,96,99,107)
                     /site_type="other"
                     /note="structural Zn binding site [ion binding]"
                     /db_xref="CDD:176186"
     Site            order(106,165,169,261,266..268,270,280,282..283,286..293)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:176186"
ORIGIN      
        1 mkikavgsys akqplepmdi trrepgpndv kieiaycgvc hsdlhqvrse wagtvypcvp
       61 gheivgrvva vgdqvekhap gdlvgvgciv dsckhceece dglenycdhm tgtynsptpd
      121 epghtlggys qqivvheryv lrirhpqeql aavapllcag ittysplrhw qagpgkkvgv
      181 vgigglghmg iklahamgah vvafttseak reaakalgad evvnsrnade maahlksfdf
      241 ilntvaaphn lddfttllkr dgtmtlvgap atphkspevf nlimkrraia gsmiggipet
      301 qemldfcaeh givadiemir adqineayer mlrgdvkyrf vidnrtltd