aminobutyraldehyde dehydrogenase [Escherichia coli].

LOCUS       WP_001163885             474 aa            linear   BCT 03-JUN-2024
ACCESSION   WP_001163885
VERSION     WP_001163885.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 474)
  AUTHORS   Schneider,B.L. and Reitzer,L.
  TITLE     Pathway and enzyme redundancy in putrescine catabolism in
            Escherichia coli
  JOURNAL   J Bacteriol 194 (15), 4080-4088 (2012)
   PUBMED   22636776
REFERENCE   2  (residues 1 to 474)
  AUTHORS   Samsonova,N.N., Smirnov,S.V., Novikova,A.E. and Ptitsyn,L.R.
  TITLE     Identification of Escherichia coli K12 YdcW protein as a
            gamma-aminobutyraldehyde dehydrogenase
  JOURNAL   FEBS Lett 579 (19), 4107-4112 (2005)
   PUBMED   16023116
REFERENCE   3  (residues 1 to 474)
  AUTHORS   Gruez,A., Roig-Zamboni,V., Grisel,S., Salomoni,A., Valencia,C.,
            Campanacci,V., Tegoni,M. and Cambillau,C.
  TITLE     Crystal structure and kinetics identify Escherichia coli YdcW gene
            product as a medium-chain aldehyde dehydrogenase
  JOURNAL   J Mol Biol 343 (1), 29-41 (2004)
   PUBMED   15381418
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  :: HMM
            Evidence Accession :: TIGR03374.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..474
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     gene            1..474
                     /gene="patD"
     Protein         1..474
                     /product="aminobutyraldehyde dehydrogenase"
                     /EC_number="1.2.1.19"
                     /GO_function="GO:0019145 - aminobutyraldehyde
                     dehydrogenase activity [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /GO_process="GO:0009447 - putrescine catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=50769
     Region          2..473
                     /region_name="ALDH-SF"
                     /note="NAD(P)+-dependent aldehyde dehydrogenase
                     superfamily; cl11961"
                     /db_xref="CDD:448367"
     Site            order(59,106,116,120..123,125..126,128,134..135,218,230,
                     233,240,247,412..416,419..420,422,425,427..432,441..443,
                     448..449,454,467..472)
                     /site_type="other"
                     /note="tetrameric interface [polypeptide binding]"
                     /db_xref="CDD:143411"
     Site            order(145..146,148,172,174..175,204,209,223..225,228,231,
                     246,248,280,327,378)
                     /site_type="other"
                     /note="NAD binding site [chemical binding]"
                     /db_xref="CDD:143411"
     Site            order(149,246,277,280)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:143411"
     Site            order(279,438)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:143411"
ORIGIN      
        1 mqhkllinge lvsgegekqp vynpatgdvl leiaeasaeq vdaavraada afaewgqttp
       61 kvraecllkl advieengqv faelesrncg kplhsafnde ipaivdvfrf fagaarclng
      121 laageylegh tsmirrdplg vvasiapwny plmmaawkla palaagncvv lkpseitplt
      181 alklaelakd ifpagvinvl fgrgktvgdp ltghpkvrmv sltgsiatge hiishtapsi
      241 krthmelggk apvivfddad ieavvegvrt fgyynagqdc tvacriyaqk giydtlvekl
      301 gaavatlksg apddestelg plsslahler vskaveeaka tghikvitgg ekrkgngyyy
      361 aptllagalq ddaivqkevf gpvvsvtlfd neeqvvnwan dsqyglassv wtkdvgrahr
      421 vsarlqygct wvnthfmlvs emphggqkls gygkdmslyg ledytvvrhv mvkh