MULTISPECIES: aminobutyraldehyde dehydrogenase [Salmonella].

LOCUS       WP_000158107             481 aa            linear   BCT 03-JUN-2024
ACCESSION   WP_000158107
VERSION     WP_000158107.1
KEYWORDS    RefSeq.
SOURCE      Salmonella
  ORGANISM  Salmonella
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
REFERENCE   1  (residues 1 to 481)
  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 481)
  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 481)
  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..481
                     /organism="Salmonella"
                     /db_xref="taxon:590"
     gene            1..481
                     /gene="patD"
     Protein         1..481
                     /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=51907
     Region          9..480
                     /region_name="ABALDH"
                     /note="1-pyrroline dehydrogenase; TIGR03374"
                     /db_xref="CDD:132417"
     Site            order(66,113,123,127..130,132..133,135,141..142,225,237,
                     240,247,254,419..423,426..427,429,432,434..439,448..450,
                     455..456,461,474..479)
                     /site_type="other"
                     /note="tetrameric interface [polypeptide binding]"
                     /db_xref="CDD:143411"
     Site            order(152..153,155,179,181..182,211,216,230..232,235,238,
                     253,255,287,334,385)
                     /site_type="other"
                     /note="NAD binding site [chemical binding]"
                     /db_xref="CDD:143411"
     Site            order(156,253,284,287)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:143411"
     Site            order(286,445)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:143411"
ORIGIN      
        1 mtiwenamqy qllingvlvd gegerqsvyn patgevilei aeaspaqvda avqaadnafa
       61 ewgqttpkar aecllklads ieqnalefar lesqncgkpl hcvindeipa ivdvfrffag
      121 aarclsglaa geyleghtsm irrdpigvva siapwnyplm maawklapal aagncvvikp
      181 seitpltalk lavlakdifp pgvlnvlfgr gqtvgdvltg hekvrmvslt gsiatgehil
      241 rhtapaikrt hmelggkapv ivfddadlda vaqgvrtfgf ynagqdctaa criyaqrgiy
      301 dalveklgna vsslkmgape destelgpls slahlkrvta aveeakalsh irvitggsqt
      361 egkgyyfapt lladakqeda ivqrevfgpv vsitvfdded qvlrwandsr yglassvwtq
      421 dvgrahrlsa rlqygctwin thfmlvsemp hggqkqsgyg kdmslygled ytlvrhimvk
      481 h