NAD-dependent succinate-semialdehyde dehydrogenase [Listeria

LOCUS       WP_010989613             488 aa            linear   BCT 29-MAR-2023
            monocytogenes].
ACCESSION   WP_010989613
VERSION     WP_010989613.1
KEYWORDS    RefSeq.
SOURCE      Listeria monocytogenes
  ORGANISM  Listeria monocytogenes
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Listeriaceae;
            Listeria.
REFERENCE   1  (residues 1 to 488)
  AUTHORS   Marchitti,S.A., Brocker,C., Stagos,D. and Vasiliou,V.
  TITLE     Non-P450 aldehyde oxidizing enzymes: the aldehyde dehydrogenase
            superfamily
  JOURNAL   Expert Opin Drug Metab Toxicol 4 (6), 697-720 (2008)
   PUBMED   18611112
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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10162917
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..488
                     /organism="Listeria monocytogenes"
                     /db_xref="taxon:1639"
     Protein         1..488
                     /product="NAD-dependent succinate-semialdehyde
                     dehydrogenase"
                     /EC_number="1.2.1.-"
                     /calculated_mol_wt=53036
     Region          32..484
                     /region_name="ALDH_F5_SSADH_GabD"
                     /note="Mitochondrial succinate-semialdehyde dehydrogenase
                     and ALDH family members 5A1 and 5F1-like; cd07103"
                     /db_xref="CDD:143421"
     Site            order(70,79,120,123..124,126..134,139..141,146,228,240,
                     244,247,304,308,353,425,427..428,432,434,437,439..445,451,
                     454..455,461,466,478..484)
                     /site_type="other"
                     /note="tetramerization interface [polypeptide binding]"
                     /db_xref="CDD:143421"
     Site            order(154..158,166,181,183..184,232..235,238,241..242,
                     256..258,290,390,392,418,456)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:143421"
     Site            order(158,256,287,290)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:143421"
ORIGIN      
        1 msiketalpk vqtklfingk wtdgdnketk divnpangdv iakiaqagps etkkaikaak
       61 dafpdwakme ladrvkllhk iadlmeekad tlakimtleq gkplkeskge vltgvenfrf
      121 aaeearrlyg etipapnnha fivkkqpigv vaaitpwnfp ggmvtrklap alatgntivl
      181 kpsgdtplsa laifeifeea glpkgvaniv mgsskeiget ltdsddvrkl tftgstkvgq
      241 tlfkqsadtl kkislelggh apfivfddan ldaavndlva akfrnngqvc vspnrifvak
      301 eikekftkal vakveqlkvg nglddvnvgp liredaidki dkqlknatek gakvltgggr
      361 ltgsdydkgn fykptvldnv trkmdifyee tfgpviplit fetedeaiem andsefglas
      421 yfytkdlarv ekvgaaleyg mvganeiais npetpfggvk hsgfgrengh ygmeeyiqvk
      481 finlkyrd