MULTISPECIES: SDR family NAD(P)-dependent oxidoreductase

LOCUS       WP_004152218             239 aa            linear   BCT 26-FEB-2025
            [Enterobacteriaceae].
ACCESSION   WP_004152218
VERSION     WP_004152218.1
KEYWORDS    RefSeq.
SOURCE      Enterobacteriaceae
  ORGANISM  Enterobacteriaceae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales.
REFERENCE   1  (residues 1 to 239)
  AUTHORS   Yamashita,A., Kato,H., Wakatsuki,S., Tomizaki,T., Nakatsu,T.,
            Nakajima,K., Hashimoto,T., Yamada,Y. and Oda,J.
  TITLE     Structure of tropinone reductase-II complexed with NADP+ and
            pseudotropine at 1.9 A resolution: implication for stereospecific
            substrate binding and catalysis
  JOURNAL   Biochemistry 38 (24), 7630-7637 (1999)
   PUBMED   10387002
REFERENCE   2  (residues 1 to 239)
  AUTHORS   Benach,J., Atrian,S., Gonzalez-Duarte,R. and Ladenstein,R.
  TITLE     The refined crystal structure of Drosophila lebanonensis alcohol
            dehydrogenase at 1.9 A resolution
  JOURNAL   J Mol Biol 282 (2), 383-399 (1998)
   PUBMED   9735295
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 :: NF012334.6
            Evidence Source    :: EMBL-EBI
            Source Identifier  :: PF00106.31
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..239
                     /organism="Enterobacteriaceae"
                     /db_xref="taxon:543"
     Protein         1..239
                     /product="SDR family NAD(P)-dependent oxidoreductase"
                     /calculated_mol_wt=25330
     Region          1..237
                     /region_name="Rossmann-fold NAD(P)(+)-binding proteins"
                     /note="A large family of proteins that share a
                     Rossmann-fold NAD(P)H/NAD(P)(+) binding (NADB) domain. The
                     NADB domain is found in numerous dehydrogenases of
                     metabolic pathways such as glycolysis, and many other
                     redox enzymes. NAD binding involves numerous...; cl21454"
                     /db_xref="CDD:473865"
     Site            order(8,10..11,13,32..34,76..78,124..126,139,143,169..172)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:187608"
     Site            order(100,126,139,143)
                     /site_type="active"
                     /db_xref="CDD:187608"
ORIGIN      
        1 mmtvlitgas sgigaglaks faadghlvia cgrdasrlaa lqqlspnisv rlfdmtdrda
       61 crqaltgcfa dliilcagtc eyldhgqvda alvervmatn flgpvnclaa lqtqleagdr
      121 vvlvssmahw lpfpraeayg askaaltwfa nslrldwepk gvavtvvspg fvdtpltrkn
      181 dfampgrvsv dravaairhg lakgknhiaf ptgfslalrl laslpsgiqr lllrrmvrs