MULTISPECIES: SDR family oxidoreductase [Klebsiella].

LOCUS       WP_002915212             369 aa            linear   BCT 02-MAR-2025
ACCESSION   WP_002915212
VERSION     WP_002915212.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella
  ORGANISM  Klebsiella
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Klebsiella/Raoultella group.
REFERENCE   1  (residues 1 to 369)
  AUTHORS   Aarts,M.G., Hodge,R., Kalantidis,K., Florack,D., Wilson,Z.A.,
            Mulligan,B.J., Stiekema,W.J., Scott,R. and Pereira,A.
  TITLE     The Arabidopsis MALE STERILITY 2 protein shares similarity with
            reductases in elongation/condensation complexes
  JOURNAL   Plant J 12 (3), 615-623 (1997)
   PUBMED   9351246
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 :: NF019605.6
            Evidence Source    :: EMBL-EBI
            Source Identifier  :: PF07993.18
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..369
                     /organism="Klebsiella"
                     /db_xref="taxon:570"
     Protein         1..369
                     /product="SDR family oxidoreductase"
                     /calculated_mol_wt=41135
     Region          3..279
                     /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..11,13,34..36,94..96,133..135,163,167,188..191)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:187547"
     Site            order(113,135,163,167)
                     /site_type="active"
                     /db_xref="CDD:187547"
ORIGIN      
        1 mttllitgvt gflggaalek ilhqetrldl lllvradspe aglervkenm rkfniaeekl
       61 amlrqqhill gdlassehfl ndprleqvth vlncaavasf gsnpliwkvn vegtlrlaqr
      121 maqvtglqrf lhvgtamscs pepdslvaes aefreraehl veythsksti eqlmqqqcpt
      181 lplviarpsi vvghthhgcr psssifwvfs mglmlqkfmc smedridvip vdycadallm
      241 llnqplahge vvhisageen svkfaeidra maqaleqapv gdkyaqvsye tlvkmrrelk
      301 gifgpcnerl mlkamrlyga fatlnvrfsn dkllsmgmpk pprftdyidr cvettrglsi
      361 pqqmavdfk