MULTISPECIES: 2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD

LOCUS       WP_002901621             253 aa            linear   BCT 01-JUL-2024
            [Klebsiella].
ACCESSION   WP_002901621
VERSION     WP_002901621.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella
  ORGANISM  Klebsiella
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Klebsiella/Raoultella group.
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 :: TIGR01832.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..253
                     /organism="Klebsiella"
                     /db_xref="taxon:570"
     gene            1..253
                     /gene="kduD"
     Protein         1..253
                     /product="2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase
                     KduD"
                     /EC_number="1.1.1.127"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /GO_process="GO:0000272 - polysaccharide catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=26804
     Region          1..253
                     /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(17,19..22,41..43,64..66,92..95,115,143..145,158,162,
                     188..191,193..196)
                     /site_type="other"
                     /note="NADP binding site [chemical binding]"
                     /db_xref="CDD:187605"
     Site            order(69,100..104,106,109..110,113,118,121..122,125,128,
                     147..149,155..156,159..160,163..164,167..168,170..172,
                     174..176)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:187605"
     Site            order(116,145,158,162)
                     /site_type="active"
                     /db_xref="CDD:187605"
ORIGIN      
        1 mvlnafdltg kvaivtgcdt glgqgmtlgl aqagcdivgi nrkiphdtaa qvlalgrrfh
       61 aiqadlsqen dmsglvdqav aamgrvdilv nnagiirrhd altftesdwd avidlnlkav
      121 fflsqavarq firqgeggki iniasmlsfq ggirvpsyta sksgvlgltr llanewagqg
      181 invnaiapgy matnntqalr edeernqail eripagrwgv pkdlqgpvvf lassaadyin
      241 gytlavdggw lar