MULTISPECIES: NAD(P)H-quinone oxidoreductase [Klebsiella].

LOCUS       WP_004140406             326 aa            linear   BCT 31-DEC-2024
ACCESSION   WP_004140406
VERSION     WP_004140406.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella
  ORGANISM  Klebsiella
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Klebsiella/Raoultella group.
REFERENCE   1  (residues 1 to 326)
  AUTHORS   Persson,B., Hedlund,J. and Jornvall,H.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the MDR superfamily
  JOURNAL   Cell Mol Life Sci 65 (24), 3879-3894 (2008)
   PUBMED   19011751
REFERENCE   2  (residues 1 to 326)
  AUTHORS   Nordling,E., Jornvall,H. and Persson,B.
  TITLE     Medium-chain dehydrogenases/reductases (MDR). Family
            characterizations including genome comparisons and active site
            modeling
  JOURNAL   Eur J Biochem 269 (17), 4267-4276 (2002)
   PUBMED   12199705
REFERENCE   3  (residues 1 to 326)
  AUTHORS   Lesk,A.M.
  TITLE     NAD-binding domains of dehydrogenases
  JOURNAL   Curr Opin Struct Biol 5 (6), 775-783 (1995)
   PUBMED   8749365
REFERENCE   4  (residues 1 to 326)
  AUTHORS   Persson,B., Zigler,J.S. Jr. and Jornvall,H.
  TITLE     A super-family of medium-chain dehydrogenases/reductases (MDR).
            Sub-lines including zeta-crystallin, alcohol and polyol
            dehydrogenases, quinone oxidoreductase enoyl reductases, VAT-1 and
            other proteins
  JOURNAL   Eur J Biochem 226 (1), 15-22 (1994)
   PUBMED   7957243
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 10143004
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..326
                     /organism="Klebsiella"
                     /db_xref="taxon:570"
     Protein         1..326
                     /product="NAD(P)H-quinone oxidoreductase"
                     /EC_number="1.6.5.5"
                     /GO_function="GO:0003960 - NADPH:quinone reductase
                     activity [Evidence IEA]"
                     /GO_function="GO:0048038 - quinone binding [Evidence IEA]"
                     /GO_function="GO:0070402 - NADPH binding [Evidence IEA]"
                     /calculated_mol_wt=34441
     Region          1..322
                     /region_name="p53_inducible_oxidoreductase"
                     /note="PIG3 p53-inducible quinone oxidoreductase; cd05276"
                     /db_xref="CDD:176180"
     Site            order(40..41,122,126,129,147,150..152,171..172,176,189,
                     213..214,235..236,238,261..263,311,316)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:176180"
ORIGIN      
        1 mkyiaisqpg gpevlqireg eiptigehev lievkaagvn rpdilqrqgl ypmpegvtpv
       61 pglevagvvv kvgaqvtaft pgdrvcaltn gggyaeycav pagqtlpipa glsfseaaai
      121 petfftvwan vfqlgklqpg esilvhggas gigttavllc halgmtvyat vgqdekiaal
      181 rpyatainyk tddfaekigq ltndegvdvi ldivggpyfn rnlgllkkdg rlviigfmgg
      241 riahevdiqt lmlkratvtg stmrgrtaae kqqiaealrr hvwplleagk ckpliyasyp
      301 maeiaeahac ldsgqhlgkv vitmts