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MULTISPECIES: NADPH:quinone oxidoreductase family protein


LOCUS       WP_003114042             325 aa            linear   BCT 31-DEC-2024
            [Pseudomonas].
ACCESSION   WP_003114042
VERSION     WP_003114042.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 325)
  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 325)
  AUTHORS   Shimomura,Y., Kakuta,Y. and Fukuyama,K.
  TITLE     Crystal structures of the quinone oxidoreductase from Thermus
            thermophilus HB8 and its complex with NADPH: implication for NADPH
            and substrate recognition
  JOURNAL   J Bacteriol 185 (14), 4211-4218 (2003)
   PUBMED   12837796
REFERENCE   3  (residues 1 to 325)
  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   4  (residues 1 to 325)
  AUTHORS   Lesk,A.M.
  TITLE     NAD-binding domains of dehydrogenases
  JOURNAL   Curr Opin Struct Biol 5 (6), 775-783 (1995)
   PUBMED   8749365
REFERENCE   5  (residues 1 to 325)
  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 10169523
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..325
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..325
                     /product="NADPH:quinone oxidoreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016655 - oxidoreductase activity, acting
                     on NAD(P)H, quinone or similar compound as acceptor
                     [Evidence IEA]"
                     /GO_function="GO:0048038 - quinone binding [Evidence IEA]"
                     /GO_function="GO:0070402 - NADPH binding [Evidence IEA]"
                     /calculated_mol_wt=33880
     Region          1..323
                     /region_name="QOR1"
                     /note="Quinone oxidoreductase (QOR); cd08241"
                     /db_xref="CDD:176203"
     Site            order(40..41,122,126,147,150..152,171..172,176,191,215,
                     237..238,240..241,262..264,314,316,318)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:176203"
ORIGIN      
        1 mkavlckafg passlvleei aspspaknei lldvhaagvn fpdtliiegk yqfkppfpfs
       61 pggeaagvva avgekvahvr pgdrvmaltg wgsfaeqvkv pgynvmpipe gmdfasaaaf
      121 gmtygtsmha lkqranlqpg etllvlgasg gvglaaveig kamgarviaa astpdklava
      181 kaagadelin ysegslreql kaltggqgvd viydpvggel feeafrsiaw ngrmlvvgfa
      241 sgsipslpan ltllkgaslv gvfwgsfaqr qpqdnadnfr qlfawhaegk lkplvsqrfp
      301 leragdaida lgqrravgkv vvevr