molybdopterin-dependent oxidoreductase [Klebsiella pneumoniae].

LOCUS       WP_002906463             195 aa            linear   BCT 26-FEB-2025
ACCESSION   WP_002906463
VERSION     WP_002906463.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella pneumoniae
  ORGANISM  Klebsiella pneumoniae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Klebsiella/Raoultella group;
            Klebsiella; Klebsiella pneumoniae complex.
REFERENCE   1  (residues 1 to 195)
  AUTHORS   Schneider,F., Lowe,J., Huber,R., Schindelin,H., Kisker,C. and
            Knablein,J.
  TITLE     Crystal structure of dimethyl sulfoxide reductase from Rhodobacter
            capsulatus at 1.88 A resolution
  JOURNAL   J Mol Biol 263 (1), 53-69 (1996)
   PUBMED   8890912
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 :: NF012602.6
            Evidence Source    :: EMBL-EBI
            Source Identifier  :: PF00384.27
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..195
                     /organism="Klebsiella pneumoniae"
                     /db_xref="taxon:573"
     Protein         1..195
                     /product="molybdopterin-dependent oxidoreductase"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=21370
     Region          2..>195
                     /region_name="Molybdopterin-Binding"
                     /note="Molybdopterin-Binding (MopB) domain of the MopB
                     superfamily of proteins, a large, diverse, heterogeneous
                     superfamily of enzymes that, in general, bind
                     molybdopterin as a cofactor. The MopB domain is found in a
                     wide variety of molybdenum- and...; cl09928"
                     /db_xref="CDD:447860"
ORIGIN      
        1 mdvsrrkffk icaggmagtt aaalgfapkm alaqarnfkl lrakeirntc tycsvgcgll
       61 myslgdgakn akeaiyhieg dpdhpvsrga lcpkgaglld yvhsenrlry pqyrapgsdk
      121 wqriswdeaf nriarlmkad rdanfiekne qgvtvnrwls tgmlcasaas netgmltqkf
      181 vrslgmlavd nqarv