MULTISPECIES: PDR/VanB family oxidoreductase [Klebsiella].

LOCUS       WP_014343144             322 aa            linear   BCT 01-JAN-2025
ACCESSION   WP_014343144
VERSION     WP_014343144.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella
  ORGANISM  Klebsiella
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Klebsiella/Raoultella group.
REFERENCE   1  (residues 1 to 322)
  AUTHORS   Meyer,J.
  TITLE     Ferredoxins of the third kind
  JOURNAL   FEBS Lett 509 (1), 1-5 (2001)
   PUBMED   11734195
REFERENCE   2  (residues 1 to 322)
  AUTHORS   Mathews,F.S., Cunane,L. and Durley,R.C.
  TITLE     Flavin electron transfer proteins
  JOURNAL   Subcell Biochem 35, 29-72 (2000)
   PUBMED   11192725
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 18977663
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..322
                     /organism="Klebsiella"
                     /db_xref="taxon:570"
     Protein         1..322
                     /product="PDR/VanB family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051537 - 2 iron, 2 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=34218
     Region          13..224
                     /region_name="PDR_like"
                     /note="Phthalate dioxygenase reductase (PDR) is an
                     FMN-dependent reductase that mediates electron transfer
                     from NADH to FMN to an iron sulfur cluster. PDR has an an
                     N-terminal ferrredoxin reductase (FNR)-like NAD(H) binding
                     domain and a C-terminal iron-sulfur...; cd06185"
                     /db_xref="CDD:99782"
     Site            order(53..54,56,70..72,78,80..81,121,223)
                     /site_type="other"
                     /note="FMN-binding pocket [chemical binding]"
                     /db_xref="CDD:99782"
     Site            order(53,55..56)
                     /site_type="active"
                     /note="flavin binding motif [active]"
                     /db_xref="CDD:99782"
     Site            order(78,81,84,91)
                     /site_type="other"
                     /note="phosphate binding motif [ion binding]"
                     /db_xref="CDD:99782"
     Site            order(113,117..120,122)
                     /site_type="other"
                     /note="beta-alpha-beta structure motif"
                     /db_xref="CDD:99782"
     Site            order(118..119,142..144,196..197)
                     /site_type="other"
                     /note="NAD binding pocket [chemical binding]"
                     /db_xref="CDD:99782"
     Region          238..322
                     /region_name="Fdx"
                     /note="Ferredoxin [Energy production and conversion];
                     COG0633"
                     /db_xref="CDD:440398"
ORIGIN      
        1 mhshdlisvs vgeirpngeg nlslilqaaa geilptysag ahidiiipgi gprqyslcgm
       61 pdrgngyevc irltdtstgg srylhqqlka gdrlaisppr nhfplpeagr yllfaggigi
      121 tpllamaeai aarkgglelh yyvasarqta fsprltqlaa ggtvaihcse egasfrqrip
      181 aclttpdpdt avvacgpegf iqrlqsvmee yrwspsqfvf erftpatenn taaknafyie
      241 lassgqrlqv aadqtiaqvl qhagvevmls ceqgmcgsci tgvldgipeh rdsvltaeek
      301 agndqitlcc srakspglvl dl