MULTISPECIES: PDR/VanB family oxidoreductase [Klebsiella].

LOCUS       WP_002898475             321 aa            linear   BCT 31-DEC-2024
ACCESSION   WP_002898475
VERSION     WP_002898475.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella
  ORGANISM  Klebsiella
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Klebsiella/Raoultella group.
REFERENCE   1  (residues 1 to 321)
  AUTHORS   Meyer,J.
  TITLE     Ferredoxins of the third kind
  JOURNAL   FEBS Lett 509 (1), 1-5 (2001)
   PUBMED   11734195
REFERENCE   2  (residues 1 to 321)
  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..321
                     /organism="Klebsiella"
                     /db_xref="taxon:570"
     Protein         1..321
                     /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=35399
     Region          12..225
                     /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(53,57,59,73..75,81,83..84,125,225)
                     /site_type="other"
                     /note="FMN-binding pocket [chemical binding]"
                     /db_xref="CDD:99782"
     Site            order(53,58..59)
                     /site_type="active"
                     /note="flavin binding motif [active]"
                     /db_xref="CDD:99782"
     Site            order(81,84,87,94)
                     /site_type="other"
                     /note="phosphate binding motif [ion binding]"
                     /db_xref="CDD:99782"
     Site            order(117,121..124,126)
                     /site_type="other"
                     /note="beta-alpha-beta structure motif"
                     /db_xref="CDD:99782"
     Site            order(122..123,146..148,198..199)
                     /site_type="other"
                     /note="NAD binding pocket [chemical binding]"
                     /db_xref="CDD:99782"
     Region          236..321
                     /region_name="Fdx"
                     /note="Ferredoxin [Energy production and conversion];
                     COG0633"
                     /db_xref="CDD:440398"
ORIGIN      
        1 msdyqmfeav vrdveqitpl vkrftlvspt gaplpafsgg shiivqmqdg eqrysnaysl
       61 msspldttsw qiavrlesps kggsrfmhqr vrpgdtltvs tpnnlfaiep qarkhlliag
      121 gigitpflsh ipeleqrqad wqlhycfhda dsnafadals aapwrdrvnv hvsalgsrld
      181 lprlfadlep gthvytcgpa alneavkaaa erhqvpasql hfeqfiledk sgeaftlvla
      241 rsgreftvpq dmtilqvien nkaakveclc regvcgtcet milegeadhr dqyyseeeka
      301 sqqsmliccs rakggrlvld l