MULTISPECIES: ferredoxin--NADP reductase [Enterovibrio].

LOCUS       WP_016961930             247 aa            linear   BCT 28-AUG-2024
ACCESSION   WP_016961930
VERSION     WP_016961930.1
KEYWORDS    RefSeq.
SOURCE      Enterovibrio
  ORGANISM  Enterovibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
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 10153094
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..247
                     /organism="Enterovibrio"
                     /db_xref="taxon:188143"
     Protein         1..247
                     /product="ferredoxin--NADP reductase"
                     /EC_number="1.18.1.2"
                     /GO_function="GO:0004324 - ferredoxin-NADP+ reductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=27838
     Region          9..246
                     /region_name="FNR1"
                     /note="Ferredoxin-NADP+ (oxido)reductase is an
                     FAD-containing enzyme that catalyzes the reversible
                     electron transfer between NADP(H) and electron carrier
                     proteins such as ferredoxin and flavodoxin. Isoforms of
                     these flavoproteins (i.e. having a non-covalently...;
                     cd06195"
                     /db_xref="CDD:99792"
     Site            order(36,50..53,66,68,70,73,75..76,116,246)
                     /site_type="other"
                     /note="FAD binding pocket [chemical binding]"
                     /db_xref="CDD:99792"
     Site            order(50,52..53)
                     /site_type="other"
                     /note="FAD binding motif [chemical binding]"
                     /db_xref="CDD:99792"
     Site            order(73,76,79,85,94,96)
                     /site_type="other"
                     /note="phosphate binding motif [ion binding]"
                     /db_xref="CDD:99792"
     Site            order(111,115..118,120)
                     /site_type="other"
                     /note="beta-alpha-beta structure motif"
                     /db_xref="CDD:99792"
     Site            order(116..117,142..144,213..214)
                     /site_type="other"
                     /note="NAD binding pocket [chemical binding]"
                     /db_xref="CDD:99792"
ORIGIN      
        1 matwikaevi enrrwnkdlf sltldadvap fvagqfaklg leidgkliqr aysyvnppss
       61 kyleiyatrv adgllsprlh eleagdnvmi tkdatgfftl eeipqgehlw mistgtalgp
      121 flsilqeeev wqrfrkvvli havrfsadls yqaeinelkk khsdqilvqp fvsrepkaga
      181 lsgrithale dgmlervvgi pltpeksqim lcgnpqmvkd vralleqkgl eknlrrkpgh
      241 itteqyw