FAD-dependent oxidoreductase [Listeria monocytogenes].

LOCUS       WP_010989931             641 aa            linear   BCT 26-FEB-2025
ACCESSION   WP_010989931
VERSION     WP_010989931.1
KEYWORDS    RefSeq.
SOURCE      Listeria monocytogenes
  ORGANISM  Listeria monocytogenes
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Listeriaceae;
            Listeria.
REFERENCE   1  (residues 1 to 641)
  AUTHORS   Mande,S.S., Sarfaty,S., Allen,M.D., Perham,R.N. and Hol,W.G.
  TITLE     Protein-protein interactions in the pyruvate dehydrogenase
            multienzyme complex: dihydrolipoamide dehydrogenase complexed with
            the binding domain of dihydrolipoamide acetyltransferase
  JOURNAL   Structure 4 (3), 277-286 (1996)
   PUBMED   8805537
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 :: NF019604.6
            Evidence Source    :: EMBL-EBI
            Source Identifier  :: PF07992.20
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..641
                     /organism="Listeria monocytogenes"
                     /db_xref="taxon:1639"
     Protein         1..641
                     /product="FAD-dependent oxidoreductase"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=68700
     Region          7..333
                     /region_name="OYE_like_FMN_family"
                     /note="Old yellow enzyme (OYE)-like FMN binding domain.
                     OYE was the first flavin-dependent enzyme identified,
                     however its true physiological role remains elusive to
                     this day. Each monomer of OYE contains FMN as a
                     non-covalently bound cofactor, uses NADPH as a...;
                     cd02803"
                     /db_xref="CDD:239201"
     Site            order(25,27,60,102,172,220,317..318)
                     /site_type="active"
                     /db_xref="CDD:239201"
     Site            order(25,27,60,102,220,317..318)
                     /site_type="other"
                     /note="FMN binding site [chemical binding]"
                     /db_xref="CDD:239201"
     Site            order(170,172)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:239201"
     Site            172
                     /site_type="active"
                     /note="putative catalytic residue [active]"
                     /db_xref="CDD:239201"
     Region          <401..>495
                     /region_name="GltD"
                     /note="NADPH-dependent glutamate synthase beta chain or
                     related oxidoreductase [Amino acid transport and
                     metabolism, General function prediction only]; COG0493"
                     /db_xref="CDD:440259"
     Region          <460..620
                     /region_name="Pyr_redox_2"
                     /note="Pyridine nucleotide-disulphide oxidoreductase;
                     cl39093"
                     /db_xref="CDD:476868"
ORIGIN      
        1 mkfnsmfspi digpmkvpnr fvvspmcnny antdgtlsdt slayykeral ggfglitfea
       61 tvvdvrakgg ankaclysdh qiasfkrvid vchdagakis vqlqhagpeg nskvsgyplr
      121 aasaiasaag rntpeaisre elyelielyg eaalrakkag adavevhcah gylvssflsa
      181 rtnkrvdefg gcfenrmrlp rliiesirkr vghsiailcr instdgvdgg lsvqdsatva
      241 ayledcgldg lhvsrsvhir deymwaptvl hagfssdlvt qikravsipv itvgrfteph
      301 yaelmvregr adlvafgrqs ladpetpnka aagkldellp ciaclqgcva nmyagkpitc
      361 lvnpllgres eaylpktpsk kvvvvgggvg glyagwmags rghdvtvyea sdmiggqmrl
      421 aayppgkgdl tnmvrsyikk ceqfdveikt ntpvtleliq evapdaviia tgatplvlpi
      481 pgiedaglih avdlldgkek cgqkvlvvgg gmvgsetaaf lgeaghdvtv velrdevgad
      541 visehrkflm hdfdeykiks vtnakvtsff edgvtyslad nkeqridgfd svvlamgsra
      601 ynpleeaika ivpetyvigd avrarralda tkealdavlq l