FAD-dependent oxidoreductase [Pseudomonas aeruginosa].

LOCUS       WP_003113937             679 aa            linear   BCT 27-FEB-2025
ACCESSION   WP_003113937
VERSION     WP_003113937.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas aeruginosa
  ORGANISM  Pseudomonas aeruginosa
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 679)
  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..679
                     /organism="Pseudomonas aeruginosa"
                     /db_xref="taxon:287"
     Protein         1..679
                     /product="FAD-dependent oxidoreductase"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=72839
     Region          10..362
                     /region_name="DCR_FMN"
                     /note="2,4-dienoyl-CoA reductase (DCR) FMN-binding domain.
                     DCR in E. coli is an iron-sulfur flavoenzyme which
                     contains FMN, FAD, and a 4Fe-4S cluster. It is also a
                     monomer, unlike that of its eukaryotic counterparts which
                     form homotetramers and lack the...; cd02930"
                     /db_xref="CDD:239240"
     Site            order(29,31,63,105,169,171,180,219,257,260,315..316,339,
                     342,346,358)
                     /site_type="active"
                     /db_xref="CDD:239240"
     Site            order(29,31,63,105,219,315..316)
                     /site_type="other"
                     /note="FMN binding site [chemical binding]"
                     /db_xref="CDD:239240"
     Site            order(169,171,180,257,260)
                     /site_type="other"
                     /note="2,4-decadienoyl-CoA binding site"
                     /db_xref="CDD:239240"
     Site            171
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:239240"
     Site            order(339,342,346,358)
                     /site_type="other"
                     /note="4Fe-4S cluster binding site [ion binding]"
                     /db_xref="CDD:239240"
     Region          399..644
                     /region_name="Pyr_redox_2"
                     /note="Pyridine nucleotide-disulphide oxidoreductase;
                     cl39093"
                     /db_xref="CDD:476868"
ORIGIN      
        1 mtaavpyphl lapldlgftt lrnrtlmgsm htgleekpqg fermaayfae rarggvglmv
       61 tggigpneeg gvysgaakls tpeeaekhri vtqavheagg kicmqilhag ryayspkqva
      121 psaiqapinp fkpkeldeeg iekqiadfvn caslaqvagy dgveimgseg yfinqflvqh
      181 tnqrtdrwgg syenrmrlpv eivrrvreav gpnfiiiyrl smldlveggs swdeivllak
      241 avekagatli ntgigwhear iptiatkvpr aaftkvtakl rgevgiplit tnrintpeva
      301 ekvlaegdad mvsmarpfla dpdfvnkaaa ghaerintci gcnqacldht fggkltsclv
      361 nprachetel nyipttrpkk iavvgagpag laaatvaaer ghrvslfdaa geiggqfnva
      421 krvpgkeefh etlryfrnkl estgvelhln rrvgvddlva ggydeivlat givprtpaip
      481 giehpkvisy ldailerkpv ggkvavigag gigfdvsefi thagpstsle reafwkewgi
      541 dtrlearggi agikaevhpa arqvfllqrk kskvgdglgk ttgwihragl knkqvqmvna
      601 veylriddag lhirvaegep qvlpvdtviv cagqdplrel qdgllaagqs vhliggadva
      661 aeldakrain qgsrlaael