FAD-dependent oxidoreductase [Pseudomonas aeruginosa].

LOCUS       WP_003114537             648 aa            linear   BCT 01-MAR-2025
ACCESSION   WP_003114537
VERSION     WP_003114537.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas aeruginosa
  ORGANISM  Pseudomonas aeruginosa
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 648)
  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..648
                     /organism="Pseudomonas aeruginosa"
                     /db_xref="taxon:287"
     Protein         1..648
                     /product="FAD-dependent oxidoreductase"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=70080
     Region          5..648
                     /region_name="TIM-like beta/alpha barrel domains"
                     /note="A large family of domains similar to triose
                     phosphate isomerase (TIM) which, in general, share an
                     eight beta/alpha closed barrel structure; cl21457"
                     /db_xref="CDD:473867"
     Site            order(25,27,59,101,173,221,320..321)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:240085"
     Site            order(25,27,59,101,221,320..321)
                     /site_type="other"
                     /note="putative FMN binding site [chemical binding]"
                     /db_xref="CDD:240085"
     Site            order(171,173)
                     /site_type="other"
                     /note="putative substrate binding site [chemical binding]"
                     /db_xref="CDD:240085"
     Site            173
                     /site_type="active"
                     /note="putative catalytic residue [active]"
                     /db_xref="CDD:240085"
ORIGIN      
        1 mnfphlfspl eirgkrlknr imssghdtsm ptdnlvnepl vayhrararg gaglivmqva
       61 gvhdsaryts hvlmatddac ipgyrrvaea chaegcvvls qifhpgreim esadgllava
      121 ysasaspner frvmpreldq plideivagy aaaarrlhqa gldgvevvas hgylpaqfln
      181 prvnrrtdgy ngdldarlrf lrevlaavra atsedfivgl rlsaderdpe glseseslqa
      241 aeavqgeldy lhivagtsas lggaihivpp maiepaylar eastfkarla iplfvtgrin
      301 qpqeaeaila rgqadvcgmt ralicdpqmp nkaeagrsdd vraciacnqa cighfhrgyp
      361 isciqhpetg reltyatpnp asrrkrvlva gggpagmkaa avaaqrghev vlceagaqlg
      421 gqvnlaqllp rraefggast nlqremqlag vevrrntpvd ralvererpd lvivatgaep
      481 ywppfergge lqvvdawqvl rgevrvgrsv lvtdwrgdwi gpgiaeklvr eghqvrlavn
      541 gthcgeslpl yvrdqlagel hrlgipvtpy arlygcddtt vymqhsasge amlfeevdtl
      601 vlcqghqpvd rladslhgla evlrigdcla prtaeeaiye glkaawsi