alkene reductase [Pseudomonas aeruginosa].

LOCUS       WP_003114006             369 aa            linear   BCT 31-DEC-2024
ACCESSION   WP_003114006
VERSION     WP_003114006.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas aeruginosa
  ORGANISM  Pseudomonas aeruginosa
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 369)
  AUTHORS   Odat,O., Matta,S., Khalil,H., Kampranis,S.C., Pfau,R.,
            Tsichlis,P.N. and Makris,A.M.
  TITLE     Old yellow enzymes, highly homologous FMN oxidoreductases with
            modulating roles in oxidative stress and programmed cell death in
            yeast
  JOURNAL   J Biol Chem 282 (49), 36010-36023 (2007)
   PUBMED   17897954
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 10121216
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..369
                     /organism="Pseudomonas aeruginosa"
                     /db_xref="taxon:287"
     Protein         1..369
                     /product="alkene reductase"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39501
     Region          5..346
                     /region_name="OYE_like_FMN"
                     /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...;
                     cd02933"
                     /db_xref="CDD:239243"
     Site            order(24,26,58,100,233,300,320,322..324)
                     /site_type="other"
                     /note="FMN binding site [chemical binding]"
                     /db_xref="CDD:239243"
     Site            order(24,26,58,100,102,109,181,184,186,233,240,300,320,
                     322..323)
                     /site_type="active"
                     /db_xref="CDD:239243"
     Site            order(26,102,181,184,186,323)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:239243"
     Site            186
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:239243"
ORIGIN      
        1 msnlllspla vgnlalrnri vmapmtrsra qqpgdvptal nalyyaqrag aglivsegtq
       61 ishlgqgyay tpgiyseaql agwrqvteav haaggliaaq lwhvgrmshr slqaggeapi
      121 apspiqakaq vfiadgqggg smapadapre mtledirrvr defvraarna ldagfdlvel
      181 hgangylidq flasasnrrs dayggslenr arflleivda lvaavgaerv glrlspwgti
      241 ndmhddepea mtlylaealq rrgiaylhla ewewsggpay pqgfrerlre rfraplivcg
      301 nydaeraeai lqagladava igrpfianpd lverirlgap laeanqarfy ggdaagytdy
      361 ptlgqsata