MULTISPECIES: alkene reductase [Pseudomonas].

LOCUS       WP_003103810             350 aa            linear   BCT 01-JAN-2025
ACCESSION   WP_003103810
VERSION     WP_003103810.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 350)
  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..350
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..350
                     /product="alkene reductase"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=37666
     Region          3..332
                     /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(23,25,56,98,225,286,306,308..310)
                     /site_type="other"
                     /note="FMN binding site [chemical binding]"
                     /db_xref="CDD:239243"
     Site            order(23,25,56,98,100,107,173,176,178,225,232,286,306,
                     308..309)
                     /site_type="active"
                     /db_xref="CDD:239243"
     Site            order(25,100,173,176,178,309)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:239243"
     Site            178
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:239243"
ORIGIN      
        1 matlfdpivl gdlelpnriv mapltrcrad egrvpnalma eyyaqradag lilseatavt
       61 pmgvgypdtp giwsddqvrg wsnvtkavha aggriflqlw hvgrisdply lngelpvaps
      121 aiaaeghvsl vrpkrpyvtp raldteeiad iveayrqgae rakaagfdgv eihgangyll
      181 dqflqdstnk rtdryggsie nrarlllevt daaisvwgaq rvgvhlapra dshdmgdsnr
      241 letfshvare lgkrgiafic areaqaddsi gvalkkafgg pyianeqftl dsanailakg
      301 dadavafgvp fianpdlver lrqgaelnpp rpetfytggt egyldyptla