MULTISPECIES: alkene reductase [Pseudomonas].

LOCUS       WP_003112378             370 aa            linear   BCT 31-DEC-2024
ACCESSION   WP_003112378
VERSION     WP_003112378.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 370)
  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..370
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..370
                     /product="alkene reductase"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39305
     Region          1..348
                     /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(21,23,54,96,235,302,322,324..326)
                     /site_type="other"
                     /note="FMN binding site [chemical binding]"
                     /db_xref="CDD:239243"
     Site            order(21,23,54,96,98,105,183,186,188,235,242,302,322,
                     324..325)
                     /site_type="active"
                     /db_xref="CDD:239243"
     Site            order(23,98,183,186,188,325)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:239243"
     Site            188
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:239243"
ORIGIN      
        1 mlfspytlgh ltlpnrivmp pmtrsraasg evatalmaey ysqragagli vsegtqisrq
       61 gqgyawtpgi hsaeqvagwr qvtdavhaag grifaqlwhv grvshtslqp gnaapvsssa
      121 lvaegvkvfv dpqgrgaqag ggemvqhsap ralaveeire ivadyaqaar naldagfdgv
      181 elhgangyli nqfidsqana rndqyggsle nrlrflreva eavtavvgre rigvrlaplt
      241 tlqgavddtp qatylaaarl ldeigvayih iaeadwedap ampaafkeal rivyrgsliy
      301 sgmytkarae ealargwadl vgfgrpfian pdlpyrlehd laladgdrst yfgggaagyt
      361 dypslpqaag