MULTISPECIES: NADPH-dependent 2,4-dienoyl-CoA reductase

LOCUS       WP_000121523             672 aa            linear   BCT 28-MAR-2023
            [Salmonella].
ACCESSION   WP_000121523
VERSION     WP_000121523.1
KEYWORDS    RefSeq.
SOURCE      Salmonella
  ORGANISM  Salmonella
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
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 11554248
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..672
                     /organism="Salmonella"
                     /db_xref="taxon:590"
     Protein         1..672
                     /product="NADPH-dependent 2,4-dienoyl-CoA reductase"
                     /EC_number="1.3.1.34"
                     /GO_function="GO:0008670 - 2,4-dienoyl-CoA reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051539 - 4 iron, 4 sulfur cluster
                     binding [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0033543 - fatty acid beta-oxidation,
                     unsaturated, even number, reductase/isomerase pathway
                     [Evidence IEA]"
                     /calculated_mol_wt=72999
     Region          6..358
                     /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(25,27,59,101,165,167,176,215,253,256,311..312,335,
                     338,342,354)
                     /site_type="active"
                     /db_xref="CDD:239240"
     Site            order(25,27,59,101,215,311..312)
                     /site_type="other"
                     /note="FMN binding site [chemical binding]"
                     /db_xref="CDD:239240"
     Site            order(165,167,176,253,256)
                     /site_type="other"
                     /note="2,4-decadienoyl-CoA binding site"
                     /db_xref="CDD:239240"
     Site            167
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:239240"
     Site            order(335,338,342,354)
                     /site_type="other"
                     /note="4Fe-4S cluster binding site [ion binding]"
                     /db_xref="CDD:239240"
     Region          <367..>512
                     /region_name="GltD"
                     /note="NADPH-dependent glutamate synthase beta chain or
                     related oxidoreductase [Amino acid transport and
                     metabolism, General function prediction only]; COG0493"
                     /db_xref="CDD:440259"
     Region          400..>652
                     /region_name="FadH2"
                     /note="NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur
                     reductase, or a related oxidoreductase [Lipid transport
                     and metabolism]; COG0446"
                     /db_xref="CDD:440215"
ORIGIN      
        1 msypslfapl dlgfttlrnr vlmgsmhtgl eehpdgaerl aafyaerarh gvalivtggi
       61 apvpsgvvmt ggamlndasq ltphrvvtda vhaqggkial qilhtgrysy qphlvapsai
      121 qapinrfmph elthdeilql iddfahcaql areagydgve vmgsegylin efltrrtnhr
      181 ddewggdyas rmrfavevvr avrqrvgndf iiiyrlsmld lvenggtfde tvqlaqaiea
      241 agaslintgi gwhearipti atpvprgafs wvtrklkghv svpliatnri ndpqvaetil
      301 trgdadmvsm arpfladaef ltkaqsgrad eintcigcnq acldrifigk vtsclvnpra
      361 chethmpitp airkknlavv gagpaglafa inaasrghhv tlfdaqseig gqftiarqip
      421 gkeefyetlr yyrrmidvtg vtlklnqrvn aedlqpfdea ilacgivprr ppidgidhpk
      481 altylevlrd kapvgkrvai igcggigfdt amylsqhges tsqniaefct ewgidtslqq
      541 agglrpegpr larsprqivm lqrktskpge glgkttgwih ratllargvk mipavsyqki
      601 dddglhllig gepqllevdh vvicagqepr reladplraa gktvhliggc dvameldarr
      661 aiaqgtrlal ei