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

LOCUS       WP_004181395             673 aa            linear   BCT 28-MAR-2023
            [Klebsiella].
ACCESSION   WP_004181395
VERSION     WP_004181395.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella
  ORGANISM  Klebsiella
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Klebsiella/Raoultella group.
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..673
                     /organism="Klebsiella"
                     /db_xref="taxon:570"
     Protein         1..673
                     /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=72090
     Region          7..359
                     /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(26,28,60,102,166,168,177,216,254,257,312..313,336,
                     339,343,355)
                     /site_type="active"
                     /db_xref="CDD:239240"
     Site            order(26,28,60,102,216,312..313)
                     /site_type="other"
                     /note="FMN binding site [chemical binding]"
                     /db_xref="CDD:239240"
     Site            order(166,168,177,254,257)
                     /site_type="other"
                     /note="2,4-decadienoyl-CoA binding site"
                     /db_xref="CDD:239240"
     Site            168
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:239240"
     Site            order(336,339,343,355)
                     /site_type="other"
                     /note="4Fe-4S cluster binding site [ion binding]"
                     /db_xref="CDD:239240"
     Region          <376..>513
                     /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          401..>653
                     /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 msrypslfap lelgfttlkn rvlmgsmhtg leelpdgaqr laafyaerar hgvalivtgg
       61 iapapsgvtm aggavlndas hlahhrhitd avhqeggkia lqilhtgrys yqpalvapsa
      121 lqapinrftp helshdeilt liddfahcaq lareagydgv evmgsegyli neflaartnq
      181 rddqwggdya rrmrfavevv kavrqraghd fiiiyrlsml dlvndgstla evtelakaie
      241 aagatiintg igwheaript iatpvprgaf swvtrklkga vsiplittnr indpqvaedi
      301 largdadmvs marpfladae fiskaqddra dqintcigcn qacldrifvg kvtsclvnpr
      361 achetlmpvl panapkrlav vgagpaglaf avnaaarghh vtlfdalpei ggqfniakqi
      421 pgkeefhetl ryyrtmldlh gvdlrlntrv ttddllafde tilatgiapr lpaidgidhp
      481 kvlsyldvlr dkapvgakva iigcggigfd tamflsqsga atsqdigefc rewgidtslq
      541 tagglsaegp qlsksprqiv mlqrkaskpg eglgkttgwi hratllargv kmipavsyek
      601 iddeglhvti ggerqllavd qvvicagqep rreladplra agktvhligg cdvaaeldar
      661 raiaqgtkla lai