NADPH-dependent 2,4-dienoyl-CoA reductase [Photobacterium

LOCUS       WP_008987616             670 aa            linear   BCT 28-MAR-2023
            leiognathi].
ACCESSION   WP_008987616
VERSION     WP_008987616.1
KEYWORDS    RefSeq.
SOURCE      Photobacterium leiognathi
  ORGANISM  Photobacterium leiognathi
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Photobacterium.
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..670
                     /organism="Photobacterium leiognathi"
                     /db_xref="taxon:553611"
     Protein         1..670
                     /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=72972
     Region          9..361
                     /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(28,30,62,104,168,170,179,218,256,259,314..315,338,
                     341,345,357)
                     /site_type="active"
                     /db_xref="CDD:239240"
     Site            order(28,30,62,104,218,314..315)
                     /site_type="other"
                     /note="FMN binding site [chemical binding]"
                     /db_xref="CDD:239240"
     Site            order(168,170,179,256,259)
                     /site_type="other"
                     /note="2,4-decadienoyl-CoA binding site"
                     /db_xref="CDD:239240"
     Site            170
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:239240"
     Site            order(338,341,345,357)
                     /site_type="other"
                     /note="4Fe-4S cluster binding site [ion binding]"
                     /db_xref="CDD:239240"
     Region          398..>626
                     /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 mdnkayphll apldlgfttl rnrvlmgsmh tgleesrdgf kklsafyaar arggvglivt
       61 ggfspnfrgr lhpfsaefss sraarthrti tdavhqeggk ialqllhagr yamspfavsa
      121 sairspiskf tpskmserqi lktidafaks aelareagyd gvelmgsegy linqficqrs
      181 ncryddwggs yenrirfple ivkavrarvg rdfiiifrls mldlveqgst heevvilaka
      241 lekagvtiln tgigwheari ptiatqvpra afawvteklk sevsiplvtc nrintpqvad
      301 dilssgqadm vsmarpflad pefvnkaeqd raddintcig cnqacldhaf vgkrasclvn
      361 pqacyetelv ltptahnrkv avvgagpagm acavaaaerg fsvdlfdknd hvggqfnlam
      421 qipgkeefke tiryftrrla qtgvnvklgh tvtennlsgy deviiatgvk prippipgvd
      481 npkvidyqtl irdkvqlgnk vavigaggig vdvstmltep enqelsqwld ewgidqslen
      541 eggllphddf isprqvwlmq rkpgkvgkgp grttgwihrr tlekrgvell ggvsydkidd
      601 eglhitvegq srllpvdhiv lctgqtsvee lseklvakgn nvnviggade agevdakrvi
      661 rqgvelaakl