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Database: UniProt
Entry: S6AVS5_PSERE
LinkDB: S6AVS5_PSERE
Original site: S6AVS5_PSERE 
ID   S6AVS5_PSERE            Unreviewed;       670 AA.
AC   S6AVS5;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   24-JAN-2024, entry version 43.
DE   SubName: Full=2,4-dienoyl-CoA reductase {ECO:0000313|EMBL:BAN48576.1};
DE            EC=1.3.1.34 {ECO:0000313|EMBL:BAN48576.1};
GN   Name=fadH {ECO:0000313|EMBL:BAN48576.1};
GN   ORFNames=PCA10_28440 {ECO:0000313|EMBL:BAN48576.1};
OS   Pseudomonas resinovorans NBRC 106553.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=1245471 {ECO:0000313|EMBL:BAN48576.1, ECO:0000313|Proteomes:UP000015503};
RN   [1] {ECO:0000313|EMBL:BAN48576.1, ECO:0000313|Proteomes:UP000015503}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 106553 {ECO:0000313|EMBL:BAN48576.1,
RC   ECO:0000313|Proteomes:UP000015503};
RX   PubMed=23887915; DOI=10.1128/genomeA.00488-13;
RA   Shintani M., Hosoyama A., Ohji S., Tsuchikane K., Takarada H., Yamazoe A.,
RA   Fujita N., Nojiri H.;
RT   "Complete Genome Sequence of the Carbazole Degrader Pseudomonas
RT   resinovorans Strain CA10 (NBRC 106553).";
RL   Genome Announc. 1:e00488-13(2013).
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210;
CC         Evidence={ECO:0000256|ARBA:ARBA00001917};
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DR   EMBL; AP013068; BAN48576.1; -; Genomic_DNA.
DR   RefSeq; WP_016492768.1; NC_021499.1.
DR   AlphaFoldDB; S6AVS5; -.
DR   STRING; 1245471.PCA10_28440; -.
DR   KEGG; pre:PCA10_28440; -.
DR   PATRIC; fig|1245471.3.peg.2880; -.
DR   eggNOG; COG0446; Bacteria.
DR   eggNOG; COG1902; Bacteria.
DR   HOGENOM; CLU_012153_1_2_6; -.
DR   OrthoDB; 8523426at2; -.
DR   Proteomes; UP000015503; Chromosome.
DR   GO; GO:0008670; F:2,4-dienoyl-CoA reductase (NADPH) activity; IEA:UniProtKB-EC.
DR   GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR   CDD; cd02803; OYE_like_FMN_family; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR023753; FAD/NAD-binding_dom.
DR   InterPro; IPR001155; OxRdtase_FMN_N.
DR   PANTHER; PTHR42917; 2,4-DIENOYL-COA REDUCTASE; 1.
DR   PANTHER; PTHR42917:SF2; 2,4-DIENOYL-COA REDUCTASE [(2E)-ENOYL-COA-PRODUCING]; 1.
DR   Pfam; PF00724; Oxidored_FMN; 1.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   PRINTS; PR00368; FADPNR.
DR   PRINTS; PR00469; PNDRDTASEII.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   SUPFAM; SSF51395; FMN-linked oxidoreductases; 1.
PE   4: Predicted;
KW   Oxidoreductase {ECO:0000313|EMBL:BAN48576.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000015503}.
FT   DOMAIN          9..338
FT                   /note="NADH:flavin oxidoreductase/NADH oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00724"
FT   DOMAIN          389..624
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
SQ   SEQUENCE   670 AA;  72547 MW;  4ED09771590D848A CRC64;
     MPDAPYPNLF QDLVLRNLRI PNRTVMAPMS TNLGSHEGFV TPEQIAFYRE RAAGGTGMII
     VEFCCVEGAT GRSEHRQLTL ESPAQVAGHQ RLVEAITSAG AVACLQLQHG GRGAKRDLLS
     DGMPIAPSDV ATRSGRLMAR AMDDAEIERL IEAFGRAAEL GVQAGYQAVE LHGAHGYLLT
     SFLSPYSNQR TDRWGGDEER RLNFPRRVIQ RVRQSIGDRP LIFRLSADEF TPEGLSIEDM
     ERIAPKLEAA GVDALHVSIG LGWTSFDKVV EPMSTPEGWR LPYSRRIRAV TGIPVISVGQ
     IRWPETAERA IRDGDADMIA LGRPLLADPE WANKARRGER DCIRPCTSCN YCVAVSSAAD
     GAIGCAENPR TGHELDSLPD AGSRRGQRAV VIGGGPGGMA AALMLQQAGF TTELHESRSI
     LGGGLIASAA PPFKDKLTWY LDYLHRQLEK SAVEVHLDSR VDLAGLIQGE APAIVMLATG
     GQPIRMPIAG VDGPAVRDAY DLLMGDSPRL PVEIGEWPVL VYGGGETGCE TAELLSEQGH
     EVVLVSRSPV EQLARSAEMI YRGVLKRRLL ENPRIHIQDN ASIERIDHDG RVLLRHQDGG
     SSELQTSAVL IAQGRRPDES LLRSLLEANL PVTVIGDARR GGRIGDAVHD AYRAVHSLCS
     SAAPLRPLAC
//
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