ID A0A2S4HFS1_9GAMM Unreviewed; 682 AA.
AC A0A2S4HFS1;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE SubName: Full=NADPH-dependent 2,4-dienoyl-CoA reductase {ECO:0000313|EMBL:POP52779.1};
DE EC=1.3.1.34 {ECO:0000313|EMBL:POP52779.1};
GN Name=fadH {ECO:0000313|EMBL:POP52779.1};
GN ORFNames=C0068_10255 {ECO:0000313|EMBL:POP52779.1};
OS Marortus luteolus.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC Spongiibacteraceae; Marortus.
OX NCBI_TaxID=2067667 {ECO:0000313|EMBL:POP52779.1, ECO:0000313|Proteomes:UP000237222};
RN [1] {ECO:0000313|EMBL:POP52779.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ZX-21 {ECO:0000313|EMBL:POP52779.1};
RA Gaut B.S., Morton B.R., Clegg M.T., Duvall M.R.;
RL Submitted (JAN-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000256|ARBA:ARBA00001917};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:POP52779.1}.
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DR EMBL; PQGG01000024; POP52779.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S4HFS1; -.
DR OrthoDB; 8523426at2; -.
DR Proteomes; UP000237222; Unassembled WGS sequence.
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; cd02930; DCR_FMN; 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; PR00411; PNDRDTASEI.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF51395; FMN-linked oxidoreductases; 1.
PE 4: Predicted;
KW Oxidoreductase {ECO:0000313|EMBL:POP52779.1}.
FT DOMAIN 11..336
FT /note="NADH:flavin oxidoreductase/NADH oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00724"
FT DOMAIN 381..648
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
SQ SEQUENCE 682 AA; 73892 MW; 11EE75FFBCA4BF61 CRC64;
MSTENQHYPH LFTPLDLGFT QLKNRVVMGS MHTGLEDRFW QFPKLAAYFA ERAKGGVGLM
ITGGYSPNRS GWLYPGASTF NSRLDIRNHR KVTKAVHQAG GKICLQILHA GRYSYHPLSK
TASTSKAPIN PFKARALSTR GVASTVNDFA RTAQLAQKAG YDGVEIMGSE GYLINQFLAP
ATNKRKDRYG GSPENRRRFA VEIVSAARKK VGPNFIIIFR LSMLDLVPNG CTREEIIDLA
KEIEAAGANL INSGIGWHEA RVPTIVTSVP RAAFSEATAA VKQAVNIPVI ASNRINMPDI
AEHILAKGQA DMVSMARPML ADAEWVNKAA SNRSDQINTC IACNQACLDH TFQLKRASCL
VNPRACHETE LVFKPTTKAK KIAVVGAGPA GLSCATSAAD CGHLVHLFDQ ADKIGGQFNL
AKTIPGKEEF SETLRYFGTQ IDRSGVKLTL NHRVEKAELI SGAYDDVVIA TGVSPRALNI
PGIDHPKVVS YIDVLKGTVT VGKRVALIGA GGIGFDVAEY LAHDHSAESP QSIASWSAEW
GIDQSSAERG GLVTSKPQAS QREIFLLQRK TTALGKDLGK TSGWVHRATL KNKGVNMLAG
CSYDRIDDQG LHISQEGKQR LLEVDHIVIC AGQEPLRELY NSESEQGAKT SPRYHLIGGA
NIASELDAKR AIREGAELAA RL
//
