ID A0A1D8YBV4_9GAMM Unreviewed; 677 AA.
AC A0A1D8YBV4;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=NADPH-dependent 2,4-dienoyl-CoA reductase {ECO:0000313|EMBL:AOX63084.1};
GN ORFNames=BIZ42_13235 {ECO:0000313|EMBL:AOX63084.1};
OS Stenotrophomonas sp. LM091.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Stenotrophomonas.
OX NCBI_TaxID=1904944 {ECO:0000313|EMBL:AOX63084.1, ECO:0000313|Proteomes:UP000177427};
RN [1] {ECO:0000313|EMBL:AOX63084.1, ECO:0000313|Proteomes:UP000177427}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LM091 {ECO:0000313|EMBL:AOX63084.1,
RC ECO:0000313|Proteomes:UP000177427};
RA Lefeuvre P.;
RT "Complete genome sequence of a copper-resistant commensal bacteria:
RT Stenotrophomonas sp. strain LM091.";
RL Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000256|ARBA:ARBA00001917};
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DR EMBL; CP017483; AOX63084.1; -; Genomic_DNA.
DR RefSeq; WP_070426697.1; NZ_CP017483.1.
DR AlphaFoldDB; A0A1D8YBV4; -.
DR STRING; 1904944.BIZ42_13235; -.
DR KEGG; slm:BIZ42_13235; -.
DR OrthoDB; 8523426at2; -.
DR Proteomes; UP000177427; Chromosome.
DR GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; 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 SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF51395; FMN-linked oxidoreductases; 1.
DR SUPFAM; SSF51971; Nucleotide-binding domain; 1.
PE 4: Predicted;
FT DOMAIN 13..336
FT /note="NADH:flavin oxidoreductase/NADH oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00724"
FT DOMAIN 383..652
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
SQ SEQUENCE 677 AA; 72716 MW; 9F71EE50C2E52954 CRC64;
MSPAAESAAY PHLFAPLDLG FTQLRNRVLM GSMHTGLEDR ARDFPRLAAY FAERAAGGVG
LIVTGGFAPN VVGWLKPFGG KLSWPWEVRP HRQVTRAVHD NGSRICLQLL HAGRYAYHPL
SVAPSRLKAP INPFTPRALS ARGVDRHIAD YARSARLARE AGYDGVEVMG SEGYLINEFI
APRTNQRNDR WGGDAAQRMR FAVEIVRRIR EACGPDFIII YRLSLVDLVP DGSNWAEIVQ
QAQAIEAVGA TLINSGIGWH EARIPTIATS VPRGAFAGVT AKLKPHVRVP VIATNRINMP
DVAERILAAG GADMVSLARP LLADPQWANK SRAGRPEAIN TCIACNQACL DHVFENKTAS
CLVNPRAVHE TELVYRPTTA PRRIAVVGAG PAGLACATVA AERGHAVTLF DAGSEIGGQF
NVAKRIPGKE EFHETLRYFR HKLDETGVDV KLDTVADVAA LANFDEVVIA TGITPRRVDF
PGADHPKVVT YLDVLLGRVR VGEQVAIIGA GGIGFDVGEF LVHEGPSSAL DPARWMAEWG
VDPSFEGRGA LARPAPEPPA RKVWLLQRSP GKPGARLGKT TGWIHRATLK AKGVSMLGGV
EYLGVDDSGL RIRVEGEEQL LPVSHVVVCA GQEPRRDLHA ALQAAGITAQ LIGGADVAAE
LDAKRAINQG SRVAAAL
//
