ID   A0A0F2RY76_9RHOB        Unreviewed;       657 AA.
AC   A0A0F2RY76;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   SubName: Full=Oxidoreductase {ECO:0000313|EMBL:KJS42976.1};
GN   ORFNames=VR71_12330 {ECO:0000313|EMBL:KJS42976.1};
OS   Roseovarius sp. BRH_c41.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Roseovarius.
OX   NCBI_TaxID=1629709 {ECO:0000313|EMBL:KJS42976.1, ECO:0000313|Proteomes:UP000033676};
RN   [1] {ECO:0000313|EMBL:KJS42976.1, ECO:0000313|Proteomes:UP000033676}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BRH_c41 {ECO:0000313|EMBL:KJS42976.1};
RA   Bagnoud A., Chourey K., Hettich R.L., de Bruijn I., Andersson A.F.,
RA   Leupin O.X., Schwyn B., Bernier-Latmani R.;
RT   "Microbial metabolic network in the subsurface.";
RL   Submitted (MAR-2015) 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:KJS42976.1}.
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DR   EMBL; LADY01000039; KJS42976.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0F2RY76; -.
DR   PATRIC; fig|1629709.5.peg.4546; -.
DR   Proteomes; UP000033676; Unassembled WGS sequence.
DR   GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   CDD; cd04734; OYE_like_3_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          10..343
FT                   /note="NADH:flavin oxidoreductase/NADH oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00724"
FT   DOMAIN          394..496
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
SQ   SEQUENCE   657 AA;  70048 MW;  A2499ECA22AA5855 CRC64;
     MPNAPFYPRL FAPLTLGGFE IRNRIASTGH QTFLAENNLP GGALVAYHEA RARGGAGLII
     TEAARFHESA FAAPRELHLV EDSAIPAYAR LAKVVQGHGA RIIGQLSHSG RVSHRMREGH
     RGVAFAPSPV PDRRYQTVPR QMSTELIEEL VSTIGTGAQR YAEAGYDGVE LMASHGLLFA
     QFLNPDANRR TDAYGGTLDN RMRFLCESLA EVRRKIRIGM VIGLRISAED FEADGTEPDV
     IESACSYLAK TGAIDYLNVT AGSMAGLGGS IHVVPPMEIA SAYLASHAGR LRAATSLPIL
     VAGRINQPQE AEQVLAGNYA DICGMTRAMI TDPELASKAR SGRGESIKAC IGCNQACIGH
     LHKGVGISCI QSPLSGREAR FAPALAEPAR IPGRILVVGG GPAGMRAAVT AAQRGHNVLL
     MEAAPMLGGQ ALLAQRLPER AEFGGLITNL EMELASANVE IRMRQFVDRA MIEAEAPDAL
     ILATGARPAP LEIEIEDDRS PVLAVEVLQG TAQVRGRVVI ADWRCDWVGI GTAAHLAAKG
     HHVRLAVDGV CAGQNLPTYV RDYWAGRLHA LGVEVIPYAR AFGMDADTAY FSQSVTGAPI
     LFEGVDDLVI SGPYLPDTRL EDTLSGLNIR ISRAGDCLSP RTAEEAVYEG FLAGLEA
//