ID   A0A366H139_9BURK        Unreviewed;       407 AA.
AC   A0A366H139;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   24-JAN-2024, entry version 10.
DE   SubName: Full=3-phenylpropionate/trans-cinnamate dioxygenase ferredoxin reductase subunit {ECO:0000313|EMBL:RBP33662.1};
GN   ORFNames=DFR37_12524 {ECO:0000313|EMBL:RBP33662.1};
OS   Eoetvoesiella caeni.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Eoetvoesiella.
OX   NCBI_TaxID=645616 {ECO:0000313|EMBL:RBP33662.1, ECO:0000313|Proteomes:UP000253628};
RN   [1] {ECO:0000313|EMBL:RBP33662.1, ECO:0000313|Proteomes:UP000253628}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 25520 {ECO:0000313|EMBL:RBP33662.1,
RC   ECO:0000313|Proteomes:UP000253628};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT   most valuable type-strain genomes for metagenomic binning, comparative
RT   biology and taxonomic classification.";
RL   Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
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:RBP33662.1}.
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DR   EMBL; QNRQ01000025; RBP33662.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A366H139; -.
DR   Proteomes; UP000253628; Unassembled WGS sequence.
DR   GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   Gene3D; 3.30.390.30; -; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR023753; FAD/NAD-binding_dom.
DR   InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer_sf.
DR   InterPro; IPR028202; Reductase_C.
DR   PANTHER; PTHR43557; APOPTOSIS-INDUCING FACTOR 1; 1.
DR   PANTHER; PTHR43557:SF2; RIESKE DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   Pfam; PF14759; Reductase_C; 1.
DR   PRINTS; PR00368; FADPNR.
DR   PRINTS; PR00411; PNDRDTASEI.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 2.
DR   SUPFAM; SSF55424; FAD/NAD-linked reductases, dimerisation (C-terminal) domain; 1.
PE   4: Predicted;
KW   Dioxygenase {ECO:0000313|EMBL:RBP33662.1};
KW   Oxidoreductase {ECO:0000313|EMBL:RBP33662.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000253628}.
FT   DOMAIN          5..303
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
FT   DOMAIN          322..403
FT                   /note="Reductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF14759"
SQ   SEQUENCE   407 AA;  43704 MW;  64FDF55D0EAF2C49 CRC64;
     MNRGVVVLGG GQAACQLVAS LRQMKYDGTL TMIGDEHALP YQRPPLSKGF LKGEADIASI
     SLRTAEFYQK IGCEMRMGVR AVSINRESQI VELENGDSLG YECLVLATGA RPKTYPGLPI
     ETKNLHYLRT LAHAGQLSES LSKAKKLAII GAGYVGMEVA ASARQLGVEV SIFETAPRVM
     LRSVGPQLAS IIQDIHTRHG VRLNLSAEIK EIKHDALKGS FTIVTGTHGT DDFDLLVIGI
     GAQANTELAV GAGIGCGYGI LVDASCRTSD PAVFAIGDCS EQNHPIYGPG FRLESVQNAV
     DQAKCAAAAI VGGPQPPPSV PWFWSDQYGH RVQVAGLPRH HDVCVIREQT ANEGALTNAG
     SVWYLKDRKV VSVETLDAPK DFMVGRSYIK NNTEVDAERL AKEELLA
//