ID   A0A0M9YCB3_9ACTN        Unreviewed;       387 AA.
AC   A0A0M9YCB3;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   SubName: Full=Oxidoreductase {ECO:0000313|EMBL:KOU40068.1};
GN   ORFNames=ADK54_23990 {ECO:0000313|EMBL:KOU40068.1};
OS   Streptomyces sp. WM6378.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1415557 {ECO:0000313|EMBL:KOU40068.1, ECO:0000313|Proteomes:UP000037774};
RN   [1] {ECO:0000313|Proteomes:UP000037774}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WM6378 {ECO:0000313|Proteomes:UP000037774};
RA   Ju K.-S., Doroghazi J.R., Metcalf W.W.;
RL   Submitted (JUL-2015) 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:KOU40068.1}.
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DR   EMBL; LGDD01000293; KOU40068.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0M9YCB3; -.
DR   PATRIC; fig|1415557.3.peg.5283; -.
DR   Proteomes; UP000037774; Unassembled WGS sequence.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; 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; PR00469; PNDRDTASEII.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   SUPFAM; SSF55424; FAD/NAD-linked reductases, dimerisation (C-terminal) domain; 1.
PE   4: Predicted;
FT   DOMAIN          1..278
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
FT   DOMAIN          302..385
FT                   /note="Reductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF14759"
SQ   SEQUENCE   387 AA;  40528 MW;  98ABD1888290BF4E CRC64;
     MAGVQTAVAL REQGFAGAIT LIGAEPHQPY DRPPLSKAVL LGKAEGSAFE VDFEALGVDL
     RLGLEVTGVR PAEHVVVTEA GEVGYDTLVI ATGAEPLTLP GSGGVPGVHL LRTLDDARRL
     RPVLDQRHRI VVVGAGWIGA EFATAARDAG CEVTVVEAAD RPLAGVLPAE VAAPMAGWYA
     ESGAELLTGA RVQAVVPGEV LLADGRRLPA DAVVIGIGAR PATGWLTGSD IALGPEGAIT
     ADARLRTSLP DVYAVGDCAS FPSARFGERL LVHHWDNALQ GPRTVAADIV GEAAVDYDPV
     PYFWSEQFGR FVQYAGHHTD ADDVVWRGDP SSAPWSVCWL RDGALVAVLA VGRPRDLAQG
     RKLIESALPL DPTKTADPSV PLKSAVR
//