ID   A0A2M9IYG8_9ACTN        Unreviewed;       420 AA.
AC   A0A2M9IYG8;
DT   25-APR-2018, integrated into UniProtKB/TrEMBL.
DT   25-APR-2018, sequence version 1.
DT   24-JAN-2024, entry version 12.
DE   SubName: Full=FAD-dependent oxidoreductase {ECO:0000313|EMBL:PJM99679.1};
GN   ORFNames=CG740_29575 {ECO:0000313|EMBL:PJM99679.1};
OS   Streptomyces sp. CB01201.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=2020324 {ECO:0000313|EMBL:PJM99679.1, ECO:0000313|Proteomes:UP000231916};
RN   [1] {ECO:0000313|Proteomes:UP000231916}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CB01201 {ECO:0000313|Proteomes:UP000231916};
RA   Pan G., Xu Z., Guo Z., Ma M., Yang D., Zhou H., Gansemans Y., Zhu X.,
RA   Zhao L.-X., Jiang Y., Cheng J., van Nieuwerburgh F., Suh J.W., Duan Y.,
RA   Shen B.;
RT   "Discovery of the Leinamycin Family of Natural Products by Mining
RT   Actinobacterial Genomes.";
RL   Proc. Natl. Acad. Sci. U.S.A. 114:0-0(2017).
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:PJM99679.1}.
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DR   EMBL; NNBJ01000016; PJM99679.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2M9IYG8; -.
DR   OrthoDB; 1145at2; -.
DR   Proteomes; UP000231916; 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; 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;
FT   DOMAIN          8..313
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
FT   DOMAIN          333..418
FT                   /note="Reductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF14759"
SQ   SEQUENCE   420 AA;  45126 MW;  D492E215912F4A22 CRC64;
     MVDADRTFVI VGGGLAGAKA AETLRSEGFN GRVILIGDER EHPYERPPLS KGFLSGKDER
     DSVFVHEVAW YAQHDIELHL GQTVTTIDRA AKTVRLGDGT LIQYDRLLLA TGAEPRRLDV
     PGTDLAGVHH LRRLAHSERL RHVLKALGRD NGHLVISGAG WIGLEVAAAA RGYGAEVTVV
     EPEATPLHNV LGPELGQLFA DLHAEHGVRF HFGARLTEIV GQDGLVLAAR TDDGEEHLAH
     DVLAAIGAAP RTSLAENAGL ALADRAHGGG IAVDASLRTS DPDIFAAGDV AAVHHPLLDT
     RLRVEHWANA LNGGPAAARA MLDQHVTYDR VPYFFSDQYD LGLEYSGWAP PGSYDQVVIR
     GDAGKREFIA FWLKDRRVLA GMNVNVWDVT EPIQALIRGG AQVDTEALAD PSVALDSLAP
//