ID   A0A1V0A109_9ACTN        Unreviewed;       408 AA.
AC   A0A1V0A109;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   SubName: Full=FAD-dependent oxidoreductase {ECO:0000313|EMBL:AQZ63873.1};
GN   ORFNames=BKM31_22565 {ECO:0000313|EMBL:AQZ63873.1};
OS   Nonomuraea sp. ATCC 55076.
OC   Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC   Streptosporangiaceae; Nonomuraea.
OX   NCBI_TaxID=1909395 {ECO:0000313|EMBL:AQZ63873.1, ECO:0000313|Proteomes:UP000190797};
RN   [1] {ECO:0000313|Proteomes:UP000190797}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 55076 {ECO:0000313|Proteomes:UP000190797};
RX   PubMed=28626548; DOI=10.1039/c6md00637j;
RA   Nazari B., Forneris C.C., Gibson M.I., Moon K., Schramma K.R.,
RA   Seyedsayamdost M.R.;
RT   "Nonomuraea sp. ATCC 55076 harbours the largest actinomycete chromosome to
RT   date and the kistamicin biosynthetic gene cluster.";
RL   Med. Chem. Commun. 8:780-788(2017).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR   EMBL; CP017717; AQZ63873.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1V0A109; -.
DR   STRING; 1909395.BKM31_22565; -.
DR   KEGG; noa:BKM31_22565; -.
DR   OrthoDB; 1145at2; -.
DR   Proteomes; UP000190797; Chromosome.
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;
KW   Reference proteome {ECO:0000313|Proteomes:UP000190797}.
FT   DOMAIN          7..298
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
FT   DOMAIN          318..403
FT                   /note="Reductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF14759"
SQ   SEQUENCE   408 AA;  43303 MW;  90CEBC2A26A3B12A CRC64;
     MPAPTTFVIA GGGLAAAKAA EALREEGFDG TIVLVGREPH LPYERPPLSK GYLQGGDERQ
     KIFVHDAGWY REHAVDVRTG VTVTAVDPAA HQVTLSGGER LRYDKLLLAT GATPRRLTVP
     GHDRGHVLYL RTVDDSDRLR ATLSTARRIA VVGAGWIGLE TAAAARAAGV AVTVIEQERQ
     PLLGALGPEI GAVFAGLHRE HGVDLRLGAR LAEVTEEGVR LADGSHIDAD AVVAGIGAVP
     DTDLAAAAGL TVDNGVKTTA DLRTSDPDIF AAGDVANAYH PRLGGHVRVE HWANALNQPA
     VAARAMLGKE AAYEELPYFY TDQYDLGMEY LGHVPPGTAH DVVVRGDVRE RAFLAFWLRD
     DRVIAAMNVN IWDQGDQLKA LVLAGSPVER AALADPSVAL ERLVPSGA
//