ID   A0A101N609_9ACTN        Unreviewed;       381 AA.
AC   A0A101N609;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   SubName: Full=Pyridine nucleotide-disulfide oxidoreductase {ECO:0000313|EMBL:KUM87150.1};
GN   ORFNames=AQI94_17505 {ECO:0000313|EMBL:KUM87150.1};
OS   Streptomyces pseudovenezuelae.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces; Streptomyces aurantiacus group.
OX   NCBI_TaxID=67350 {ECO:0000313|EMBL:KUM87150.1, ECO:0000313|Proteomes:UP000053039};
RN   [1] {ECO:0000313|EMBL:KUM87150.1, ECO:0000313|Proteomes:UP000053039}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 40212 {ECO:0000313|EMBL:KUM87150.1,
RC   ECO:0000313|Proteomes:UP000053039};
RA   Ruckert C., Winkler A., Kalinowski J., Kampfer P., Glaeser S.;
RT   "Draft genome sequence of Streptomyces pseudovenezuelae DSM 40212, type
RT   strain for the species Streptomyces pseudovenezuelae.";
RL   Submitted (OCT-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:KUM87150.1}.
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DR   EMBL; LMWM01000018; KUM87150.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A101N609; -.
DR   Proteomes; UP000053039; 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          2..289
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
FT   DOMAIN          314..379
FT                   /note="Reductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF14759"
SQ   SEQUENCE   381 AA;  39254 MW;  EEC28D32F6A91672 CRC64;
     MVGASLAGLS AARSLRRQGF DGRLVVIGDE PHRPYDRPPL SKEFLAGSLA EADLALEPDE
     EDLRAEWLLG VRAVGLDGPQ RAVRLADGSE VRADGVVIAT GAAARTLPGT DGLAGVHTLR
     TLDDARALRD ELALGGRLVV IGGGFIGAEV ASTAYALGLD VTVVEAAPTP LAGPLGETMG
     GIVSALHADH GVRLLCGVGV KGLRGGSRVE AVLLADGRSV GADIVVVGVG ARPCVEWLAG
     SGLALGDGVT CGADGRTGLA GVVAVGDCAS WYDPRAGLHR RVEHWTGARE RPDAAVTALL
     AGGAVEPSAP RPPYFWSDQY GVKIQFAGHA AAADSVTIEE GARDEHNVLA VYRRSGHPVA
     VLGMNQPRLF TRWRKQLAAA A
//