ID   A0A1D7Y7K7_9ACTN        Unreviewed;       464 AA.
AC   A0A1D7Y7K7;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Flavoprotein oxidoreductase {ECO:0000313|EMBL:AOR31496.1};
GN   ORFNames=BFF78_10965 {ECO:0000313|EMBL:AOR31496.1};
OS   Streptomyces fodineus.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1904616 {ECO:0000313|EMBL:AOR31496.1, ECO:0000313|Proteomes:UP000094960};
RN   [1] {ECO:0000313|Proteomes:UP000094960}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TW1S1 {ECO:0000313|Proteomes:UP000094960};
RA   Kim M.-K., Kim S.B.;
RT   "Streptomyces puniciscabiei strain:TW1S1 Genome sequencing and assembly.";
RL   Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- SIMILARITY: Belongs to the class-III pyridine nucleotide-disulfide
CC       oxidoreductase family. {ECO:0000256|ARBA:ARBA00009130}.
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DR   EMBL; CP017248; AOR31496.1; -; Genomic_DNA.
DR   RefSeq; WP_069778140.1; NZ_CP017248.1.
DR   AlphaFoldDB; A0A1D7Y7K7; -.
DR   KEGG; spun:BFF78_10965; -.
DR   Proteomes; UP000094960; Chromosome.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
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; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
DR   PANTHER; PTHR43429:SF1; COENZYME A DISULFIDE REDUCTASE; 1.
DR   PANTHER; PTHR43429; PYRIDINE NUCLEOTIDE-DISULFIDE OXIDOREDUCTASE DOMAIN-CONTAINING; 1.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   Pfam; PF02852; Pyr_redox_dim; 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   3: Inferred from homology;
FT   DOMAIN          12..304
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
FT   DOMAIN          344..446
FT                   /note="Pyridine nucleotide-disulphide oxidoreductase
FT                   dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF02852"
SQ   SEQUENCE   464 AA;  48868 MW;  04C17F3FDA1ACF86 CRC64;
     MSMGDGRGGA ERLVVIGGDA AGMSAASQAR RLKGPGELEI VAFERGHFTS FSACGIPYWV
     GGDVPERDLL IARTPEEHRA RGIDLRLRTE VTEIDVAGQR VRARDVDSGA ESWTSYDKLV
     IATGARPVRP DLPGVDAPGV HGVQTLDDGQ ALLETLGRTR GRKAVVVGAG YIGVEMAEAL
     INRGFEVTVV NRGKEPMSTL DADMGRLVHR AMEGLGITMV NDAEVTKILT GQDGRARAVA
     TQDAEYPADV VVLGIGVRPE TALAKAAGLP LGAHGGLLTD RAMRVRGHED IWAGGDCVEV
     LNLVSGQDQY VPLGTHANKH GQVIGSNAGG GYATFPGVVG TAVSKVCDLE IARTGLREKD
     ADRVGLRYET VTIESTSRAG YYPGASPMTV KMLAERRTGR LLGVQIVGRE GAAKRVDIAA
     VALTAQLTVE QMTALDLGYA PPFSPVWDPV LVAARKAAAK VRAS
//