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Database: UniProt
Entry: A0A101P4Q8_9ACTN
LinkDB: A0A101P4Q8_9ACTN
Original site: A0A101P4Q8_9ACTN 
ID   A0A101P4Q8_9ACTN        Unreviewed;       463 AA.
AC   A0A101P4Q8;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=Flavoprotein oxidoreductase {ECO:0000313|EMBL:KUN04866.1};
GN   ORFNames=AQI95_18480 {ECO:0000313|EMBL:KUN04866.1};
OS   Streptomyces yokosukanensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=67386 {ECO:0000313|EMBL:KUN04866.1, ECO:0000313|Proteomes:UP000053127};
RN   [1] {ECO:0000313|EMBL:KUN04866.1, ECO:0000313|Proteomes:UP000053127}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 40224 {ECO:0000313|EMBL:KUN04866.1,
RC   ECO:0000313|Proteomes:UP000053127};
RA   Ruckert C., Winkler A., Kalinowski J., Kampfer P., Glaeser S.;
RT   "Draft genome sequence of Streptomyces yokosukanensis DSM 40224, type
RT   strain for the species Streptomyces yokosukanensis.";
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   -!- SIMILARITY: Belongs to the class-III pyridine nucleotide-disulfide
CC       oxidoreductase family. {ECO:0000256|ARBA:ARBA00009130}.
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:KUN04866.1}.
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DR   EMBL; LMWN01000024; KUN04866.1; -; Genomic_DNA.
DR   RefSeq; WP_067124340.1; NZ_KQ948212.1.
DR   AlphaFoldDB; A0A101P4Q8; -.
DR   STRING; 67386.AQI95_18480; -.
DR   OrthoDB; 9802028at2; -.
DR   Proteomes; UP000053127; 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; 3.50.50.60; 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;
KW   Reference proteome {ECO:0000313|Proteomes:UP000053127}.
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   463 AA;  48776 MW;  BDFDDC03C41898BC CRC64;
     MSMREGQDGT ERLVVIGGDA AGMSAASQAR RLKGPGELEI VAFERGRFTS FSACGIPYWV
     GGDVAERDAL IARTPEEHRA RGIDLRLGTE VTAIDVPGRR VRARDVDSGT ESWTPYDKLV
     IATGARPVRP DLPGVDAPGV HGVQTLGDGQ ALLQTLARAH GRRAVVVGAG YIGVEMAEAL
     INRGFEVTVV NRGKEPMSTL DADMGRLVHR AMEGLGITMV NDAEVTKILT GEDGRARAVA
     TQDAEYPADV VVLGIGVRPD TALARAAGLP LGAHGGLLTD LAMRVRGHED IWAGGDCVEV
     LNLVSGQEQY VPLGTHANKH GQVIGSNVGG GYATFPGVVG TAVSKVCDLE IARTGLREKD
     AGRVGLRYET VTIESTSRAG YYPGASPMTV KMLAERRTGR LLGVQIVGRE GAAKRVDIAA
     VALTAQMTVE QMTALDLGYA PPFSPVWDPV LVAARKAAAK VRP
//
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