ID   A0A0X3XI74_9ACTN        Unreviewed;       482 AA.
AC   A0A0X3XI74;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   24-JAN-2024, entry version 32.
DE   SubName: Full=Flavoprotein disulfide reductase {ECO:0000313|EMBL:KUL69262.1};
GN   ORFNames=ADL34_30970 {ECO:0000313|EMBL:KUL69262.1};
OS   Streptomyces sp. NRRL WC-3605.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1609103 {ECO:0000313|EMBL:KUL69262.1, ECO:0000313|Proteomes:UP000052945};
RN   [1] {ECO:0000313|EMBL:KUL69262.1, ECO:0000313|Proteomes:UP000052945}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL WC-3605 {ECO:0000313|EMBL:KUL69262.1,
RC   ECO:0000313|Proteomes:UP000052945};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|PIRSR:PIRSR000350-3};
CC       Note=Binds 1 FAD per subunit. {ECO:0000256|PIRSR:PIRSR000350-3};
CC   -!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide
CC       oxidoreductase family. {ECO:0000256|ARBA:ARBA00007532}.
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:KUL69262.1}.
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DR   EMBL; LLZN01000098; KUL69262.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0X3XI74; -.
DR   OrthoDB; 4678789at2; -.
DR   Proteomes; UP000052945; 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; IPR001100; Pyr_nuc-diS_OxRdtase.
DR   InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
DR   PANTHER; PTHR43014; MERCURIC REDUCTASE; 1.
DR   PANTHER; PTHR43014:SF1; NAD(P)H DEHYDROGENASE (QUINONE); 1.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   Pfam; PF02852; Pyr_redox_dim; 1.
DR   PIRSF; PIRSF000350; Mercury_reductase_MerA; 1.
DR   PRINTS; PR00368; FADPNR.
DR   PRINTS; PR00411; PNDRDTASEI.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   SUPFAM; SSF55424; FAD/NAD-linked reductases, dimerisation (C-terminal) domain; 1.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|PIRSR:PIRSR000350-3};
KW   Flavoprotein {ECO:0000256|PIRSR:PIRSR000350-3};
KW   NAD {ECO:0000256|PIRSR:PIRSR000350-3};
KW   Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000350-3};
KW   Reference proteome {ECO:0000313|Proteomes:UP000052945}.
FT   DOMAIN          6..341
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
FT   DOMAIN          362..468
FT                   /note="Pyridine nucleotide-disulphide oxidoreductase
FT                   dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF02852"
FT   BINDING         51
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT   BINDING         126
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT   BINDING         198..205
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT   BINDING         285
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT   BINDING         326
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
SQ   SEQUENCE   482 AA;  50516 MW;  1FA10306D911CD5E CRC64;
     MEYVTRIVII GGGPGGYEAA LVAAQLGAEV TVVDSDGLGG ASVLTDCVPS KTLIATAEVM
     TTFDSSYEEL GIIVADDTPH IDTPARVVGV DLGKVNRRVK RLALAQSHDI TASVTRAGAR
     VMRGRGRLEG MQALDGSRKV VVRTADGSEE TLVADAVLIA TGGHPRELPD AQPDGERILN
     WTQVYDLDEL PEELIVVGSG VTGAEFAGAY QALGSRVTLV SSRDRVLPGE DPDAAAVLED
     VFRRRGMNVM ARSRAAAAKR VGDRVEVTLA DGRVISGSHC LMAVGAVPNS EGLGLEEAGV
     KVRESGHIWT DKVSRTTAPG VYAAGDVTGV FALASVAAMQ GRIAMYHFLG DAVAPLNLKT
     VSSNVFTDPE IATVGYTQAD VDAGKIDARV VKLPLLRNPR AKMQGIRDGF VKIFCRPGTG
     IVVGGVVVAP RASELIHPIS IAVDNNLTVE QIANAFTVYP SLSGSIAEVA RQLHTRKAGA
     DL
//