ID   A0A239F823_9ACTN        Unreviewed;       482 AA.
AC   A0A239F823;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   SubName: Full=Dihydrolipoamide dehydrogenase {ECO:0000313|EMBL:SNS53069.1};
GN   ORFNames=SAMN05216252_106367 {ECO:0000313|EMBL:SNS53069.1};
OS   Actinacidiphila glaucinigra.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Actinacidiphila.
OX   NCBI_TaxID=235986 {ECO:0000313|EMBL:SNS53069.1, ECO:0000313|Proteomes:UP000198280};
RN   [1] {ECO:0000313|EMBL:SNS53069.1, ECO:0000313|Proteomes:UP000198280}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 4.1858 {ECO:0000313|EMBL:SNS53069.1,
RC   ECO:0000313|Proteomes:UP000198280};
RA   Kim H.J., Triplett B.A.;
RL   Submitted (JUN-2017) 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}.
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DR   EMBL; FZOF01000006; SNS53069.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A239F823; -.
DR   OrthoDB; 4678789at2; -.
DR   Proteomes; UP000198280; 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:UP000198280}.
FT   DOMAIN          6..341
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
FT   DOMAIN          362..470
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;  50482 MW;  134E004BC9BF1A7C CRC64;
     MGYVNRIVII GGGPGGYEAA LVASQLGAEV TVVDCDGLGG ASVLTDCVPS KTLIATAEVM
     TTFDSSYEEL GIIVADDTPH IEQAARVVGV DLGKVNRRVK RLALAQSHDI TASVTRAGAR
     VMRGRGRLEG MQAIDGSRTV IVEAADGTSE TLTADAVLIA TGGRPRELPD AKPDGERILN
     WTQVYDLDEL PEELIVVGSG VTGAEFAGAY QALGSKVTLV SSRDRVLPGE DPDAAAVLED
     VFRRRGMNVM ARSRAEAVKR VGDRVEVTLS DGRVITGSHC LMAVGAIPNT SAMGLEGAGV
     KLKESGHIWT DKVSRTSAPG VYAAGDVTGV FALASVAAMQ GRIAMYHFLG ETVGPLNLKT
     VSSNVFTDPE IATVGYTQAD VDSGLMDARV VKLPLLRNPR AKMQGIRDGF VKLFCRPGTG
     IVVGGVVVSP RASELIHPIS IAVDNNLTVE QMANTYTVYP SLSGSIAEAA RQLATRKAAG
     EL
//