ID A0A0D7CTN0_9ACTN Unreviewed; 486 AA.
AC A0A0D7CTN0;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=Pyridine nucleotide-disulfide oxidoreductase {ECO:0000313|EMBL:KIZ18727.1};
GN ORFNames=SNA_05485 {ECO:0000313|EMBL:KIZ18727.1};
OS Streptomyces natalensis ATCC 27448.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1240678 {ECO:0000313|EMBL:KIZ18727.1, ECO:0000313|Proteomes:UP000032458};
RN [1] {ECO:0000313|EMBL:KIZ18727.1, ECO:0000313|Proteomes:UP000032458}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27448 {ECO:0000313|EMBL:KIZ18727.1,
RC ECO:0000313|Proteomes:UP000032458};
RA Mendes M.V., Beites T., Pires S., Santos C.L., Moradas-Ferreira P.;
RT "Draft genome sequence of Streptomyces natalensis ATCC 27448, producer of
RT the antifungal pimaricin.";
RL Submitted (SEP-2014) 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:KIZ18727.1}.
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DR EMBL; JRKI01000008; KIZ18727.1; -; Genomic_DNA.
DR RefSeq; WP_044363539.1; NZ_JRKI01000008.1.
DR AlphaFoldDB; A0A0D7CTN0; -.
DR PATRIC; fig|1240678.4.peg.1159; -.
DR Proteomes; UP000032458; 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; PTHR22912:SF217; DIHYDROLIPOYL DEHYDROGENASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR22912; DISULFIDE OXIDOREDUCTASE; 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|ARBA:ARBA00023027, ECO:0000256|PIRSR:PIRSR000350-3};
KW Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000350-3}.
FT DOMAIN 8..331
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 371..477
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
FT BINDING 54
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 142..144
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 179..186
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 280
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 322
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT DISULFID 45..50
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-4"
SQ SEQUENCE 486 AA; 50314 MW; 8B0A51248A36E38F CRC64;
MAATEATHDV LVLGAGPTGE NVADRAHAAG LSVAIMESEL VGGECSYWAC MPSKALLRPV
TARSEARRVP GLADAAAGPL DAPAVLGHRD AFASHWKDDG QVRWLETAGI ELVRGHARLA
GPHQVSVGDR VLRARHAVAV CTGSRPVLPA IPGLADARPW TSRDATSAKT VPGRLVVVGG
GVVGVEMATA WRALGASVTL LVRGDGLLPR MEPFAGHLVA ESLAEAGVFL RTGVEVTEVR
REAPGGPVTV VLDSTASGAD RGATGSGDEI VADELLIATG RAPRTDDVGL ETVGLAPGSW
LPVDDSCLVT DVPGGWLYGV GDVNHRALLT HQGKYQARIA GAAIAARARN VPILDHGPWG
AHAATADTAA VPQVVFSDPE AASVGLTAAA AERAGRRVRV IDQDLGAVAG AALYADGYRG
RARMIVDLDR EVLLGVTFVG PGVGELLHSA TVAVVGEIPI ERLWHAVPAY PTISEVWLRL
LESYRG
//
