ID V6KN60_STRNV Unreviewed; 486 AA.
AC V6KN60;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE SubName: Full=FAD-dependent pyridine nucleotide-disulfide oxidoreductase {ECO:0000313|EMBL:EST32861.1};
GN ORFNames=M877_03530 {ECO:0000313|EMBL:EST32861.1};
OS Streptomyces niveus NCIMB 11891.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1352941 {ECO:0000313|EMBL:EST32861.1, ECO:0000313|Proteomes:UP000017971};
RN [1] {ECO:0000313|EMBL:EST32861.1, ECO:0000313|Proteomes:UP000017971}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCIMB 11891 {ECO:0000313|EMBL:EST32861.1,
RC ECO:0000313|Proteomes:UP000017971};
RX PubMed=24407644;
RA Flinspach K., Ruckert C., Kalinowski J., Heide L., Apel A.K.;
RT "Draft Genome Sequence of Streptomyces niveus NCIMB 11891, Producer of the
RT Aminocoumarin Antibiotic Novobiocin.";
RL Genome Announc. 2:e01146-e01113(2014).
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:EST32861.1}.
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DR EMBL; AWQW01000026; EST32861.1; -; Genomic_DNA.
DR AlphaFoldDB; V6KN60; -.
DR STRING; 193462.BBN63_03390; -.
DR PATRIC; fig|1352941.4.peg.729; -.
DR eggNOG; COG1249; Bacteria.
DR HOGENOM; CLU_016755_1_3_11; -.
DR OrthoDB; 9800167at2; -.
DR Proteomes; UP000017971; Chromosome.
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 17..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 63
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 193..200
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 282
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 54..59
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-4"
SQ SEQUENCE 486 AA; 51282 MW; 649F6650872A2CA3 CRC64;
MRRAPHETVL MTEAIEYDVV VLGAGPVGEN VAERVRAAGL SAAVVESELV GGECSYWACM
PSKALLRPVI ARAEARRVPG LSRYVQGPLD MPAVFAHRDE YTSHWNDDGQ VAWLDGIGAV
LYRGQGRLDG KKRVTVTDSG GAVQVLTARH AVAVCTGTTA IVPDLPGLAD AKPWTSRQAT
SSPKVPDRLV VVGGGVVGVE MATAYCGFGS AVTLLVRGDG LLPRMEPFVG ERITDSLKEA
GASVRMGVSV ASVERDGGTG PVTAVLDNGE RIEADEILFA TGRAPHTQDI GLDTVGLKAG
SWLTVDDSCL VAGSDWLYAV GDVNHRALLT HQGKYQARIA GAAIGARAQR VPLLETDRWG
AHTATADHAA VPQVVFTDPE AASVGLTLKE AEAAGHRVRA VDYAIENVAG ASLYAEGYQG
HARMIVDLDS EILRGVTFVG PGVGELLHSA TVAVAGEVPI NRLWHAVPSY PTISEVWLRL
LETYRG
//
