ID A0A1P8XMY7_9ACTN Unreviewed; 479 AA.
AC A0A1P8XMY7;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Pyridine nucleotide-disulfide oxidoreductase {ECO:0000313|EMBL:AQA09370.1};
GN ORFNames=BV401_01540 {ECO:0000313|EMBL:AQA09370.1};
OS Streptomyces autolyticus.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=75293 {ECO:0000313|EMBL:AQA09370.1, ECO:0000313|Proteomes:UP000187851};
RN [1] {ECO:0000313|Proteomes:UP000187851}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC0516 {ECO:0000313|Proteomes:UP000187851};
RA Yin M., Jiang M., Lu T.;
RT "Streptomyces autolyticus CGMCC0516 complete genome sequence.";
RL Submitted (JAN-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; CP019458; AQA09370.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1P8XMY7; -.
DR STRING; 75293.BV401_01540; -.
DR KEGG; sauo:BV401_01540; -.
DR OrthoDB; 9800167at2; -.
DR Proteomes; UP000187851; 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 6..328
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 364..470
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
FT BINDING 52
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 115
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 145..147
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 182..189
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 269
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 316
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT DISULFID 43..48
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-4"
SQ SEQUENCE 479 AA; 49920 MW; EC0FA60B3FE372F7 CRC64;
MDDHTYDVIV IGAGPVGENV ADRVAQGGLS AAIVERDLVG GECSYWACMP TKALLRSTAA
LRAARHVPGS REAVTGDLDV TAVLRRRDSF SSHWKDDGQV SWLDSAGITL YRGQGRIRPD
RVVEVTDAAG VATSLTARHA VVIATGSAAL LPDIPGLREA EPWSSREAAA ASAVPGRLAV
IGGGVVASEM ATAFAALGSS VTMLVRDGVL PLAEPFAGER VTESLREAGV SVLLGAEAGT
VKRDGDGTVH ITLTTGEDVE ADEVLVAIGR APNTQNMGLG TVGLTPGDWL AVDDTLRVVG
DDGAPLAGGW LYAAGDVNRR VLLTHQGKYQ ARAVGDVIVA RAKGEAVDDS PWGRHVATAD
ERAVPQVVFT EPEIASVGLT AAAAETAGFR IRVVDYDLGA VAGSALHADG YRGQARMVVD
EDRKVIVGFT LVGPDVAELL HAATIAVVGE VPLDRLWHAV PAFPTVSEVW LRLLEAYGH
//
