ID K4R3G3_STRDJ Unreviewed; 482 AA.
AC K4R3G3;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE SubName: Full=NAD(P)H dehydrogenase (Quinone) {ECO:0000313|EMBL:CCK27858.1};
DE EC=1.6.5.2 {ECO:0000313|EMBL:CCK27858.1};
GN Name=lpdA {ECO:0000313|EMBL:CCK27858.1};
GN ORFNames=BN159_3479 {ECO:0000313|EMBL:CCK27858.1};
OS Streptomyces davaonensis (strain DSM 101723 / JCM 4913 / KCC S-0913 / 768).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1214101 {ECO:0000313|EMBL:CCK27858.1, ECO:0000313|Proteomes:UP000008043};
RN [1] {ECO:0000313|EMBL:CCK27858.1, ECO:0000313|Proteomes:UP000008043}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 101723 / JCM 4913 / KCC S-0913 / 768
RC {ECO:0000313|Proteomes:UP000008043};
RX PubMed=23043000; DOI=10.1128/JB.01592-12;
RA Jankowitsch F., Schwarz J., Ruckert C., Gust B., Szczepanowski R., Blom J.,
RA Pelzer S., Kalinowski J., Mack M.;
RT "Genome sequence of the bacterium Streptomyces davawensis JCM 4913 and
RT heterologous production of the unique antibiotic roseoflavin.";
RL J. Bacteriol. 194:6818-6827(2012).
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; HE971709; CCK27858.1; -; Genomic_DNA.
DR RefSeq; WP_015658235.1; NC_020504.1.
DR AlphaFoldDB; K4R3G3; -.
DR STRING; 1214101.BN159_3479; -.
DR KEGG; sdv:BN159_3479; -.
DR PATRIC; fig|1214101.3.peg.3530; -.
DR eggNOG; COG1249; Bacteria.
DR HOGENOM; CLU_016755_0_3_11; -.
DR OrthoDB; 4678789at2; -.
DR Proteomes; UP000008043; Chromosome.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0003955; F:NAD(P)H dehydrogenase (quinone) activity; IEA:UniProtKB-EC.
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 Oxidoreductase {ECO:0000313|EMBL:CCK27858.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008043}.
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; 50448 MW; 753DD4F19F703E7D CRC64;
MEYVTRIVII GGGPGGYEAA LVAAQLGAEV TVVDSDGLGG ASVLTDCVPS KTLIATAEVM
TTFDSSYEEL GIIVADDTPH IDTPARVVGV DLGKVNRRVK RLALAQSHDI TASVTRAGAR
VMRGRGRLDG MQGLDGSRKV IVTTADGTEE TLVADAVLIA TGGHPREVPD ALPDGERILN
WTQVYDLTEL PEELIVVGSG VTGAEFAGAY QALGSKVTLV SSRDRVLPGE DPDAAAVLED
VFRRRGMNVM ARSRAAAAKR VGDRVEVTLA DGRVITGTHC LMAVGAIPNS AGLGLEEAGV
KLRESGHIWT DKVSRTTAPG VYAAGDVTGV FALASVAAMQ GRIAMYHFLG DAVAPLNLKT
VSSNVFTDPE IATVGYTQAD VEAGKIDARV VKLPLLRNPR AKMQGIRDGF VKIFCRPGTG
IVVGGVVVAP RASELIHPIS IAVDNNLTVE QIANAFTVYP SLSGSIAEVA RQLHTRKTGS
EV
//
