ID A0A2I2KL39_9ACTN Unreviewed; 492 AA.
AC A0A2I2KL39;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=NAD(P)H dehydrogenase (Quinone) {ECO:0000313|EMBL:SNQ46391.1};
DE EC=1.6.5.2 {ECO:0000313|EMBL:SNQ46391.1};
GN Name=lpdA {ECO:0000313|EMBL:SNQ46391.1};
GN ORFNames=FRACA_1390007 {ECO:0000313|EMBL:SNQ46391.1};
OS Frankia canadensis.
OC Bacteria; Actinomycetota; Actinomycetes; Frankiales; Frankiaceae; Frankia.
OX NCBI_TaxID=1836972 {ECO:0000313|EMBL:SNQ46391.1, ECO:0000313|Proteomes:UP000234331};
RN [1] {ECO:0000313|EMBL:SNQ46391.1, ECO:0000313|Proteomes:UP000234331}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FRACA_ARgP5 {ECO:0000313|EMBL:SNQ46391.1};
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; FZMO01000045; SNQ46391.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2I2KL39; -.
DR OrthoDB; 4678789at2; -.
DR Proteomes; UP000234331; Unassembled WGS sequence.
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; 2.
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:SNQ46391.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000234331}.
FT DOMAIN 3..347
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 368..476
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
FT BINDING 48
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 142
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 204..211
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 291
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 332
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT DISULFID 39..44
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-4"
SQ SEQUENCE 492 AA; 50933 MW; A428969594C48BC1 CRC64;
MTRIVILGGG PGGYEAALVG ASLGATVTVI DSDGIGGACV LTDCVPSKTL IATSETMTNL
ALAPGLGIQP HGPGAGGEPA LPAVAWGMPS SADSGPALTP PEVVSVEPEQ VYERVRELAK
AQSADIERRL QRERVEVVHA AGRLVGPHAI ETSSGETFVG DVILIATGAS PRDLSTAQPD
GERILTWRHL YDLKEIPEHL VVVGSGVTGA EFASAYRALG AEVTLVSSRE RVLPGEDPDA
ARVIEEVFVR RGIEVLNRSR AASVRRIGDG VIVELTDGRT VTGSHALMAV GSVPRTKGLG
LTDVGVRLGP GGHVNVDRMS RTSVPGVYAA GDCTGVLPLA SVAAMQGRIA MWHALGEAVS
PLRLGTVSSN IFTEPEIATV GVTQVMKDTG AVAAEVTTVP LSRNPRAKMM GVEDGFVKLF
CRPGSGSVLG GVIVAPRASE LILSVALAVE HGLTVDQIAH TFSIYPSLSG SITEAARVLR
PRDFFAGFDN PA
//
