ID A0A0K2YEE1_9NOCA Unreviewed; 467 AA.
AC A0A0K2YEE1;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE SubName: Full=NAD(P)H dehydrogenase (Quinone) {ECO:0000313|EMBL:CRK50347.1};
DE EC=1.6.5.2 {ECO:0000313|EMBL:CRK50347.1};
GN Name=lpdA {ECO:0000313|EMBL:CRK50347.1};
GN ORFNames=RHCRD62_110027 {ECO:0000313|EMBL:CRK50347.1};
OS Rhodococcus sp. RD6.2.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=260936 {ECO:0000313|EMBL:CRK50347.1, ECO:0000313|Proteomes:UP000044872};
RN [1] {ECO:0000313|EMBL:CRK50347.1, ECO:0000313|Proteomes:UP000044872}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RD6.2 {ECO:0000313|EMBL:CRK50347.1,
RC ECO:0000313|Proteomes:UP000044872};
RA Wang D.B., Wang M.;
RL Submitted (MAY-2015) 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; CVQP01000003; CRK50347.1; -; Genomic_DNA.
DR RefSeq; WP_050063720.1; NZ_CVQP01000003.1.
DR AlphaFoldDB; A0A0K2YEE1; -.
DR STRING; 260936.RHCRD62_110027; -.
DR OrthoDB; 4678789at2; -.
DR Proteomes; UP000044872; 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; 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:CRK50347.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000044872}.
FT DOMAIN 3..328
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 348..457
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 185..192
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 272
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 313
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 467 AA; 48656 MW; A4F7BEBBE2C25D31 CRC64;
MTRIVIIGGG PAGYEAALVA AAHGATVSLV DSDGVGGACV LWDCVPSKTF IASTGVRTDM
RRATDLGISL DPAQATISLP QIHSRVKSLA QAQSADIRDK LQTAGVELLA GTAELIDSVI
GMASHKVKAH LADGGERVLE ADVVLIATGA SPRVLPGAEP DGDRILNWRQ LYDLETLPEH
LVVVGSGVTG AEFVSAYTEM GVHVTMVSSR DRVLPHEDAD AAMVLEEALS ERGVTLVKHA
RADSVVRTAD GIRVTLSDGR TVDGSHALMT VGSTPNTSGL GLEKVGIELD RGGYLRVDRV
SRTSVSGVYA AGDCTGLLPL ASVAAMQGRI AMYHALGEGV SPIKLKTVAS AVFTRPEIAN
VGVSQAAIDN GDVPARTVML PLNTNPRAKM SSLRRGFVKI FCRPATGVVI GGVVVAPTAS
ELILPIAIAV QNNLSVNDLA QTFSVYPSLS GSITEAARQL MRHDDLD
//