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Database: UniProt
Entry: A0A0K2YEE1_9NOCA
LinkDB: A0A0K2YEE1_9NOCA
Original site: A0A0K2YEE1_9NOCA 
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
//
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