ID A0A1E3T6M0_MYCSH Unreviewed; 472 AA.
AC A0A1E3T6M0;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=NAD(P)H quinone reductase LpdA [Mycobacterium tuberculosis H37Rv] {ECO:0000313|EMBL:SRX96208.1};
GN ORFNames=MSP7336_04484 {ECO:0000313|EMBL:SRX96208.1};
OS Mycobacterium shimoidei.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=29313 {ECO:0000313|EMBL:SRX96208.1, ECO:0000313|Proteomes:UP000252015};
RN [1] {ECO:0000313|EMBL:SRX96208.1, ECO:0000313|Proteomes:UP000252015}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P7336 {ECO:0000313|EMBL:SRX96208.1,
RC ECO:0000313|Proteomes:UP000252015};
RG IHU Genomes;
RL Submitted (MAY-2018) 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; UEGW01000001; SRX96208.1; -; Genomic_DNA.
DR RefSeq; WP_069397703.1; NZ_UEGW01000001.1.
DR AlphaFoldDB; A0A1E3T6M0; -.
DR STRING; 29313.BHQ16_19370; -.
DR OrthoDB; 4678789at2; -.
DR Proteomes; UP000252015; Unassembled WGS sequence.
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; 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}.
FT DOMAIN 6..333
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 353..462
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
FT BINDING 54
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 118
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 190..197
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 277
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 318
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
SQ SEQUENCE 472 AA; 48749 MW; A3650D04EE1D8D05 CRC64;
MGSLTRVVIL GAGPAGYEAA LVAAARGPDV AEVTVVDSDG IGGAAVLCDC VPSKTFVAST
GLRTELGRAP LGLDVDVGDA EIALPEIHQR VKTLAAAQSA DITADLLSMG VELIAGRGEL
VDPNPGLARH CVKVTAPDGA TTLRDADVVL VATGASPRIL PSAQPDDERI LTWRQLYDLA
TLPDHLIVVG SGVTGAEFVN AYTELGVPVT VVASRDRVLP YEDADAAAVL EESLAERGVK
LVKNARAQSV TRSDGGVVVT TTDGRTVEGS HALMTIGSSP NTGGLGLERV GIELGRGDYL
TVDRVSRTSV PGIYAAGDCT GLLQLASVAA MQGRIAMYHA LGEAVSPIRL RTVPATVFTR
PEIAAVGVPQ TAIDDGSVPA RTIMLPLETN ARAKMSELRH GFVKLFCQQA SGVVIGGVVV
APIASELILP IAVAVQNRIT VSELAQTLAI YPSLSGSITE AARRLIGHHD VD
//
