ID   LPDA_MYCTO              Reviewed;         493 AA.
AC   P9WHH6; L0TC51; O53355; Q8VJ36;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 42.
DE   RecName: Full=NAD(P)H dehydrogenase (quinone);
DE            EC=1.6.5.2;
DE   AltName: Full=NAD(P)H quinone reductase;
DE   AltName: Full=NAD(P)H: menadione oxidoreductase;
DE   AltName: Full=NADH-menadione reductase;
GN   Name=lpdA; Synonyms=lpdA-2; OrderedLocusNames=MT3402;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA   Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA   Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA   Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
CC   -!- FUNCTION: May contribute to virulence by increasing resistance to
CC       reactive oxygen intermediates. It can reduce 2,6-dimethyl-1,4-
CC       benzoquinone (DMBQ), 5-hydroxy-1,4-naphthaquinone (5-HNQ) and menadione
CC       (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a quinone + H(+) + NADH = a quinol + NAD(+);
CC         Xref=Rhea:RHEA:46160, ChEBI:CHEBI:15378, ChEBI:CHEBI:24646,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:132124; EC=1.6.5.2;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a quinone + H(+) + NADPH = a quinol + NADP(+);
CC         Xref=Rhea:RHEA:46164, ChEBI:CHEBI:15378, ChEBI:CHEBI:24646,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:132124; EC=1.6.5.2;
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC       Note=Binds 1 FAD per subunit.;
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide
CC       oxidoreductase family. {ECO:0000305}.
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DR   EMBL; AE000516; AAK47745.1; -; Genomic_DNA.
DR   PIR; F70841; F70841.
DR   AlphaFoldDB; P9WHH6; -.
DR   SMR; P9WHH6; -.
DR   EnsemblBacteria; AAK47745; AAK47745; MT3402.
DR   KEGG; mtc:MT3402; -.
DR   HOGENOM; CLU_016755_0_3_11; -.
DR   Proteomes; UP000001020; Chromosome.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0050136; F:NADH dehydrogenase (quinone) activity; IEA:RHEA.
DR   GO; GO:0008753; F:NADPH dehydrogenase (quinone) activity; IEA:RHEA.
DR   GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
DR   Gene3D; 3.30.390.30; -; 1.
DR   Gene3D; 3.50.50.60; -; 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   Pfam; PF07992; Pyr_redox_2; 1.
DR   Pfam; PF02852; Pyr_redox_dim; 1.
DR   PIRSF; PIRSF000350; Mercury_reductase_MerA; 1.
DR   SUPFAM; SSF51905; SSF51905; 1.
DR   SUPFAM; SSF55424; SSF55424; 1.
PE   3: Inferred from homology;
KW   FAD; Flavoprotein; NAD; Oxidoreductase.
FT   CHAIN           1..493
FT                   /note="NAD(P)H dehydrogenase (quinone)"
FT                   /id="PRO_0000428185"
FT   BINDING         12..13
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT   BINDING         35..37
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT   BINDING         42..43
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT   BINDING         52
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT   BINDING         117
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT   BINDING         317
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT   BINDING         324..325
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT   BINDING         450
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
SQ   SEQUENCE   493 AA;  51489 MW;  71C3F1483665278C CRC64;
     MVTRIVILGG GPAGYEAALV AATSHPETTQ VTVIDCDGIG GAAVLDDCVP SKTFIASTGL
     RTELRRAPHL GFHIDFDDAK ISLPQIHARV KTLAAAQSAD ITAQLLSMGV QVIAGRGELI
     DSTPGLARHR IKATAADGST SEHEADVVLV ATGASPRILP SAQPDGERIL TWRQLYDLDA
     LPDHLIVVGS GVTGAEFVDA YTELGVPVTV VASQDHVLPY EDADAALVLE ESFAERGVRL
     FKNARAASVT RTGAGVLVTM TDGRTVEGSH ALMTIGSVPN TSGLGLERVG IQLGRGNYLT
     VDRVSRTLAT GIYAAGDCTG LLPLASVAAM QGRIAMYHAL GEGVSPIRLR TVAATVFTRP
     EIAAVGVPQS VIDAGSVAAR TIMLPLRTNA RAKMSEMRHG FVKIFCRRST GVVIGGVVVA
     PIASELILPI AVAVQNRITV NELAQTLAVY PSLSGSITEA ARRLMAHDDL DCTAAQDAAE
     QLALVPHHLP TSN