ID   FQR78_MYCTU             Reviewed;         119 AA.
AC   O53328; L0TET4;
DT   05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 3.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=Putative F420H(2)-dependent quinone reductase Rv3178 {ECO:0000305};
DE            Short=Fqr;
DE            EC=1.1.98.-;
GN   OrderedLocusNames=Rv3178;
OS   Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83332;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=9634230; DOI=10.1038/31159;
RA   Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA   Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA   Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA   Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA   Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA   Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA   Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA   Barrell B.G.;
RT   "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT   genome sequence.";
RL   Nature 393:537-544(1998).
CC   -!- FUNCTION: Involved in a F420-dependent anti-oxidant mechanism that
CC       protects M.tuberculosis against oxidative stress and bactericidal
CC       agents. Catalyzes the F420H(2)-dependent two-electron reduction of
CC       quinones to dihydroquinones, thereby preventing the formation of
CC       cytotoxic semiquinones obtained by the one-electron reduction pathway.
CC       Since menaquinone is the sole quinone electron carrier in the
CC       respiratory chain in M.tuberculosis, the physiological electron
CC       acceptor for Fqr-mediated F420H(2) oxidation is therefore likely to be
CC       the endogenous menaquinone found in the membrane fraction of
CC       M.tuberculosis. {ECO:0000250|UniProtKB:P9WP15}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a quinol + H(+) + oxidized coenzyme F420-(gamma-L-Glu)(n) = a
CC         quinone + reduced coenzyme F420-(gamma-L-Glu)(n);
CC         Xref=Rhea:RHEA:39663, Rhea:RHEA-COMP:12939, Rhea:RHEA-COMP:14378,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:24646, ChEBI:CHEBI:132124,
CC         ChEBI:CHEBI:133980, ChEBI:CHEBI:139511;
CC         Evidence={ECO:0000250|UniProtKB:P9WP15};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P9WP15};
CC       Peripheral membrane protein {ECO:0000250|UniProtKB:P9WP15}.
CC   -!- SIMILARITY: Belongs to the F420H(2)-dependent quinone reductase family.
CC       {ECO:0000305}.
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DR   EMBL; AL123456; CCP45989.1; -; Genomic_DNA.
DR   PIR; H70948; H70948.
DR   RefSeq; NP_217694.1; NC_000962.3.
DR   RefSeq; WP_003416632.1; NC_000962.3.
DR   AlphaFoldDB; O53328; -.
DR   SMR; O53328; -.
DR   STRING; 83332.Rv3178; -.
DR   PaxDb; O53328; -.
DR   DNASU; 888786; -.
DR   GeneID; 888786; -.
DR   KEGG; mtu:Rv3178; -.
DR   TubercuList; Rv3178; -.
DR   eggNOG; COG0748; Bacteria.
DR   OMA; QWYRNLV; -.
DR   PhylomeDB; O53328; -.
DR   Proteomes; UP000001584; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0070967; F:coenzyme F420 binding; IBA:GO_Central.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   Gene3D; 2.30.110.10; -; 1.
DR   InterPro; IPR004378; F420H2_quin_Rdtase.
DR   InterPro; IPR012349; Split_barrel_FMN-bd.
DR   Pfam; PF04075; F420H2_quin_red; 1.
DR   TIGRFAMs; TIGR00026; hi_GC_TIGR00026; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Membrane; Oxidoreductase; Reference proteome.
FT   CHAIN           1..119
FT                   /note="Putative F420H(2)-dependent quinone reductase
FT                   Rv3178"
FT                   /id="PRO_0000399508"
FT   BINDING         21..23
FT                   /ligand="coenzyme F420-(gamma-Glu)n"
FT                   /ligand_id="ChEBI:CHEBI:133980"
FT                   /evidence="ECO:0000250|UniProtKB:P9WP15"
FT   BINDING         27..32
FT                   /ligand="coenzyme F420-(gamma-Glu)n"
FT                   /ligand_id="ChEBI:CHEBI:133980"
FT                   /evidence="ECO:0000250|UniProtKB:P9WP15"
FT   BINDING         43..46
FT                   /ligand="coenzyme F420-(gamma-Glu)n"
FT                   /ligand_id="ChEBI:CHEBI:133980"
FT                   /evidence="ECO:0000250|UniProtKB:P9WP15"
FT   BINDING         54..58
FT                   /ligand="coenzyme F420-(gamma-Glu)n"
FT                   /ligand_id="ChEBI:CHEBI:133980"
FT                   /evidence="ECO:0000250|UniProtKB:P9WP15"
SQ   SEQUENCE   119 AA;  13497 MW;  E6E07393EE396E44 CRC64;
     MRLGAGFRKP VPTLLLEHRS RKSGKNFVAP LLYITDRNNV IVVASALGQA ENPQWYRNLP
     PNPDTHIQIG SDRRPVRAVV ASSDERARLW PRPVDAYADF DSCQSWTERG IPVIILRPR