ID   FQR58_MYCTO             Reviewed;         148 AA.
AC   P9WP10; L0T770; P64875; Q10772;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 38.
DE   RecName: Full=F420H(2)-dependent quinone reductase MT1609 {ECO:0000250|UniProtKB:P9WP11};
DE            Short=Fqr {ECO:0000250|UniProtKB:P9WP11};
DE            EC=1.1.98.- {ECO:0000250|UniProtKB:P9WP11};
GN   OrderedLocusNames=MT1609;
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: 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       In vitro, catalyzes the reduction of menadione to menadiol; since
CC       menaquinone is the sole quinone electron carrier in the respiratory
CC       chain in M.tuberculosis, the physiological electron acceptor for Fqr-
CC       mediated F420H(2) oxidation is therefore likely to be the endogenous
CC       menaquinone found in the membrane fraction of M.tuberculosis.
CC       {ECO:0000250|UniProtKB:P9WP11}.
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:P9WP11};
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE000516; AAK45876.1; -; Genomic_DNA.
DR   PIR; C70763; C70763.
DR   RefSeq; WP_003407780.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WP10; -.
DR   SMR; P9WP10; -.
DR   EnsemblBacteria; AAK45876; AAK45876; MT1609.
DR   KEGG; mtc:MT1609; -.
DR   PATRIC; fig|83331.31.peg.1731; -.
DR   HOGENOM; CLU_114921_1_0_11; -.
DR   Proteomes; UP000001020; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..148
FT                   /note="F420H(2)-dependent quinone reductase MT1609"
FT                   /id="PRO_0000427033"
FT   BINDING         46..48
FT                   /ligand="coenzyme F420-(gamma-Glu)n"
FT                   /ligand_id="ChEBI:CHEBI:133980"
FT                   /evidence="ECO:0000250|UniProtKB:P9WP15"
FT   BINDING         52..57
FT                   /ligand="coenzyme F420-(gamma-Glu)n"
FT                   /ligand_id="ChEBI:CHEBI:133980"
FT                   /evidence="ECO:0000250|UniProtKB:P9WP15"
FT   BINDING         68..71
FT                   /ligand="coenzyme F420-(gamma-Glu)n"
FT                   /ligand_id="ChEBI:CHEBI:133980"
FT                   /evidence="ECO:0000250|UniProtKB:P9WP15"
FT   BINDING         79..83
FT                   /ligand="coenzyme F420-(gamma-Glu)n"
FT                   /ligand_id="ChEBI:CHEBI:133980"
FT                   /evidence="ECO:0000250|UniProtKB:P9WP15"
FT   BINDING         125
FT                   /ligand="coenzyme F420-(gamma-Glu)n"
FT                   /ligand_id="ChEBI:CHEBI:133980"
FT                   /evidence="ECO:0000250|UniProtKB:P9WP15"
SQ   SEQUENCE   148 AA;  16348 MW;  A9F98E90398719B8 CRC64;
     MPLSGEYAPS PLDWSREQAD TYMKSGGTEG TQLQGKPVIL LTTVGAKTGK LRKTPLMRVE
     HDGQYAIVAS LGGAPKNPVW YHNVVKNPRV ELQDGTVTGD YDAREVFGDE KAIWWQRAVA
     VWPDYASYQT KTDRQIPVFV LTPVRAGG