ID   FQR61_MYCTO             Reviewed;         149 AA.
AC   P9WP12; L0T6C5; P64787; Q11057;
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 MT1299 {ECO:0000250|UniProtKB:P9WP13};
DE            Short=Fqr {ECO:0000250|UniProtKB:P9WP13};
DE            EC=1.1.98.- {ECO:0000250|UniProtKB:P9WP13};
GN   OrderedLocusNames=MT1299;
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:P9WP13}.
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:P9WP13};
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; AE000516; AAK45558.1; -; Genomic_DNA.
DR   PIR; E70753; E70753.
DR   RefSeq; WP_003406364.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WP12; -.
DR   SMR; P9WP12; -.
DR   EnsemblBacteria; AAK45558; AAK45558; MT1299.
DR   KEGG; mtc:MT1299; -.
DR   PATRIC; fig|83331.31.peg.1403; -.
DR   HOGENOM; CLU_114921_2_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   CHAIN           1..149
FT                   /note="F420H(2)-dependent quinone reductase MT1299"
FT                   /id="PRO_0000427032"
FT   BINDING         48..50
FT                   /ligand="coenzyme F420-(gamma-Glu)n"
FT                   /ligand_id="ChEBI:CHEBI:133980"
FT                   /evidence="ECO:0000250|UniProtKB:P9WP15"
FT   BINDING         54..59
FT                   /ligand="coenzyme F420-(gamma-Glu)n"
FT                   /ligand_id="ChEBI:CHEBI:133980"
FT                   /evidence="ECO:0000250|UniProtKB:P9WP15"
FT   BINDING         70..73
FT                   /ligand="coenzyme F420-(gamma-Glu)n"
FT                   /ligand_id="ChEBI:CHEBI:133980"
FT                   /evidence="ECO:0000250|UniProtKB:P9WP15"
FT   BINDING         81..85
FT                   /ligand="coenzyme F420-(gamma-Glu)n"
FT                   /ligand_id="ChEBI:CHEBI:133980"
FT                   /evidence="ECO:0000250|UniProtKB:P9WP15"
FT   BINDING         130
FT                   /ligand="coenzyme F420-(gamma-Glu)n"
FT                   /ligand_id="ChEBI:CHEBI:133980"
FT                   /evidence="ECO:0000250|UniProtKB:P9WP15"
SQ   SEQUENCE   149 AA;  16756 MW;  D8F22A51B5F43FCF CRC64;
     MDISRWLERH VGVQLLRLHD AIYRGTNGRI GHRIPGAPPS LLLHTTGAKT SQPRTTSLTY
     ARDGDAYLIV ASKGGDPRSP GWYHNLKANP DVEINVGPKR FGVTAKPVQP HDPDYARLWQ
     IVNENNANRY TNYQSRTSRP IPVVVLTRR