ID   FQR92_MYCBO             Reviewed;         149 AA.
AC   P64788; A0A1R3XYS7; Q11057; X2BH95;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=Putative F420H(2)-dependent quinone reductase Mb1292c {ECO:0000305};
DE            Short=Fqr;
DE            EC=1.1.98.-;
GN   OrderedLocusNames=BQ2027_MB1292C;
OS   Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=233413;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-935 / AF2122/97;
RX   PubMed=12788972; DOI=10.1073/pnas.1130426100;
RA   Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., Pryor M.,
RA   Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B.,
RA   Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J.,
RA   Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G.;
RT   "The complete genome sequence of Mycobacterium bovis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC   STRAIN=ATCC BAA-935 / AF2122/97;
RX   PubMed=28385856; DOI=10.1128/genomea.00157-17;
RA   Malone K.M., Farrell D., Stuber T.P., Schubert O.T., Aebersold R.,
RA   Robbe-Austerman S., Gordon S.V.;
RT   "Updated reference genome sequence and annotation of Mycobacterium bovis
RT   AF2122/97.";
RL   Genome Announc. 5:E00157-E00157(2017).
CC   -!- FUNCTION: Involved in a F420-dependent anti-oxidant mechanism that
CC       protects M.bovis against oxidative stress and bactericidal agents.
CC       Catalyzes the F420H(2)-dependent two-electron reduction of quinones to
CC       dihydroquinones, thereby preventing the formation of cytotoxic
CC       semiquinones obtained by the one-electron reduction pathway.
CC       {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; LT708304; SIT99893.1; -; Genomic_DNA.
DR   RefSeq; NP_854946.1; NC_002945.3.
DR   RefSeq; WP_003406364.1; NC_002945.4.
DR   AlphaFoldDB; P64788; -.
DR   SMR; P64788; -.
DR   EnsemblBacteria; SIT99893; SIT99893; BQ2027_MB1292C.
DR   PATRIC; fig|233413.5.peg.1417; -.
DR   OMA; NGWIGHR; -.
DR   Proteomes; UP000001419; 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="Putative F420H(2)-dependent quinone reductase
FT                   Mb1292c"
FT                   /id="PRO_0000103779"
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