FQR84_MYCBO
ID FQR84_MYCBO Reviewed; 148 AA.
AC P64876; A0A1R3XYP7; Q10772; X2BHX8;
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 Mb1584 {ECO:0000305};
DE Short=Fqr;
DE EC=1.1.98.-;
GN OrderedLocusNames=BQ2027_MB1584;
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; SIU00187.1; -; Genomic_DNA.
DR RefSeq; NP_855236.1; NC_002945.3.
DR RefSeq; WP_003407780.1; NC_002945.4.
DR AlphaFoldDB; P64876; -.
DR SMR; P64876; -.
DR EnsemblBacteria; SIU00187; SIU00187; BQ2027_MB1584.
DR PATRIC; fig|233413.5.peg.1731; -.
DR OMA; NPVWYYN; -.
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..148
FT /note="Putative F420H(2)-dependent quinone reductase
FT Mb1584"
FT /id="PRO_0000103880"
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