FQR61_MYCTU
ID FQR61_MYCTU Reviewed; 149 AA.
AC P9WP13; 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 39.
DE RecName: Full=F420H(2)-dependent quinone reductase Rv1261c {ECO:0000303|PubMed:23240649};
DE Short=Fqr {ECO:0000303|PubMed:23240649};
DE EC=1.1.98.- {ECO:0000269|PubMed:23240649};
GN OrderedLocusNames=Rv1261c; ORFNames=MTCY50.21;
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).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RC STRAIN=H37Rv;
RX PubMed=16000731; DOI=10.1099/mic.0.27799-0;
RA Sinha S., Kosalai K., Arora S., Namane A., Sharma P., Gaikwad A.N.,
RA Brodin P., Cole S.T.;
RT "Immunogenic membrane-associated proteins of Mycobacterium tuberculosis
RT revealed by proteomics.";
RL Microbiology 151:2411-2419(2005).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
RN [4]
RP FUNCTION AS A F420-DEPENDENT QUINONE REDUCTASE, CATALYTIC ACTIVITY, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=ATCC 27294 / TMC 102 / H37Rv;
RX PubMed=23240649; DOI=10.1111/mmi.12127;
RA Gurumurthy M., Rao M., Mukherjee T., Rao S.P., Boshoff H.I., Dick T.,
RA Barry C.E. III, Manjunatha U.H.;
RT "A novel F(420)-dependent anti-oxidant mechanism protects Mycobacterium
RT tuberculosis against oxidative stress and bactericidal agents.";
RL Mol. Microbiol. 87:744-755(2013).
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:0000269|PubMed:23240649}.
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:0000269|PubMed:23240649};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=47.1 uM for menadione {ECO:0000269|PubMed:23240649};
CC Note=kcat is 18.7 min(-1) for the reduction of menadione.
CC {ECO:0000269|PubMed:23240649};
CC -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein
CC {ECO:0000269|PubMed:16000731}.
CC -!- SIMILARITY: Belongs to the F420H(2)-dependent quinone reductase family.
CC {ECO:0000305}.
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DR EMBL; AL123456; CCP44017.1; -; Genomic_DNA.
DR PIR; E70753; E70753.
DR RefSeq; NP_215777.1; NC_000962.3.
DR RefSeq; WP_003406364.1; NZ_NVQJ01000049.1.
DR AlphaFoldDB; P9WP13; -.
DR SMR; P9WP13; -.
DR STRING; 83332.Rv1261c; -.
DR PaxDb; P9WP13; -.
DR DNASU; 887055; -.
DR GeneID; 887055; -.
DR KEGG; mtu:Rv1261c; -.
DR TubercuList; Rv1261c; -.
DR eggNOG; COG3945; Bacteria.
DR OMA; NGWIGHR; -.
DR PhylomeDB; P9WP13; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0009274; C:peptidoglycan-based cell wall; HDA:MTBBASE.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
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 1: Evidence at protein level;
KW Cell membrane; Membrane; Oxidoreductase; Reference proteome.
FT CHAIN 1..149
FT /note="F420H(2)-dependent quinone reductase Rv1261c"
FT /id="PRO_0000103778"
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
