FQR58_MYCTU
ID FQR58_MYCTU Reviewed; 148 AA.
AC P9WP11; 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 40.
DE RecName: Full=F420H(2)-dependent quinone reductase Rv1558 {ECO:0000303|PubMed:23240649};
DE Short=Fqr {ECO:0000303|PubMed:23240649};
DE EC=1.1.98.- {ECO:0000269|PubMed:23240649};
GN OrderedLocusNames=Rv1558; ORFNames=MTCY48.07c;
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, DETERMINATION OF TRANSLATIONAL START
RP SITE, AND CLEAVAGE OF INITIATOR METHIONINE.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=17259624; DOI=10.1099/mic.0.2006/001537-0;
RA Rison S.C., Mattow J., Jungblut P.R., Stoker N.G.;
RT "Experimental determination of translational starts using peptide mass
RT mapping and tandem mass spectrometry within the proteome of Mycobacterium
RT tuberculosis.";
RL Microbiology 153:521-528(2007).
RN [3]
RP IDENTIFICATION AS A DRUG TARGET [LARGE SCALE ANALYSIS].
RX PubMed=19099550; DOI=10.1186/1752-0509-2-109;
RA Raman K., Yeturu K., Chandra N.;
RT "targetTB: a target identification pipeline for Mycobacterium tuberculosis
RT through an interactome, reactome and genome-scale structural analysis.";
RL BMC Syst. Biol. 2:109-109(2008).
RN [4]
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 [5]
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=17.3 uM for menadione {ECO:0000269|PubMed:23240649};
CC Note=kcat is 98 min(-1) for the reduction of menadione.
CC {ECO:0000269|PubMed:23240649};
CC -!- MISCELLANEOUS: Was identified as a high-confidence drug target.
CC {ECO:0000305|PubMed:19099550}.
CC -!- SIMILARITY: Belongs to the F420H(2)-dependent quinone reductase family.
CC {ECO:0000305}.
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DR EMBL; AL123456; CCP44322.1; -; Genomic_DNA.
DR PIR; C70763; C70763.
DR RefSeq; NP_216074.1; NC_000962.3.
DR RefSeq; WP_003407780.1; NZ_NVQJ01000004.1.
DR PDB; 7KL8; X-ray; 2.47 A; A/B=6-145.
DR PDBsum; 7KL8; -.
DR AlphaFoldDB; P9WP11; -.
DR SMR; P9WP11; -.
DR STRING; 83332.Rv1558; -.
DR PaxDb; P9WP11; -.
DR DNASU; 886363; -.
DR GeneID; 886363; -.
DR KEGG; mtu:Rv1558; -.
DR TubercuList; Rv1558; -.
DR eggNOG; COG1846; Bacteria.
DR OMA; NPVWYYN; -.
DR PhylomeDB; P9WP11; -.
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 3D-structure; Oxidoreductase; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:17259624"
FT CHAIN 2..148
FT /note="F420H(2)-dependent quinone reductase Rv1558"
FT /id="PRO_0000103879"
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"
FT HELIX 11..24
FT /evidence="ECO:0007829|PDB:7KL8"
FT TURN 25..27
FT /evidence="ECO:0007829|PDB:7KL8"
FT STRAND 28..30
FT /evidence="ECO:0007829|PDB:7KL8"
FT STRAND 36..44
FT /evidence="ECO:0007829|PDB:7KL8"
FT TURN 46..48
FT /evidence="ECO:0007829|PDB:7KL8"
FT STRAND 51..57
FT /evidence="ECO:0007829|PDB:7KL8"
FT STRAND 59..61
FT /evidence="ECO:0007829|PDB:7KL8"
FT STRAND 64..68
FT /evidence="ECO:0007829|PDB:7KL8"
FT HELIX 80..86
FT /evidence="ECO:0007829|PDB:7KL8"
FT STRAND 89..94
FT /evidence="ECO:0007829|PDB:7KL8"
FT STRAND 97..105
FT /evidence="ECO:0007829|PDB:7KL8"
FT HELIX 108..121
FT /evidence="ECO:0007829|PDB:7KL8"
FT HELIX 124..130
FT /evidence="ECO:0007829|PDB:7KL8"
FT STRAND 138..143
FT /evidence="ECO:0007829|PDB:7KL8"
SQ SEQUENCE 148 AA; 16348 MW; A9F98E90398719B8 CRC64;
MPLSGEYAPS PLDWSREQAD TYMKSGGTEG TQLQGKPVIL LTTVGAKTGK LRKTPLMRVE
HDGQYAIVAS LGGAPKNPVW YHNVVKNPRV ELQDGTVTGD YDAREVFGDE KAIWWQRAVA
VWPDYASYQT KTDRQIPVFV LTPVRAGG
