QR2_TRIVS
ID QR2_TRIVS Reviewed; 205 AA.
AC Q9AYU0;
DT 12-APR-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=Quinone-oxidoreductase QR2 {ECO:0000303|PubMed:11260494};
DE Short=TvQR2 {ECO:0000303|PubMed:11260494};
DE EC=1.6.5.2 {ECO:0000269|Ref.2};
OS Triphysaria versicolor (Yellow owl's clover).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Lamiales; Orobanchaceae; Pedicularideae; Castillejinae;
OC Triphysaria.
OX NCBI_TaxID=64093 {ECO:0000312|EMBL:AAG53945.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND INDUCTION BY QUINONES.
RC TISSUE=Root;
RX PubMed=11260494; DOI=10.1046/j.1365-313x.2001.00971.x;
RA Matvienko M., Wojtowicz A., Wrobel R., Jamison D., Goldwasser Y.,
RA Yoder J.I.;
RT "Quinone oxidoreductase message levels are differentially regulated in
RT parasitic and non-parasitic plants exposed to allelopathic quinones.";
RL Plant J. 25:375-387(2001).
RN [2]
RP FUNCTION, SUBSTRATE SPECIFICITY, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND ACTIVITY REGULATION.
RX DOI=10.1016/S0981-9428(02)01361-X;
RA Wrobel R.L., Matvienko M., Yoder J.I.;
RT "Heterologous expression and biochemical characterization of an
RT NAD(P)H:quinone oxidoreductase from the hemiparasitic plant Triphysaria
RT versicolor.";
RL Plant Physiol. Biochem. 40:265-272(2002).
RN [3]
RP INDUCTION BY ROOT CONTACT.
RX PubMed=20424175; DOI=10.1105/tpc.110.074831;
RA Bandaranayake P.C., Filappova T., Tomilov A., Tomilova N.B.,
RA Jamison-McClung D., Ngo Q., Inoue K., Yoder J.I.;
RT "A single-electron reducing quinone oxidoreductase is necessary to induce
RT haustorium development in the root parasitic plant Triphysaria.";
RL Plant Cell 22:1404-1419(2010).
CC -!- FUNCTION: NAD(P)H:quinone oxidoreductase reducing quinones by a two-
CC electron transfer mechanism (PubMed:11260494, Ref.2). Can use either
CC NADPH or NADH as electron donor (Ref.2). Can use menadione, 5-hydroxy-
CC 1,4-naphthoquinone (juglone) and 2,6-dimethoxy-p-benzoquinone (DMBQ) as
CC substrates (Ref.2). Mitigates the toxicity of exogenous quinones in the
CC rhizosphere (Ref.2). {ECO:0000269|PubMed:11260494, ECO:0000269|Ref.2}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a quinone + H(+) + NADH = a quinol + NAD(+);
CC Xref=Rhea:RHEA:46160, ChEBI:CHEBI:15378, ChEBI:CHEBI:24646,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:132124; EC=1.6.5.2;
CC Evidence={ECO:0000269|Ref.2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a quinone + H(+) + NADPH = a quinol + NADP(+);
CC Xref=Rhea:RHEA:46164, ChEBI:CHEBI:15378, ChEBI:CHEBI:24646,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:132124; EC=1.6.5.2;
CC Evidence={ECO:0000269|Ref.2};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000250|UniProtKB:Q9LSQ5};
CC Note=Binds 1 FMN per monomer. {ECO:0000250|UniProtKB:Q9LSQ5};
CC -!- ACTIVITY REGULATION: Inhibited by dicumarol. {ECO:0000269|Ref.2}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 6.5. {ECO:0000269|Ref.2};
CC -!- INDUCTION: Up-regulated by 2,6-dimethoxy-p-benzoquinone (DMBQ), 2,6-
CC dimethylbenzoquinone and menadione (PubMed:11260494, PubMed:20424175).
CC Not regulated by host root contact (PubMed:20424175).
CC {ECO:0000269|PubMed:11260494, ECO:0000269|PubMed:20424175}.
CC -!- SIMILARITY: Belongs to the WrbA family. {ECO:0000305}.
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DR EMBL; AF304462; AAG53945.1; -; mRNA.
DR AlphaFoldDB; Q9AYU0; -.
DR SMR; Q9AYU0; -.
DR GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR GO; GO:0050136; F:NADH dehydrogenase (quinone) activity; IEA:RHEA.
DR GO; GO:0008753; F:NADPH dehydrogenase (quinone) activity; IEA:RHEA.
DR Gene3D; 3.40.50.360; -; 1.
DR InterPro; IPR008254; Flavodoxin/NO_synth.
DR InterPro; IPR029039; Flavoprotein-like_sf.
DR InterPro; IPR010089; Flavoprotein_WrbA-like.
DR InterPro; IPR005025; FMN_Rdtase-like.
DR Pfam; PF03358; FMN_red; 1.
DR SUPFAM; SSF52218; SSF52218; 1.
DR TIGRFAMs; TIGR01755; flav_wrbA; 1.
DR PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
PE 1: Evidence at protein level;
KW Flavoprotein; FMN; NAD; NADP; Nucleotide-binding; Oxidoreductase.
FT CHAIN 1..205
FT /note="Quinone-oxidoreductase QR2"
FT /id="PRO_0000439503"
FT DOMAIN 5..192
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00088"
FT BINDING 11..15
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00088"
FT BINDING 13
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P0A8G6"
FT BINDING 112..165
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00088"
FT BINDING 136
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:P0A8G6"
SQ SEQUENCE 205 AA; 22100 MW; A90998C4DBFAC6A6 CRC64;
MATKVYIVYY STYGHVERLA QEIKKGAESV GNVEVKLWQV PEILSDEVLG KMWAPPKSDV
PVITPDELVE ADGIIFGFPT RFGMMAAQFK AFFDSTGGLW KTQALAGKPA GIFFSTGTQG
GGQETTALTA ITQLTHHGMI YVPIGYTFGA DMFNMEKIKG GSPYGAGTFA GADGSRQPSD
IELKQAFHQG MYIAGITKKI KQTSA
