ID   QR1_TRIVS               Reviewed;         329 AA.
AC   Q9AYU1;
DT   12-APR-2017, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   25-MAY-2022, entry version 62.
DE   RecName: Full=Quinone-oxidoreductase QR1, chloroplastic {ECO:0000303|PubMed:11260494};
DE            Short=TvQR1 {ECO:0000303|PubMed:11260494};
DE            EC=1.6.5.5 {ECO:0000269|PubMed:20424175};
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:AAG53944.1};
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], 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, ACTIVITY REGULATION, INDUCTION BY ROOT CONTACT, AND SUBCELLULAR
RP   LOCATION.
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: NADPH-dependent single-electron reducing quinone reductase
CC       (PubMed:20424175). Involved in haustorium initiation in parasitic
CC       plants through redox cycling of exogenous haustorium-inducing factors
CC       (PubMed:20424175). Can use 9,10-phenanthrenequinone (PAQ), 1,2-
CC       naphthoquinone, 5-hydroxy-1,4-naphthoquinone (juglone) and 2,6-
CC       dimethoxy-p-benzoquinone (DMBQ) as substrates, but has no activity with
CC       menadione, diamide, 2,3-dimethoxy-5-methyl-1,4-benzoquinone or 1,4-
CC       naphthoquinone (PubMed:20424175). {ECO:0000269|PubMed:20424175}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 a quinone + H(+) + NADPH = 2 a 1,4-benzosemiquinone +
CC         NADP(+); Xref=Rhea:RHEA:14269, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:58349, ChEBI:CHEBI:132124, ChEBI:CHEBI:134225;
CC         EC=1.6.5.5; Evidence={ECO:0000269|PubMed:20424175};
CC   -!- ACTIVITY REGULATION: Inhibited by dicumarol.
CC       {ECO:0000269|PubMed:20424175}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         Note=kcat is 23.3 sec(-1) with 9,10-phenanthrenequinone as substrate.
CC         kcat is 2.44 sec(-1) with 1,2-naphthoquinone as substrate. kcat is
CC         0.31 sec(-1) with 5-hydroxy-1,4-naphthoquinone as substrate. kcat is
CC         0.09 sec(-1) with 2,6-dimethoxy-p-benzoquinone.
CC         {ECO:0000269|PubMed:20424175};
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast outer membrane
CC       {ECO:0000269|PubMed:20424175}.
CC   -!- INDUCTION: Up-regulated by 2,6-dimethoxy-p-benzoquinone (DMBQ), 5-
CC       hydroxy-1,4-naphthoquinone (juglone), 2,6-dimethylbenzoquinone and
CC       menadione (PubMed:11260494, PubMed:20424175). Up-regulated by host root
CC       contact (PubMed:20424175). {ECO:0000269|PubMed:11260494,
CC       ECO:0000269|PubMed:20424175}.
CC   -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC       family. Quinone oxidoreductase subfamily. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AF304461; AAG53944.1; -; mRNA.
DR   AlphaFoldDB; Q9AYU1; -.
DR   SMR; Q9AYU1; -.
DR   GO; GO:0009707; C:chloroplast outer membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0003960; F:NADPH:quinone reductase activity; IEA:UniProtKB-EC.
DR   InterPro; IPR013154; ADH_N.
DR   InterPro; IPR011032; GroES-like_sf.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020843; PKS_ER.
DR   Pfam; PF08240; ADH_N; 1.
DR   SMART; SM00829; PKS_ER; 1.
DR   SUPFAM; SSF50129; SSF50129; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
PE   1: Evidence at protein level;
KW   Chloroplast; Membrane; NADP; Oxidoreductase; Plastid;
KW   Plastid outer membrane.
FT   CHAIN           1..329
FT                   /note="Quinone-oxidoreductase QR1, chloroplastic"
FT                   /id="PRO_0000439502"
SQ   SEQUENCE   329 AA;  34872 MW;  57D21A720295A1E0 CRC64;
     MAGKLMRAVQ YDGYGGGAAG LKHVEVPIPS PGKGEVLIKL EAISLNQLDW KLQNGMVRPF
     LPRKFPFIPA TDVAGEVVRI GQDVKNFKPG DKVVAMLGSF GGGGLAEYGV ASEKLTVHRP
     PEVSAAESSG LPIAGLTAHM ALTQHIGLNL DKSGPHKNIL ITAASGGVGQ YAVQLAKLGN
     THVTATCGSR NFDLVKSLGA DEVIDYKTPE GAALKSPSGK KYDAVIHCAS PLPWSVFKPN
     LSKHGKVIDI TPGPRVMLTS AMTKLTCSKK RLVTLLVVIK GEHLSYLVEL MREGKLKTVI
     DSKFSLSKAE EAWAKSIDGH ATGKIVVEP