QORH_ARATH
ID QORH_ARATH Reviewed; 329 AA.
AC Q9SV68;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Chloroplast envelope quinone oxidoreductase homolog {ECO:0000303|PubMed:20424175};
DE Short=ceQORH {ECO:0000303|PubMed:20424175};
DE EC=1.3.1.- {ECO:0000269|PubMed:26678323};
GN Name=CEQORH {ECO:0000303|PubMed:20424175};
GN OrderedLocusNames=At4g13010 {ECO:0000312|Araport:AT4G13010};
GN ORFNames=F25G13_100 {ECO:0000312|EMBL:CAB45500.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP SUBCELLULAR LOCATION, AND DOMAIN.
RX PubMed=17636260; DOI=10.1074/jbc.m611112200;
RA Miras S., Salvi D., Piette L., Seigneurin-Berny D., Grunwald D.,
RA Reinbothe C., Joyard J., Reinbothe S., Rolland N.;
RT "Toc159- and Toc75-independent import of a transit sequence-less precursor
RT into the inner envelope of chloroplasts.";
RL J. Biol. Chem. 282:29482-29492(2007).
RN [5]
RP LACK OF INDUCTION, AND SUBCELLULAR 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).
RN [6]
RP INTERACTION WITH CALMODULIN.
RX PubMed=23549413; DOI=10.1039/c3mb00004d;
RA Dell'Aglio E., Giustini C., Salvi D., Brugiere S., Delpierre F., Moyet L.,
RA Baudet M., Seigneurin-Berny D., Matringe M., Ferro M., Rolland N.,
RA Curien G.;
RT "Complementary biochemical approaches applied to the identification of
RT plastidial calmodulin-binding proteins.";
RL Mol. Biosyst. 9:1234-1248(2013).
RN [7]
RP INTERACTION WITH HP30-1; HP30-2 AND HP20, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=24248378; DOI=10.1073/pnas.1319648110;
RA Rossig C., Reinbothe C., Gray J., Valdes O., von Wettstein D.,
RA Reinbothe S.;
RT "Three proteins mediate import of transit sequence-less precursors into the
RT inner envelope of chloroplasts in Arabidopsis thaliana.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:19962-19967(2013).
RN [8]
RP CRYSTALLIZATION, AND SUBUNIT.
RX PubMed=25849509; DOI=10.1107/s2053230x1500480x;
RA Mas y mas S., Giustini C., Ferrer J.L., Rolland N., Curien G., Cobessi D.;
RT "Analytical ultracentrifugation and preliminary X-ray studies of the
RT chloroplast envelope quinone oxidoreductase homologue from Arabidopsis
RT thaliana.";
RL Acta Crystallogr. F Struct. Biol. Commun. 71:455-458(2015).
RN [9]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RX PubMed=26678323; DOI=10.1016/j.phytochem.2015.11.015;
RA Curien G., Giustini C., Montillet J.L., Mas-Y-Mas S., Cobessi D.,
RA Ferrer J.L., Matringe M., Grechkin A., Rolland N.;
RT "The chloroplast membrane associated ceQORH putative quinone oxidoreductase
RT reduces long-chain, stress-related oxidized lipids.";
RL Phytochemistry 122:45-55(2016).
RN [10] {ECO:0007744|PDB:5A3J, ECO:0007744|PDB:5A3V, ECO:0007744|PDB:5A4D}
RP X-RAY CRYSTALLOGRAPHY (2.34 ANGSTROMS) IN COMPLEX WITH
RP 13-OXO-9(Z),11(E),15(Z)-OCTADECATRIENOIC ACID.
RA Mas-Y-Mas S., Curien G., Giustini C., Rolland N., Ferrer J.L., Cobessi D.;
RT "Crystal structure of the chloroplastic gamma-ketol reductase from
RT Arabidopsis thaliana.";
RL Submitted (JUN-2015) to the PDB data bank.
CC -!- FUNCTION: NADPH-dependent alpha,beta-unsaturated oxoene reductase
CC reducing the double bond of medium-chain (C9) to long-chain (C18)
CC reactive electrophile species deriving from poly-unsaturated fatty acid
CC peroxides. The best substrates are 13-lipoxygenase-derived gamma-
CC ketols, but is unable to reduce the double bond of short-chain alkenals
CC and alkenones such as acrolein, crotonaldehyde, 3-buten-2-one, 4-hexen-
CC 3-one and trans-2-hexenal, or quinones such as duroquinone,
CC decylubiquinone, coenzyme Q0, menadione, menaquinone and phylloquinone.
CC Can use trans-2-nonenal, trans-3-decen-2-one, 4-hydroxynonenal, 12-oxo-
CC 10(E) dodecanoate (traumatin), 4-oxononenal, trans-1,3 diphenyl-2-
CC propenone, trans-1,4-diphenyl-2-butene-1,4-dione, 9-oxo-12,13-epoxy-
CC (10E)-octadecenoic acid (trans-EKODE-1b), 9-hydroxy-12-oxo-10(E)-
CC octadecenoic acid, 9-Hydroxy-12-oxo-10(E),15(Z)-octadecadienoic acid
CC and 9,13-dihydroxy-10-oxo-11-octadecenoic acid as substrates, but has
CC no activity with 13(R,S)-hydroperoxy-9(Z),11(E)-octadecadienoic acid
CC (13-HPOD), 9(S),12(S),13(S)-trihydroxy-10(E)-octadecenoic acid, 13-
CC hydroxy-12-oxo-9(Z)-octadecenoic acid, 9-oxo-10(E),12(Z)-
CC octadecadienoic acid (9-KODE), 13-oxo-9(Z),11(E)-octadecadienoic acid
CC (13-KODE) and 12-oxo-10,15(Z)-phytodienoic acid (12-OPDA).
CC {ECO:0000269|PubMed:26678323}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=200 uM for 4-oxo-nonenal {ECO:0000269|PubMed:26678323};
CC KM=9 uM for trans-1,4-diphenyl-2-butene-1,4-dione
CC {ECO:0000269|PubMed:26678323};
CC KM=14 uM for 9-hydroxy-12-oxo-10(E)-octadecenoic acid
CC {ECO:0000269|PubMed:26678323};
CC KM=10 uM for 9-Hydroxy-12-oxo-10(E),15(Z)-octadecadienoic acid
CC {ECO:0000269|PubMed:26678323};
CC Note=kcat is 14 sec(-1) for 4-oxo-nonenal. kcat is 4.5 sec(-1) for
CC trans-1,4-diphenyl-2-butene-1,4-dione. kcat is 6 sec(-1) for 9-
CC hydroxy-12-oxo-10(E)-octadecenoic acid. kcat is 3 sec(-1) for 9-
CC Hydroxy-12-oxo-10(E),15(Z)-octadecadienoic acid.
CC {ECO:0000269|PubMed:26678323};
CC -!- SUBUNIT: Homodimer or homotetramer (PubMed:25849509). Transition to
CC monomer upon NADPH binding (PubMed:25849509). Interacts with calmodulin
CC (PubMed:23549413). Interacts with HP30-1, HP30-2 and HP20
CC (PubMed:24248378). {ECO:0000269|PubMed:23549413,
CC ECO:0000269|PubMed:24248378, ECO:0000269|PubMed:25849509}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast inner membrane
CC {ECO:0000269|PubMed:17636260, ECO:0000269|PubMed:20424175,
CC ECO:0000269|PubMed:24248378}. Note=Faces the stroma side of the
CC membrane (PubMed:20424175). Targeting to the chloroplast inner membrane
CC is mediated by HP30-1, HP30-2 and HP20 (PubMed:24248378).
CC {ECO:0000269|PubMed:20424175, ECO:0000269|PubMed:24248378}.
CC -!- INDUCTION: Not regulated by 2,6-dimethoxy-p-benzoquinone (DMBQ).
CC {ECO:0000269|PubMed:20424175}.
CC -!- DOMAIN: A nonterminal hydrophilic domain (59-100) is essential for
CC targeting to the chloroplast. The C-terminal part (101-329) is
CC necessary and sufficient to select for the import site.
CC {ECO:0000269|PubMed:17636260}.
CC -!- MISCELLANEOUS: The trimeric TOC159/75/34 complex is not involved in
CC chloroplast import of CEQORH. {ECO:0000269|PubMed:17636260}.
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. Quinone oxidoreductase subfamily. {ECO:0000305}.
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DR EMBL; AL079349; CAB45500.1; -; Genomic_DNA.
DR EMBL; AL161535; CAB78343.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE83213.1; -; Genomic_DNA.
DR EMBL; AY045857; AAK76531.1; -; mRNA.
DR EMBL; AF412068; AAL06521.1; -; mRNA.
DR EMBL; AY117154; AAM51229.1; -; mRNA.
DR EMBL; AY056396; AAL08252.1; -; mRNA.
DR PIR; T10203; T10203.
DR RefSeq; NP_193037.1; NM_117370.3.
DR PDB; 5A3J; X-ray; 2.78 A; A/B/C/D/E/F/G/H/I/J/K/L=1-329.
DR PDB; 5A3V; X-ray; 2.34 A; A/B=1-329.
DR PDB; 5A4D; X-ray; 2.81 A; A/B/C/D/E/F/G/H=1-329.
DR PDBsum; 5A3J; -.
DR PDBsum; 5A3V; -.
DR PDBsum; 5A4D; -.
DR AlphaFoldDB; Q9SV68; -.
DR SMR; Q9SV68; -.
DR STRING; 3702.AT4G13010.1; -.
DR PaxDb; Q9SV68; -.
DR PRIDE; Q9SV68; -.
DR ProteomicsDB; 236602; -.
DR EnsemblPlants; AT4G13010.1; AT4G13010.1; AT4G13010.
DR GeneID; 826914; -.
DR Gramene; AT4G13010.1; AT4G13010.1; AT4G13010.
DR KEGG; ath:AT4G13010; -.
DR Araport; AT4G13010; -.
DR TAIR; locus:2123206; AT4G13010.
DR eggNOG; KOG1198; Eukaryota.
DR HOGENOM; CLU_026673_3_3_1; -.
DR InParanoid; Q9SV68; -.
DR OMA; MKAWLYS; -.
DR OrthoDB; 727365at2759; -.
DR PhylomeDB; Q9SV68; -.
DR PRO; PR:Q9SV68; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9SV68; baseline and differential.
DR Genevisible; Q9SV68; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR GO; GO:0009706; C:chloroplast inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; HDA:TAIR.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
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 3D-structure; Chloroplast; Membrane; NAD; Oxidoreductase; Plastid;
KW Plastid inner membrane; Reference proteome.
FT CHAIN 1..329
FT /note="Chloroplast envelope quinone oxidoreductase homolog"
FT /id="PRO_0000160915"
FT BINDING 58
FT /ligand="substrate"
FT /evidence="ECO:0000269|Ref.10, ECO:0007744|PDB:5A4D"
FT STRAND 5..11
FT /evidence="ECO:0007829|PDB:5A3V"
FT HELIX 18..20
FT /evidence="ECO:0007829|PDB:5A3V"
FT STRAND 22..27
FT /evidence="ECO:0007829|PDB:5A3V"
FT STRAND 35..44
FT /evidence="ECO:0007829|PDB:5A3V"
FT HELIX 47..54
FT /evidence="ECO:0007829|PDB:5A3V"
FT TURN 55..60
FT /evidence="ECO:0007829|PDB:5A3V"
FT STRAND 61..67
FT /evidence="ECO:0007829|PDB:5A3V"
FT STRAND 72..80
FT /evidence="ECO:0007829|PDB:5A3V"
FT STRAND 92..96
FT /evidence="ECO:0007829|PDB:5A3V"
FT HELIX 98..100
FT /evidence="ECO:0007829|PDB:5A3V"
FT STRAND 105..112
FT /evidence="ECO:0007829|PDB:5A3V"
FT HELIX 113..115
FT /evidence="ECO:0007829|PDB:5A3V"
FT STRAND 116..118
FT /evidence="ECO:0007829|PDB:5A3V"
FT HELIX 125..129
FT /evidence="ECO:0007829|PDB:5A3V"
FT HELIX 132..143
FT /evidence="ECO:0007829|PDB:5A3V"
FT STRAND 150..152
FT /evidence="ECO:0007829|PDB:5A3V"
FT STRAND 158..163
FT /evidence="ECO:0007829|PDB:5A3V"
FT HELIX 167..178
FT /evidence="ECO:0007829|PDB:5A3V"
FT STRAND 182..187
FT /evidence="ECO:0007829|PDB:5A3V"
FT HELIX 189..191
FT /evidence="ECO:0007829|PDB:5A3V"
FT HELIX 192..197
FT /evidence="ECO:0007829|PDB:5A3V"
FT STRAND 201..205
FT /evidence="ECO:0007829|PDB:5A3V"
FT HELIX 209..213
FT /evidence="ECO:0007829|PDB:5A3V"
FT STRAND 222..227
FT /evidence="ECO:0007829|PDB:5A3V"
FT HELIX 234..237
FT /evidence="ECO:0007829|PDB:5A3V"
FT HELIX 238..240
FT /evidence="ECO:0007829|PDB:5A3V"
FT STRAND 241..251
FT /evidence="ECO:0007829|PDB:5A3V"
FT HELIX 254..266
FT /evidence="ECO:0007829|PDB:5A3V"
FT STRAND 269..275
FT /evidence="ECO:0007829|PDB:5A3V"
FT HELIX 281..292
FT /evidence="ECO:0007829|PDB:5A3V"
FT STRAND 300..305
FT /evidence="ECO:0007829|PDB:5A3V"
FT HELIX 306..308
FT /evidence="ECO:0007829|PDB:5A3V"
FT HELIX 309..318
FT /evidence="ECO:0007829|PDB:5A3V"
FT STRAND 322..328
FT /evidence="ECO:0007829|PDB:5A3V"
SQ SEQUENCE 329 AA; 34436 MW; 12F5ED95B5F081D6 CRC64;
MAGKLMHALQ YNSYGGGAAG LEHVQVPVPT PKSNEVCLKL EATSLNPVDW KIQKGMIRPF
LPRKFPCIPA TDVAGEVVEV GSGVKNFKAG DKVVAVLSHL GGGGLAEFAV ATEKLTVKRP
QEVGAAEAAA LPVAGLTALQ ALTNPAGLKL DGTGKKANIL VTAASGGVGH YAVQLAKLAN
AHVTATCGAR NIEFVKSLGA DEVLDYKTPE GAALKSPSGK KYDAVVHCAN GIPFSVFEPN
LSENGKVIDI TPGPNAMWTY AVKKITMSKK QLVPLLLIPK AENLEFMVNL VKEGKVKTVI
DSKHPLSKAE DAWAKSIDGH ATGKIIVEP
