OPR3_ARATH
ID OPR3_ARATH Reviewed; 391 AA.
AC Q9FUP0; B9DGR2; Q9LLD6; Q9SCY4; Q9XHD2; Q9ZQ01;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 2.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=12-oxophytodienoate reductase 3 {ECO:0000303|PubMed:10872231};
DE EC=1.3.1.42 {ECO:0000269|PubMed:10872231, ECO:0000269|PubMed:11094980, ECO:0000269|Ref.4};
DE AltName: Full=12-oxophytodienoate-10,11-reductase 3 {ECO:0000303|PubMed:10872231};
DE Short=AtOPR3 {ECO:0000303|PubMed:10872231};
DE Short=OPDA-reductase 3 {ECO:0000303|PubMed:10872231};
DE AltName: Full=Protein DELAYED DEHISCENCE 1 {ECO:0000303|PubMed:10899973};
DE Contains:
DE RecName: Full=12-oxophytodienoate reductase 3, N-terminally processed {ECO:0000305};
GN Name=OPR3 {ECO:0000303|PubMed:10872231};
GN Synonyms=DDE1 {ECO:0000303|PubMed:10899973};
GN OrderedLocusNames=At2g06050 {ECO:0000312|Araport:AT2G06050};
GN ORFNames=F5K7.19 {ECO:0000312|EMBL:AAD19764.1};
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 [MRNA], FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES,
RP CATALYTIC ACTIVITY, COFACTOR, INDUCTION, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=11094980; DOI=10.1023/a:1006464822434;
RA Costa C.L., Arruda P., Benedetti C.E.;
RT "An Arabidopsis gene induced by wounding functionally homologous to
RT flavoprotein oxidoreductases.";
RL Plant Mol. Biol. 44:61-71(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RC STRAIN=cv. Wassilewskija;
RX PubMed=10899973; DOI=10.2307/3871254;
RA Sanders P.M., Lee P.Y., Biesgen C., Boone J.D., Beals T.P., Weiler E.W.,
RA Goldberg R.B.;
RT "The Arabidopsis DELAYED DEHISCENCE1 gene encodes an enzyme in the jasmonic
RT acid synthesis pathway.";
RL Plant Cell 12:1041-1061(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=cv. Wassilewskija;
RX PubMed=10973494; DOI=10.1073/pnas.190264497;
RA Stintzi A., Browse J.;
RT "The Arabidopsis male-sterile mutant, opr3, lacks a 12-oxo-phytodienoic
RT acid reductase required for jasmonate synthesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:10625-10630(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA], INDUCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=cv. Columbia;
RA Muessig C., Biesgen C., Lisso J., Uwer U., Weiler E.W., Altmann T.;
RT "A novel stress-inducible 12-oxo-phytodienoate reductase from Arabidopsis
RT thaliana provides a potential link between brassinosteroid-action and
RT jasmonic acid synthesis.";
RL J. Plant Physiol. 157:143-152(2000).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [6]
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 [7]
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 [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [9]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RX PubMed=10872231; DOI=10.1007/s004250050706;
RA Schaller F., Biesgen C., Muessig C., Altmann T., Weiler E.W.;
RT "12-Oxophytodienoate reductase 3 (OPR3) is the isoenzyme involved in
RT jasmonate biosynthesis.";
RL Planta 210:979-984(2000).
RN [10]
RP SUBCELLULAR LOCATION.
RX PubMed=12445129; DOI=10.1046/j.1365-313x.2002.01449.x;
RA Strassner J., Schaller F., Frick U.B., Howe G.A., Weiler E.W., Amrhein N.,
RA Macheroux P., Schaller A.;
RT "Characterization and cDNA-microarray expression analysis of 12-
RT oxophytodienoate reductases reveals differential roles for octadecanoid
RT biosynthesis in the local versus the systemic wound response.";
RL Plant J. 32:585-601(2002).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=17951448; DOI=10.1105/tpc.107.050989;
RA Reumann S., Babujee L., Ma C., Wienkoop S., Siemsen T., Antonicelli G.E.,
RA Rasche N., Lueder F., Weckwerth W., Jahn O.;
RT "Proteome analysis of Arabidopsis leaf peroxisomes reveals novel targeting
RT peptides, metabolic pathways, and defense mechanisms.";
RL Plant Cell 19:3170-3193(2007).
RN [12]
RP DISRUPTION PHENOTYPE.
RX PubMed=19765234; DOI=10.1111/j.1365-313x.2009.04023.x;
RA Brioudes F., Joly C., Szecsi J., Varaud E., Leroux J., Bellvert F.,
RA Bertrand C., Bendahmane M.;
RT "Jasmonate controls late development stages of petal growth in Arabidopsis
RT thaliana.";
RL Plant J. 60:1070-1080(2009).
RN [13]
RP FUNCTION.
RX PubMed=19605548; DOI=10.1104/pp.109.141598;
RA Beynon E.R., Symons Z.C., Jackson R.G., Lorenz A., Rylott E.L., Bruce N.C.;
RT "The role of oxophytodienoate reductases in the detoxification of the
RT explosive 2,4,6-trinitrotoluene by Arabidopsis.";
RL Plant Physiol. 151:253-261(2009).
RN [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [15]
RP FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=29291349; DOI=10.1038/nchembio.2540;
RA Chini A., Monte I., Zamarreno A.M., Hamberg M., Lassueur S., Reymond P.,
RA Weiss S., Stintzi A., Schaller A., Porzel A., Garcia-Mina J.M., Solano R.;
RT "An OPR3-independent pathway uses 4,5-didehydrojasmonate for jasmonate
RT synthesis.";
RL Nat. Chem. Biol. 14:171-178(2018).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH FMN, AND COFACTOR.
RX PubMed=15468319; DOI=10.1002/prot.20162;
RA Malone T.E., Madson S.E., Wrobel R.L., Jeon W.B., Rosenberg N.S.,
RA Johnson K.A., Bingman C.A., Smith D.W., Phillips G.N. Jr., Markley J.L.,
RA Fox B.G.;
RT "X-ray structure of Arabidopsis At2g06050, 12-oxophytodienoate reductase
RT isoform 3.";
RL Proteins 58:243-245(2005).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH FMN.
RX PubMed=17850744; DOI=10.1016/j.str.2007.06.019;
RA Levin E.J., Kondrashov D.A., Wesenberg G.E., Phillips G.N. Jr.;
RT "Ensemble refinement of protein crystal structures: validation and
RT application.";
RL Structure 15:1040-1052(2007).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (2.58 ANGSTROMS) IN COMPLEX WITH FMN AND SUBSTRATE,
RP AND ACTIVE SITE.
RX PubMed=21915915; DOI=10.1002/prot.23153;
RA Han B.W., Malone T.E., Kim D.J., Bingman C.A., Kim H.J., Fox B.G.,
RA Phillips G.N. Jr.;
RT "Crystal structure of Arabidopsis thaliana 12-oxophytodienoate reductase
RT isoform 3 in complex with 8-iso prostaglandin A(1).";
RL Proteins 79:3236-3241(2011).
CC -!- FUNCTION: Specifically cleaves olefinic bonds in cyclic enones
CC (PubMed:11094980). Involved in the biosynthesis of jasmonic acid (JA)
CC and perhaps in biosynthesis or metabolism of other oxylipin signaling
CC moleclules (PubMed:29291349, PubMed:10872231, PubMed:10973494).
CC Required for the spatial and temporal regulation of JA levels during
CC dehiscence of anthers, promoting the stomium degeneration program
CC (PubMed:10899973, PubMed:10973494). In vitro, reduces 9S,13S-12-
CC oxophytodienoic acid (9S,13S-OPDA) and 9R,13R-OPDA to 9S,13S-OPC-8:0
CC and 9R,13R-OPC-8:0, respectively (PubMed:10872231). Can detoxify the
CC explosive 2,4,6-trinitrotoluene (TNT) in vitro by catalyzing its
CC nitroreduction to form hydroxylamino-dinitrotoluene (HADNT)
CC (PubMed:19605548). {ECO:0000269|PubMed:10872231,
CC ECO:0000269|PubMed:10899973, ECO:0000269|PubMed:10973494,
CC ECO:0000269|PubMed:11094980, ECO:0000269|PubMed:19605548,
CC ECO:0000269|PubMed:29291349}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NADP(+) + OPC-8 = (10Z,15Z)-12-oxophytodienoate + H(+) +
CC NADPH; Xref=Rhea:RHEA:21888, ChEBI:CHEBI:15378, ChEBI:CHEBI:15720,
CC ChEBI:CHEBI:57411, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.3.1.42;
CC Evidence={ECO:0000269|PubMed:10872231, ECO:0000269|PubMed:11094980,
CC ECO:0000269|Ref.4};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000269|PubMed:11094980, ECO:0000269|PubMed:15468319};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=35 uM for (9S,13S)-OPDA {ECO:0000269|PubMed:10872231,
CC ECO:0000269|PubMed:11094980};
CC KM=2.5 mM for cyclohexenone {ECO:0000269|PubMed:10872231,
CC ECO:0000269|PubMed:11094980};
CC KM=12 uM for NADPH {ECO:0000269|PubMed:10872231,
CC ECO:0000269|PubMed:11094980};
CC Vmax=53.7 nmol/sec/mg enzyme with (9S,13S)-OPDA as substrate
CC {ECO:0000269|PubMed:10872231, ECO:0000269|PubMed:11094980};
CC pH dependence:
CC Optimum pH is 7-8. Active from pH 5.0 to 8.5.
CC {ECO:0000269|PubMed:10872231, ECO:0000269|PubMed:11094980};
CC -!- PATHWAY: Lipid metabolism; oxylipin biosynthesis. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:12445129}.
CC -!- TISSUE SPECIFICITY: Expressed in green seedling, leaves, flowers
CC (anthers, pistil, petal and stamen), and to a lower extent in roots and
CC siliques. Specifically expressed in filament during anther dehiscence
CC initiation. {ECO:0000269|PubMed:10899973, ECO:0000269|PubMed:10973494,
CC ECO:0000269|PubMed:11094980}.
CC -!- DEVELOPMENTAL STAGE: At the initiation time of the stomium degeneration
CC program, expressed in all floral organs. Later, transcripts levels
CC increase in pistil, petal, stamen filament, and in vascular region
CC close to the stamen filament. When the anther dehiscence is initiated,
CC levels of transcripts decrease, except within the vascular tissues.
CC {ECO:0000269|PubMed:10899973}.
CC -!- INDUCTION: Induction mediated by wounding and methyl JA (MeJA) needs
CC COI1. Also induced by BR (24-epibrassinolide), UV LIGHT, wind, touch,
CC and the detergent Sapogenat T-110. Seems to not be influenced by
CC salicylic acid, cold and heat treatments (PubMed:11094980, Ref.4).
CC Induced by infection with the fungal pathogens Botritys cinerea and
CC Alternaria brassicicola, insect feeding with Spodoptera littoralis, and
CC wounding (PubMed:29291349). {ECO:0000269|PubMed:11094980,
CC ECO:0000269|PubMed:29291349, ECO:0000269|Ref.4}.
CC -!- DISRUPTION PHENOTYPE: Male sterility (PubMed:10973494, PubMed:19765234,
CC PubMed:29291349). Fertility can be restored by exogenous jasmonate but
CC not by 12-oxophytodienoic acid (PubMed:10973494, PubMed:19765234,
CC PubMed:29291349). Large petals with altered vein patterning
CC (PubMed:19765234). {ECO:0000269|PubMed:10973494,
CC ECO:0000269|PubMed:19765234, ECO:0000269|PubMed:29291349}.
CC -!- SIMILARITY: Belongs to the NADH:flavin oxidoreductase/NADH oxidase
CC family. {ECO:0000305}.
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DR EMBL; AF132212; AAD38925.1; -; mRNA.
DR EMBL; AF218257; AAF67635.1; -; Genomic_DNA.
DR EMBL; AF293653; AAG15379.1; -; mRNA.
DR EMBL; AJ238149; CAB66143.1; -; mRNA.
DR EMBL; AC006413; AAD19764.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC05998.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC05999.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC06000.1; -; Genomic_DNA.
DR EMBL; AF370582; AAK43901.1; -; mRNA.
DR EMBL; AF410322; AAK95308.1; -; mRNA.
DR EMBL; AY097367; AAM19883.1; -; mRNA.
DR EMBL; AK317250; BAH19929.1; -; mRNA.
DR PIR; F84474; F84474.
DR RefSeq; NP_001077884.1; NM_001084415.2.
DR RefSeq; NP_178662.1; NM_126619.4.
DR RefSeq; NP_973431.1; NM_201702.2.
DR PDB; 1Q45; X-ray; 2.00 A; A/B=1-391.
DR PDB; 2G5W; X-ray; 2.58 A; A/B=1-391.
DR PDB; 2Q3O; X-ray; 2.00 A; A/B=1-391.
DR PDBsum; 1Q45; -.
DR PDBsum; 2G5W; -.
DR PDBsum; 2Q3O; -.
DR AlphaFoldDB; Q9FUP0; -.
DR SMR; Q9FUP0; -.
DR BioGRID; 559; 2.
DR IntAct; Q9FUP0; 3.
DR STRING; 3702.AT2G06050.2; -.
DR SwissLipids; SLP:000001780; -.
DR iPTMnet; Q9FUP0; -.
DR PaxDb; Q9FUP0; -.
DR PRIDE; Q9FUP0; -.
DR ProteomicsDB; 248761; -.
DR DNASU; 815160; -.
DR EnsemblPlants; AT2G06050.1; AT2G06050.1; AT2G06050.
DR EnsemblPlants; AT2G06050.2; AT2G06050.2; AT2G06050.
DR EnsemblPlants; AT2G06050.3; AT2G06050.3; AT2G06050.
DR GeneID; 815160; -.
DR Gramene; AT2G06050.1; AT2G06050.1; AT2G06050.
DR Gramene; AT2G06050.2; AT2G06050.2; AT2G06050.
DR Gramene; AT2G06050.3; AT2G06050.3; AT2G06050.
DR KEGG; ath:AT2G06050; -.
DR Araport; AT2G06050; -.
DR TAIR; locus:2051516; AT2G06050.
DR eggNOG; KOG0134; Eukaryota.
DR HOGENOM; CLU_012153_0_2_1; -.
DR InParanoid; Q9FUP0; -.
DR OMA; QPKGHVS; -.
DR OrthoDB; 978998at2759; -.
DR PhylomeDB; Q9FUP0; -.
DR BioCyc; ARA:AT2G06050-MON; -.
DR BioCyc; MetaCyc:AT2G06050-MON; -.
DR BRENDA; 1.3.1.42; 399.
DR UniPathway; UPA00382; -.
DR EvolutionaryTrace; Q9FUP0; -.
DR PRO; PR:Q9FUP0; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9FUP0; baseline and differential.
DR Genevisible; Q9FUP0; AT.
DR GO; GO:0005777; C:peroxisome; HDA:TAIR.
DR GO; GO:0016629; F:12-oxophytodienoate reductase activity; IDA:TAIR.
DR GO; GO:0010181; F:FMN binding; IDA:UniProtKB.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0009695; P:jasmonic acid biosynthetic process; IMP:TAIR.
DR GO; GO:0031408; P:oxylipin biosynthetic process; IBA:GO_Central.
DR GO; GO:0009620; P:response to fungus; IEP:TAIR.
DR GO; GO:0010193; P:response to ozone; IEP:TAIR.
DR GO; GO:0048443; P:stamen development; IMP:TAIR.
DR Gene3D; 3.20.20.70; -; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR001155; OxRdtase_FMN_N.
DR InterPro; IPR045247; Oye-like.
DR PANTHER; PTHR22893; PTHR22893; 1.
DR Pfam; PF00724; Oxidored_FMN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Fatty acid biosynthesis; Fatty acid metabolism;
KW Flavoprotein; FMN; Lipid biosynthesis; Lipid metabolism; NADP;
KW Oxidoreductase; Oxylipin biosynthesis; Peroxisome; Reference proteome.
FT CHAIN 1..391
FT /note="12-oxophytodienoate reductase 3"
FT /id="PRO_0000434361"
FT INIT_MET 1
FT /note="Removed; alternate"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..391
FT /note="12-oxophytodienoate reductase 3, N-terminally
FT processed"
FT /id="PRO_0000194485"
FT MOTIF 389..391
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000255"
FT ACT_SITE 191
FT /note="Proton donor"
FT /evidence="ECO:0000305|PubMed:21915915"
FT BINDING 31..33
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000269|PubMed:15468319,
FT ECO:0000269|PubMed:17850744, ECO:0000269|PubMed:21915915,
FT ECO:0007744|PDB:1Q45, ECO:0007744|PDB:2G5W,
FT ECO:0007744|PDB:2Q3O"
FT BINDING 64
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000269|PubMed:15468319,
FT ECO:0000269|PubMed:17850744, ECO:0007744|PDB:1Q45,
FT ECO:0007744|PDB:2Q3O"
FT BINDING 106
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000269|PubMed:15468319,
FT ECO:0000269|PubMed:17850744, ECO:0000269|PubMed:21915915,
FT ECO:0007744|PDB:1Q45, ECO:0007744|PDB:2G5W,
FT ECO:0007744|PDB:2Q3O"
FT BINDING 186
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:21915915,
FT ECO:0007744|PDB:2G5W"
FT BINDING 238
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000269|PubMed:15468319,
FT ECO:0000269|PubMed:17850744, ECO:0000269|PubMed:21915915,
FT ECO:0007744|PDB:1Q45, ECO:0007744|PDB:2G5W,
FT ECO:0007744|PDB:2Q3O"
FT BINDING 284
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:21915915,
FT ECO:0007744|PDB:2G5W"
FT BINDING 320..322
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000269|PubMed:15468319,
FT ECO:0000269|PubMed:17850744, ECO:0000269|PubMed:21915915,
FT ECO:0007744|PDB:1Q45, ECO:0007744|PDB:2G5W,
FT ECO:0007744|PDB:2Q3O"
FT BINDING 343..344
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000269|PubMed:15468319,
FT ECO:0000269|PubMed:17850744, ECO:0000269|PubMed:21915915,
FT ECO:0007744|PDB:1Q45, ECO:0007744|PDB:2G5W,
FT ECO:0007744|PDB:2Q3O"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q8GYB8"
FT MOD_RES 2
FT /note="N-acetylthreonine; in 12-oxophytodienoate reductase
FT 3, N-terminally processed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CONFLICT 213
FT /note="A -> E (in Ref. 1; AAD38925, 2; AAF67635 and 3;
FT AAG15379)"
FT /evidence="ECO:0000305"
FT CONFLICT 252
FT /note="D -> N (in Ref. 1; AAD38925, 2; AAF67635, 3;
FT AAG15379 and 4; CAB66143)"
FT /evidence="ECO:0000305"
FT CONFLICT 262
FT /note="G -> D (in Ref. 1; AAD38925, 2; AAF67635, 3;
FT AAG15379 and 4; CAB66143)"
FT /evidence="ECO:0000305"
FT CONFLICT 269
FT /note="G -> D (in Ref. 1; AAD38925, 2; AAF67635, 3;
FT AAG15379 and 4; CAB66143)"
FT /evidence="ECO:0000305"
FT CONFLICT 273
FT /note="S -> L (in Ref. 1; AAD38925, 2; AAF67635, 3;
FT AAG15379 and 4; CAB66143)"
FT /evidence="ECO:0000305"
FT CONFLICT 314
FT /note="N -> K (in Ref. 1; AAD38925, 2; AAF67635, 3;
FT AAG15379 and 4; CAB66143)"
FT /evidence="ECO:0000305"
FT CONFLICT 361
FT /note="E -> K (in Ref. 2; AAF67635 and 3; AAG15379)"
FT /evidence="ECO:0000305"
FT CONFLICT 388
FT /note="F -> S (in Ref. 1; AAD38925, 3; AAG15379 and 4;
FT CAB66143)"
FT /evidence="ECO:0000305"
FT STRAND 16..18
FT /evidence="ECO:0007829|PDB:1Q45"
FT STRAND 21..24
FT /evidence="ECO:0007829|PDB:1Q45"
FT STRAND 26..29
FT /evidence="ECO:0007829|PDB:1Q45"
FT HELIX 38..40
FT /evidence="ECO:0007829|PDB:1Q45"
FT HELIX 44..52
FT /evidence="ECO:0007829|PDB:1Q45"
FT STRAND 59..68
FT /evidence="ECO:0007829|PDB:1Q45"
FT HELIX 83..98
FT /evidence="ECO:0007829|PDB:1Q45"
FT STRAND 102..108
FT /evidence="ECO:0007829|PDB:1Q45"
FT HELIX 116..118
FT /evidence="ECO:0007829|PDB:1Q45"
FT HELIX 120..122
FT /evidence="ECO:0007829|PDB:1Q45"
FT STRAND 126..130
FT /evidence="ECO:0007829|PDB:1Q45"
FT TURN 135..137
FT /evidence="ECO:0007829|PDB:1Q45"
FT HELIX 158..160
FT /evidence="ECO:0007829|PDB:1Q45"
FT HELIX 161..178
FT /evidence="ECO:0007829|PDB:1Q45"
FT STRAND 181..187
FT /evidence="ECO:0007829|PDB:1Q45"
FT HELIX 192..197
FT /evidence="ECO:0007829|PDB:1Q45"
FT TURN 199..201
FT /evidence="ECO:0007829|PDB:1Q45"
FT STRAND 209..211
FT /evidence="ECO:0007829|PDB:1Q45"
FT HELIX 212..230
FT /evidence="ECO:0007829|PDB:1Q45"
FT HELIX 232..234
FT /evidence="ECO:0007829|PDB:1Q45"
FT STRAND 235..239
FT /evidence="ECO:0007829|PDB:1Q45"
FT HELIX 245..247
FT /evidence="ECO:0007829|PDB:1Q45"
FT HELIX 253..269
FT /evidence="ECO:0007829|PDB:1Q45"
FT STRAND 276..281
FT /evidence="ECO:0007829|PDB:1Q45"
FT HELIX 301..312
FT /evidence="ECO:0007829|PDB:1Q45"
FT STRAND 313..315
FT /evidence="ECO:0007829|PDB:2Q3O"
FT STRAND 317..322
FT /evidence="ECO:0007829|PDB:1Q45"
FT HELIX 325..333
FT /evidence="ECO:0007829|PDB:1Q45"
FT STRAND 338..343
FT /evidence="ECO:0007829|PDB:1Q45"
FT HELIX 344..348
FT /evidence="ECO:0007829|PDB:1Q45"
FT HELIX 352..357
FT /evidence="ECO:0007829|PDB:1Q45"
FT HELIX 367..369
FT /evidence="ECO:0007829|PDB:1Q45"
FT TURN 377..379
FT /evidence="ECO:0007829|PDB:1Q45"
SQ SEQUENCE 391 AA; 42691 MW; 5E1D9888324101D7 CRC64;
MTAAQGNSNE TLFSSYKMGR FDLSHRVVLA PMTRCRALNG VPNAALAEYY AQRTTPGGFL
ISEGTMVSPG SAGFPHVPGI YSDEQVEAWK QVVEAVHAKG GFIFCQLWHV GRASHAVYQP
NGGSPISSTN KPISENRWRV LLPDGSHVKY PKPRALEASE IPRVVEDYCL SALNAIRAGF
DGIEIHGAHG YLIDQFLKDG INDRTDQYGG SIANRCRFLK QVVEGVVSAI GASKVGVRVS
PAIDHLDATD SDPLSLGLAV VGMLNKLQGV NGSKLAYLHV TQPRYHAYGQ TESGRQGSDE
EEAKLMKSLR MAYNGTFMSS GGFNKELGMQ AVQQGDADLV SYGRLFIANP DLVSRFKIDG
ELNKYNRKTF YTQDPVVGYT DYPFLAPFSR L
