ID   OPRL1_ARATH             Reviewed;         324 AA.
AC   Q8GYA3; A0ME63; O80523;
DT   26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2005, sequence version 2.
DT   03-AUG-2022, entry version 119.
DE   RecName: Full=Putative 12-oxophytodienoate reductase-like protein 1;
DE            EC=1.3.1.-;
GN   OrderedLocusNames=At1g09400; ORFNames=F14J9.6;
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=11130712; DOI=10.1038/35048500;
RA   Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA   Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA   Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA   Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA   Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA   Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA   Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA   Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA   Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA   Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA   Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA   Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA   Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA   Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA   Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL   Nature 408:816-820(2000).
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=17147637; DOI=10.1111/j.1467-7652.2006.00183.x;
RA   Underwood B.A., Vanderhaeghen R., Whitford R., Town C.D., Hilson P.;
RT   "Simultaneous high-throughput recombinational cloning of open reading
RT   frames in closed and open configurations.";
RL   Plant Biotechnol. J. 4:317-324(2006).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 106-324.
RX   PubMed=11910074; DOI=10.1126/science.1071006;
RA   Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA   Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA   Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA   Shinagawa A., Shinozaki K.;
RT   "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL   Science 296:141-145(2002).
CC   -!- FUNCTION: Putative oxophytodienoate reductase that may be involved in
CC       the biosynthesis or metabolism of oxylipin signaling molecules.
CC       {ECO:0000250}.
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000250};
CC   -!- SIMILARITY: Belongs to the NADH:flavin oxidoreductase/NADH oxidase
CC       family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABK28390.1; Type=Erroneous termination; Note=Extended C-terminus.; Evidence={ECO:0000305};
CC       Sequence=BAC42416.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AC003970; AAC33200.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE28437.1; -; Genomic_DNA.
DR   EMBL; DQ652831; ABK28390.1; ALT_SEQ; mRNA.
DR   EMBL; AK117769; BAC42416.1; ALT_INIT; mRNA.
DR   PIR; C86227; C86227.
DR   RefSeq; NP_172411.1; NM_100810.2.
DR   AlphaFoldDB; Q8GYA3; -.
DR   SMR; Q8GYA3; -.
DR   BioGRID; 22703; 1.
DR   STRING; 3702.AT1G09400.1; -.
DR   PaxDb; Q8GYA3; -.
DR   PRIDE; Q8GYA3; -.
DR   ProteomicsDB; 249373; -.
DR   EnsemblPlants; AT1G09400.1; AT1G09400.1; AT1G09400.
DR   GeneID; 837462; -.
DR   Gramene; AT1G09400.1; AT1G09400.1; AT1G09400.
DR   KEGG; ath:AT1G09400; -.
DR   Araport; AT1G09400; -.
DR   TAIR; locus:2012285; AT1G09400.
DR   eggNOG; KOG0134; Eukaryota.
DR   HOGENOM; CLU_012153_0_2_1; -.
DR   InParanoid; Q8GYA3; -.
DR   OMA; WHVGRFS; -.
DR   OrthoDB; 978998at2759; -.
DR   PhylomeDB; Q8GYA3; -.
DR   BioCyc; ARA:AT1G09400-MON; -.
DR   PRO; PR:Q8GYA3; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q8GYA3; baseline and differential.
DR   Genevisible; Q8GYA3; AT.
DR   GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
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   2: Evidence at transcript level;
KW   Acetylation; Flavoprotein; FMN; NADP; Oxidoreductase; Reference proteome.
FT   CHAIN           1..324
FT                   /note="Putative 12-oxophytodienoate reductase-like protein
FT                   1"
FT                   /id="PRO_0000194486"
FT   REGION          99..128
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        100..118
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        165
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         14..16
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250"
FT   BINDING         47
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250"
FT   BINDING         89
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250"
FT   BINDING         160..163
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         212
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250"
FT   BINDING         252
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         282
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250"
FT   BINDING         303..304
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8GYB8"
SQ   SEQUENCE   324 AA;  36413 MW;  E4F9F3D6F9C00A9B CRC64;
     MKNFNLTHRI VMAPMARMRS YGNIPQPHVA LYYCQRTTPG GLLISEATGV SETAMAYQNM
     PGIWRKEQIE AWKPIVDAVH SHGGIFFCQL WHAGRVSHQD CQPNGESPVS STDKPFADDP
     SNEFTPPRRL RTDEIPTIIN DFRLAARNAT EAGFDGVEIH GAHGYLIDQF MKDSVNDRTD
     SYGGSLENRC RFALQVIEAV SKEIGPDRVG IRLSPFADYM ESGDTDPKRL GLYMAKSLNR
     FEILYCHMIE PRMKTVSEIF ECRESLTPMR NAFNGTFIVA GGYTREDGNK AVAEGRTDLV
     AYGRLFLANP DLPKRFELNA PLNK