AOR_ARATH
ID AOR_ARATH Reviewed; 386 AA.
AC Q9ZUC1; Q945P3;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 09-NOV-2004, sequence version 2.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=NADPH-dependent alkenal/one oxidoreductase, chloroplastic {ECO:0000303|PubMed:21169366};
DE Short=AtAOR {ECO:0000303|PubMed:21169366};
DE EC=1.3.1.- {ECO:0000269|PubMed:21169366};
DE Flags: Precursor;
GN Name=AOR {ECO:0000303|PubMed:21169366};
GN OrderedLocusNames=At1g23740 {ECO:0000312|Araport:AT1G23740};
GN ORFNames=F5O8.29 {ECO:0000312|EMBL:AAC98029.1};
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=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=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 FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBSTRATE
RP SPECIFICITY.
RX PubMed=21169366; DOI=10.1074/jbc.m110.202226;
RA Yamauchi Y., Hasegawa A., Taninaka A., Mizutani M., Sugimoto Y.;
RT "NADPH-dependent reductases involved in the detoxification of reactive
RT carbonyls in plants.";
RL J. Biol. Chem. 286:6999-7009(2011).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=22575657; DOI=10.1016/j.febslet.2012.03.013;
RA Yamauchi Y., Hasegawa A., Mizutani M., Sugimoto Y.;
RT "Chloroplastic NADPH-dependent alkenal/one oxidoreductase contributes to
RT the detoxification of reactive carbonyls produced under oxidative stress.";
RL FEBS Lett. 586:1208-1213(2012).
CC -!- FUNCTION: Reduces the double bond in short-chain unsaturated carbonyls
CC (PubMed:21169366). Acts preferentially on alpha,beta-unsaturated
CC ketones rather on alpha,beta-unsaturated aldehydes (PubMed:21169366).
CC Has no activity with (E)-2-hexenal and (E)-2-pentenal
CC (PubMed:21169366). Contributes to detoxify stromal reactive carbonyls
CC produced under oxidative stress (PubMed:22575657).
CC {ECO:0000269|PubMed:21169366, ECO:0000269|PubMed:22575657}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=3.5 mM for propenal {ECO:0000269|PubMed:21169366};
CC KM=1.8 mM for butenal {ECO:0000269|PubMed:21169366};
CC KM=0.13 mM for 3-buten-2-one {ECO:0000269|PubMed:21169366};
CC KM=0.29 mM for 1-penten-3-one {ECO:0000269|PubMed:21169366};
CC KM=0.12 mM for 4-hexen-3-one {ECO:0000269|PubMed:21169366};
CC KM=0.01 mM for NADPH with propenal as substrate
CC {ECO:0000269|PubMed:21169366};
CC KM=0.053 mM for NADH with propenal as substrate
CC {ECO:0000269|PubMed:21169366};
CC Note=kcat is 22 sec(-1) for propenal. kcat is 1.3 sec(-1) for
CC butenal. kcat is 3.5 sec(-1) for 3-buten-2-one. kcat is 4.0 sec(-1)
CC for 1-penten-3-one. kcat is 3.3 sec(-1) for 4-hexen-3-one. kcat is 23
CC sec(-1) for NADPH. kcat is 23 sec(-1) for NADH.
CC {ECO:0000269|PubMed:21169366};
CC pH dependence:
CC Optimum pH is 6.0-6.5. {ECO:0000303|PubMed:21169366};
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000305|PubMed:21169366}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal conditions, but
CC enhanced susceptibility to methyl viologen.
CC {ECO:0000269|PubMed:22575657}.
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. Quinone oxidoreductase subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC98029.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC005990; AAC98029.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002684; AEE30427.1; -; Genomic_DNA.
DR EMBL; AF411799; AAL06488.1; -; mRNA.
DR EMBL; AY094032; AAM16188.1; -; mRNA.
DR PIR; E86371; E86371.
DR RefSeq; NP_173786.1; NM_102222.5.
DR AlphaFoldDB; Q9ZUC1; -.
DR SMR; Q9ZUC1; -.
DR STRING; 3702.AT1G23740.1; -.
DR iPTMnet; Q9ZUC1; -.
DR SWISS-2DPAGE; Q9ZUC1; -.
DR PaxDb; Q9ZUC1; -.
DR PRIDE; Q9ZUC1; -.
DR ProteomicsDB; 244974; -.
DR EnsemblPlants; AT1G23740.1; AT1G23740.1; AT1G23740.
DR GeneID; 838984; -.
DR Gramene; AT1G23740.1; AT1G23740.1; AT1G23740.
DR KEGG; ath:AT1G23740; -.
DR Araport; AT1G23740; -.
DR TAIR; locus:2034802; AT1G23740.
DR eggNOG; KOG1198; Eukaryota.
DR HOGENOM; CLU_026673_3_3_1; -.
DR InParanoid; Q9ZUC1; -.
DR OMA; TSWQALK; -.
DR OrthoDB; 727365at2759; -.
DR PhylomeDB; Q9ZUC1; -.
DR BioCyc; ARA:AT1G23740-MON; -.
DR BioCyc; MetaCyc:AT1G23740-MON; -.
DR BRENDA; 1.3.1.102; 399.
DR SABIO-RK; Q9ZUC1; -.
DR PRO; PR:Q9ZUC1; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9ZUC1; baseline and differential.
DR Genevisible; Q9ZUC1; AT.
DR GO; GO:0048046; C:apoplast; HDA:TAIR.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
DR GO; GO:0010319; C:stromule; IDA:TAIR.
DR GO; GO:0009579; C:thylakoid; HDA:TAIR.
DR GO; GO:0035798; F:2-alkenal reductase (NADP+) activity; IDA:TAIR.
DR GO; GO:0035671; F:enone reductase activity; IDA:TAIR.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0009409; P:response to cold; IEP:TAIR.
DR InterPro; IPR013154; ADH_N.
DR InterPro; IPR044626; AOR-like.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020843; PKS_ER.
DR InterPro; IPR002364; Quin_OxRdtase/zeta-crystal_CS.
DR PANTHER; PTHR44573; PTHR44573; 1.
DR Pfam; PF08240; ADH_N; 1.
DR SMART; SM00829; PKS_ER; 1.
DR SUPFAM; SSF50129; SSF50129; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS01162; QOR_ZETA_CRYSTAL; 1.
PE 1: Evidence at protein level;
KW Chloroplast; NAD; Oxidoreductase; Plastid; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..?
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN ?..386
FT /note="NADPH-dependent alkenal/one oxidoreductase,
FT chloroplastic"
FT /id="PRO_0000000886"
SQ SEQUENCE 386 AA; 40986 MW; 4DDD19133C9D5D84 CRC64;
MNAALATTTA TTPVLRRETP LLHYCSLTTK SPVYQINRVR FGSCVQTVSK KFLKISASSQ
SASAAVNVTA DASIPKEMKA WVYSDYGGVD VLKLESNIVV PEIKEDQVLI KVVAAALNPV
DAKRRQGKFK ATDSPLPTVP GYDVAGVVVK VGSAVKDLKE GDEVYANVSE KALEGPKQFG
SLAEYTAVEE KLLALKPKNI DFAQAAGLPL AIETADEGLV RTEFSAGKSI LVLNGAGGVG
SLVIQLAKHV YGASKVAATA STEKLELVRS LGADLAIDYT KENIEDLPDK YDVVFDAIGM
CDKAVKVIKE GGKVVALTGA VTPPGFRFVV TSNGDVLKKL NPYIESGKVK PVVDPKGPFP
FSRVADAFSY LETNHATGKV VVYPIP
