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NADPH-dependent alkenal/one oxidoreductase, chloroplastic (AtAOR) (EC 1.3.1.-)

 AOR_ARATH               Reviewed;         386 AA.
Q9ZUC1; Q945P3;
11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
09-NOV-2004, sequence version 2.
25-APR-2018, entry version 131.
RecName: Full=NADPH-dependent alkenal/one oxidoreductase, chloroplastic {ECO:0000303|PubMed:21169366};
Short=AtAOR {ECO:0000303|PubMed:21169366};
EC=1.3.1.- {ECO:0000269|PubMed:21169366};
Flags: Precursor;
Name=AOR {ECO:0000303|PubMed:21169366};
OrderedLocusNames=At1g23740 {ECO:0000312|Araport:AT1G23740};
ORFNames=F5O8.29 {ECO:0000312|EMBL:AAC98029.1};
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=11130712; DOI=10.1038/35048500;
Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S.,
White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y.,
Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W.,
Chung M.K., Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K.,
Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y.,
Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L.,
Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E.,
Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B.,
Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P.,
Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A.,
Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I.,
Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D.,
Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M.,
Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M.,
Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.;
"Sequence and analysis of chromosome 1 of the plant Arabidopsis
thaliana.";
Nature 408:816-820(2000).
[2]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
PubMed=27862469; DOI=10.1111/tpj.13415;
Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
Town C.D.;
"Araport11: a complete reannotation of the Arabidopsis thaliana
reference genome.";
Plant J. 89:789-804(2017).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[4]
FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
SUBSTRATE SPECIFICITY.
PubMed=21169366; DOI=10.1074/jbc.M110.202226;
Yamauchi Y., Hasegawa A., Taninaka A., Mizutani M., Sugimoto Y.;
"NADPH-dependent reductases involved in the detoxification of reactive
carbonyls in plants.";
J. Biol. Chem. 286:6999-7009(2011).
[5]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=22575657; DOI=10.1016/j.febslet.2012.03.013;
Yamauchi Y., Hasegawa A., Mizutani M., Sugimoto Y.;
"Chloroplastic NADPH-dependent alkenal/one oxidoreductase contributes
to the detoxification of reactive carbonyls produced under oxidative
stress.";
FEBS Lett. 586:1208-1213(2012).
-!- FUNCTION: Reduces the double bond in short-chain unsaturated
carbonyls (PubMed:21169366). Acts preferentially on alpha,beta-
unsaturated ketones rather on alpha,beta-undaturated aldehydes
(PubMed:21169366). Has no activity with (E)-2-hexenal and (E)-2-
pentenal (PubMed:21169366). Contributes to detoxify stromal
reactive carbonyls produced under oxidative stress
(PubMed:22575657). {ECO:0000269|PubMed:21169366,
ECO:0000269|PubMed:22575657}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=3.5 mM for propenal {ECO:0000269|PubMed:21169366};
KM=1.8 mM for butenal {ECO:0000269|PubMed:21169366};
KM=0.13 mM for 3-buten-2-one {ECO:0000269|PubMed:21169366};
KM=0.29 mM for 1-penten-3-one {ECO:0000269|PubMed:21169366};
KM=0.12 mM for 4-hexen-3-one {ECO:0000269|PubMed:21169366};
KM=0.01 mM for NADPH with propenal as substrate
{ECO:0000269|PubMed:21169366};
KM=0.053 mM for NADH with propenal as substrate
{ECO:0000269|PubMed:21169366};
Note=kcat is 22 sec(-1) for propenal. kcat is 1.3 sec(-1) for
butenal. kcat is 3.5 sec(-1) for 3-buten-2-one. kcat is 4.0
sec(-1) for 1-penten-3-one. kcat is 3.3 sec(-1) for 4-hexen-3-
one. kcat is 23 sec(-1) for NADPH. kcat is 23 sec(-1) for NADH.
{ECO:0000269|PubMed:21169366};
pH dependence:
Optimum pH is 6.0-6.5. {ECO:0000303|PubMed:21169366};
-!- SUBCELLULAR LOCATION: Plastid, chloroplast
{ECO:0000305|PubMed:21169366}.
-!- DISRUPTION PHENOTYPE: No visible phenotype under normal
conditions, but enhanced susceptibility to methyl viologen.
{ECO:0000269|PubMed:22575657}.
-!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
family. Quinone oxidoreductase subfamily. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAC98029.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AC005990; AAC98029.1; ALT_INIT; Genomic_DNA.
EMBL; CP002684; AEE30427.1; -; Genomic_DNA.
EMBL; AF411799; AAL06488.1; -; mRNA.
EMBL; AY094032; AAM16188.1; -; mRNA.
PIR; E86371; E86371.
RefSeq; NP_173786.1; NM_102222.5.
UniGene; At.22964; -.
UniGene; At.71159; -.
ProteinModelPortal; Q9ZUC1; -.
SMR; Q9ZUC1; -.
STRING; 3702.AT1G23740.1; -.
iPTMnet; Q9ZUC1; -.
SWISS-2DPAGE; Q9ZUC1; -.
PaxDb; Q9ZUC1; -.
PRIDE; Q9ZUC1; -.
EnsemblPlants; AT1G23740.1; AT1G23740.1; AT1G23740.
GeneID; 838984; -.
Gramene; AT1G23740.1; AT1G23740.1; AT1G23740.
KEGG; ath:AT1G23740; -.
Araport; AT1G23740; -.
TAIR; locus:2034802; AT1G23740.
eggNOG; KOG1198; Eukaryota.
eggNOG; COG0604; LUCA.
HOGENOM; HOG000294678; -.
InParanoid; Q9ZUC1; -.
KO; K18980; -.
OMA; TSWQALK; -.
OrthoDB; EOG09360IBI; -.
PhylomeDB; Q9ZUC1; -.
BioCyc; ARA:AT1G23740-MONOMER; -.
BioCyc; MetaCyc:AT1G23740-MONOMER; -.
PRO; PR:Q9ZUC1; -.
Proteomes; UP000006548; Chromosome 1.
ExpressionAtlas; Q9ZUC1; baseline and differential.
Genevisible; Q9ZUC1; AT.
GO; GO:0048046; C:apoplast; IDA:TAIR.
GO; GO:0009507; C:chloroplast; IDA:TAIR.
GO; GO:0009941; C:chloroplast envelope; IDA:TAIR.
GO; GO:0009570; C:chloroplast stroma; IDA:TAIR.
GO; GO:0010319; C:stromule; IDA:TAIR.
GO; GO:0009579; C:thylakoid; IDA:TAIR.
GO; GO:0035798; F:2-alkenal reductase (NADP+) activity; IDA:TAIR.
GO; GO:0035671; F:enone reductase activity; IDA:TAIR.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0055114; P:oxidation-reduction process; IDA:TAIR.
GO; GO:0009409; P:response to cold; IEP:TAIR.
InterPro; IPR013154; ADH_N.
InterPro; IPR011032; GroES-like_sf.
InterPro; IPR036291; NAD(P)-bd_dom_sf.
InterPro; IPR020843; PKS_ER.
InterPro; IPR002364; Quin_OxRdtase/zeta-crystal_CS.
Pfam; PF08240; ADH_N; 1.
SMART; SM00829; PKS_ER; 1.
SUPFAM; SSF50129; SSF50129; 1.
SUPFAM; SSF51735; SSF51735; 1.
PROSITE; PS01162; QOR_ZETA_CRYSTAL; 1.
1: Evidence at protein level;
Chloroplast; Complete proteome; NAD; Oxidoreductase; Plastid;
Reference proteome; Transit peptide.
TRANSIT 1 ? Chloroplast. {ECO:0000255}.
CHAIN ? 386 NADPH-dependent alkenal/one
oxidoreductase, chloroplastic.
/FTId=PRO_0000000886.
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


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