ADRC2_ARATH
ID ADRC2_ARATH Reviewed; 272 AA.
AC Q9SQR2; Q94AT6;
DT 12-APR-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=NADPH-dependent aldehyde reductase 2, chloroplastic {ECO:0000303|PubMed:21169366};
DE Short=AtChlADR2 {ECO:0000303|PubMed:21169366};
DE EC=1.1.1.- {ECO:0000269|PubMed:21169366};
DE AltName: Full=Short-chain type dehydrogenase/reductase {ECO:0000312|EMBL:AAF05859.1};
DE Flags: Precursor;
GN Name=ChlADR2 {ECO:0000303|PubMed:21169366};
GN OrderedLocusNames=At3g04000 {ECO:0000312|Araport:AT3G04000};
GN ORFNames=T11I18.11 {ECO:0000312|EMBL:AAF05859.1};
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=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(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, SUBSTRATE SPECIFICITY, SUBCELLULAR LOCATION, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
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).
CC -!- FUNCTION: Aldehyde reductase that catalyzes the reduction of the
CC aldehyde carbonyl groups on saturated and alpha,beta-unsaturated
CC aldehydes with more than 5 carbons (PubMed:21169366). No activity on
CC alpha,beta-unsaturated ketones (PubMed:21169366). Can use
CC propionaldehyde, butyraldehyde, methylglyoxal, (e)-2-pentenal, (E)-2-
CC hexenal, (Z)-3-hexenal and (E)-2-nonenal as substrates, but not
CC propenal (acrolein), crotonaldehyde, 2-butanone, 3-buten-2-one or 1-
CC penten-3-one (PubMed:21169366). {ECO:0000269|PubMed:21169366}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=7.8 mM for butyraldehyde {ECO:0000269|PubMed:21169366};
CC KM=0.6 mM for (E)-2-pentenal {ECO:0000269|PubMed:21169366};
CC KM=2.5 mM for (E)-2-hexenal {ECO:0000269|PubMed:21169366};
CC KM=5.0 mM for methylglyoxal {ECO:0000269|PubMed:21169366};
CC Note=kcat is 29.6 sec(-1) for butyraldehyde. kcat is 6.4 sec(-1) for
CC (E)-2-pentenal. kcat is 1.8 sec(-1) for (E)-2-hexenal. kcat is 28.8
CC sec(-1) for methylglyoxal. {ECO:0000269|PubMed:21169366};
CC -!- INTERACTION:
CC Q9SQR2; Q9SVQ9: At4g13180; NbExp=3; IntAct=EBI-4471202, EBI-4471207;
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:21169366}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
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DR EMBL; AC011698; AAF05859.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE74024.1; -; Genomic_DNA.
DR EMBL; BT002321; AAN86154.1; -; mRNA.
DR EMBL; AY045807; AAK76481.2; -; mRNA.
DR RefSeq; NP_566221.2; NM_111271.3.
DR AlphaFoldDB; Q9SQR2; -.
DR SMR; Q9SQR2; -.
DR IntAct; Q9SQR2; 1.
DR STRING; 3702.AT3G04000.1; -.
DR PaxDb; Q9SQR2; -.
DR PRIDE; Q9SQR2; -.
DR ProteomicsDB; 244728; -.
DR EnsemblPlants; AT3G04000.1; AT3G04000.1; AT3G04000.
DR GeneID; 819555; -.
DR Gramene; AT3G04000.1; AT3G04000.1; AT3G04000.
DR KEGG; ath:AT3G04000; -.
DR Araport; AT3G04000; -.
DR TAIR; locus:2095918; AT3G04000.
DR eggNOG; KOG0725; Eukaryota.
DR HOGENOM; CLU_010194_1_3_1; -.
DR InParanoid; Q9SQR2; -.
DR OMA; WTLHRGN; -.
DR OrthoDB; 913128at2759; -.
DR PhylomeDB; Q9SQR2; -.
DR BioCyc; ARA:AT3G04000-MON; -.
DR BioCyc; MetaCyc:AT3G04000-MON; -.
DR SABIO-RK; Q9SQR2; -.
DR PRO; PR:Q9SQR2; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9SQR2; baseline and differential.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0008106; F:alcohol dehydrogenase (NADP+) activity; IDA:TAIR.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR002347; SDR_fam.
DR PRINTS; PR00081; GDHRDH.
DR PRINTS; PR00080; SDRFAMILY.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 1: Evidence at protein level;
KW Chloroplast; NADP; Oxidoreductase; Plastid; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..53
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 54..272
FT /note="NADPH-dependent aldehyde reductase 2, chloroplastic"
FT /evidence="ECO:0000255"
FT /id="PRO_0000439504"
FT ACT_SITE 179
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q12634"
FT BINDING 26..50
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q12634"
FT BINDING 165
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q12634"
SQ SEQUENCE 272 AA; 28435 MW; 1F0542EE7C599276 CRC64;
MAAASSVSSP PLCLAGRVAI VTGSSRGIGR AIAIHLAELG ARVVVNYSTS PVEAEKVATA
ITTNCSKDAE VAGKSPRVIV VKADISEPSQ VKSLFDEAER VFESPVHILV NSAAIADPNH
STISDMSVEL FDRIISVNTR GAFICAREAA NRLKRGGGGR IILLSTSLVQ TLNTNYGSYT
ASKAAVEAMA KILAKELKGT EITVNCVSPG PVATEMFYTG LSNEIVEKVK SQNLFGRIGE
TKDIAPVVGF LASDAGEWIN GQVIMANGGC LL
