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 08-MAY-2019, entry version 141. 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; Magnoliophyta; eudicotyledons; Gunneridae; OC Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae; OC 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., RA Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B., RA Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P., RA De Simone V., Choisne N., Artiguenave F., Robert C., Brottier P., RA Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F., RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V., RA Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S., RA Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G., RA Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B., RA Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G., RA Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J., RA Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D., RA 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., RA Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., RA Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., RA Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P., RA Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S., RA Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V., RA Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C., RA Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E., RA Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y., RA Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A., RA 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 RT 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 RT reference 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., RA Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., RA Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G., RA Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., RA Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., RA Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., RA Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., RA Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., RA Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., RA Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., RA Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., RA Yuan S., Shinozaki K., Davis R.W., Theologis A., 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 CC on alpha,beta-unsaturated ketones (PubMed:21169366). Can use CC propionaldehyde, butyraldehyde, methylglyoxal, (e)-2-pentenal, CC (E)-2-hexenal, (Z)-3-hexenal and (E)-2-nonenal as substrates, but CC not propenal (acrolein), crotonaldehyde, 2-butanone, 3-buten-2-one CC or 1-penten-3-one (PubMed:21169366). CC {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) CC for (E)-2-pentenal. kcat is 1.8 sec(-1) for (E)-2-hexenal. kcat CC is 28.8 sec(-1) for methylglyoxal. CC {ECO:0000269|PubMed:21169366}; CC -!- INTERACTION: CC 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 CC (SDR) family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 SMR; Q9SQR2; -. DR IntAct; Q9SQR2; 1. DR STRING; 3702.AT3G04000.1; -. DR PaxDb; Q9SQR2; -. DR PRIDE; Q9SQR2; -. 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 eggNOG; COG1028; LUCA. DR InParanoid; Q9SQR2; -. DR KO; K00059; -. DR OMA; CHYVVAD; -. DR OrthoDB; 913128at2759; -. DR PhylomeDB; Q9SQR2; -. DR BioCyc; ARA:AT3G04000-MONOMER; -. DR BioCyc; MetaCyc:AT3G04000-MONOMER; -. 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 GO; GO:0055114; P:oxidation-reduction process; 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; Complete proteome; NADP; Oxidoreductase; Plastid; KW Reference proteome; Transit peptide. FT TRANSIT 1 53 Chloroplast. {ECO:0000255}. FT CHAIN 54 272 NADPH-dependent aldehyde reductase 2, FT chloroplastic. {ECO:0000255}. FT /FTId=PRO_0000439504. FT NP_BIND 26 50 NADP. {ECO:0000250|UniProtKB:Q12634}. FT ACT_SITE 179 179 Proton acceptor. FT {ECO:0000250|UniProtKB:Q12634}. FT BINDING 165 165 Substrate. FT {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 //