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-NOV-2023, entry version 161. 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}. 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 AlphaFoldDB; Q9SQR2; -. DR SMR; Q9SQR2; -. DR IntAct; Q9SQR2; 1. DR STRING; 3702.AT3G04000.1; -. DR PaxDb; 3702-AT3G04000-1; -. 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; AT3G04000; -. DR eggNOG; KOG0725; Eukaryota. DR HOGENOM; CLU_010194_1_3_1; -. DR InParanoid; Q9SQR2; -. DR OMA; WINGQIV; -. DR OrthoDB; 5486946at2759; -. DR PhylomeDB; Q9SQR2; -. DR BioCyc; ARA:AT3G04000-MONOMER; -. DR BioCyc; MetaCyc:AT3G04000-MONOMER; -. 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 Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1. DR InterPro; IPR036291; NAD(P)-bd_dom_sf. DR InterPro; IPR002347; SDR_fam. DR PANTHER; PTHR48107:SF20; NADPH-DEPENDENT ALDEHYDE REDUCTASE 2, CHLOROPLASTIC; 1. DR PANTHER; PTHR48107; NADPH-DEPENDENT ALDEHYDE REDUCTASE-LIKE PROTEIN, CHLOROPLASTIC-RELATED; 1. DR Pfam; PF13561; adh_short_C2; 1. DR PRINTS; PR00081; GDHRDH. DR PRINTS; PR00080; SDRFAMILY. DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 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 //