ADRC1_ARATH
ID ADRC1_ARATH Reviewed; 288 AA.
AC Q9FZ42; Q42157; Q42225; Q9C7L3;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=NADPH-dependent aldehyde reductase 1, chloroplastic {ECO:0000303|PubMed:21169366};
DE Short=AtChlADR1 {ECO:0000303|PubMed:21169366};
DE EC=1.1.1.- {ECO:0000269|PubMed:21169366};
DE AltName: Full=Glucose and ribitol dehydrogenase homolog 1;
DE Flags: Precursor;
GN Name=ChlADR1 {ECO:0000303|PubMed:21169366}; OrderedLocusNames=At1g54870;
GN ORFNames=F14C21_16, T24C10.1;
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] (ISOFORM 1).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 170-288 (ISOFORMS 1/2).
RC STRAIN=cv. Columbia; TISSUE=Dry seed;
RX PubMed=8580968; DOI=10.1046/j.1365-313x.1996.09010101.x;
RA Cooke R., Raynal M., Laudie M., Grellet F., Delseny M., Morris P.-C.,
RA Guerrier D., Giraudat J., Quigley F., Clabault G., Li Y.-F., Mache R.,
RA Krivitzky M., Gy I.J.-J., Kreis M., Lecharny A., Parmentier Y., Marbach J.,
RA Fleck J., Clement B., Philipps G., Herve C., Bardet C., Tremousaygue D.,
RA Lescure B., Lacomme C., Roby D., Jourjon M.-F., Chabrier P.,
RA Charpenteau J.-L., Desprez T., Amselem J., Chiapello H., Hoefte H.;
RT "Further progress towards a catalogue of all Arabidopsis genes: analysis of
RT a set of 5000 non-redundant ESTs.";
RL Plant J. 9:101-124(1996).
RN [5]
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). May act as a short alcohol-polyol-sugar
CC dehydrogenase possibly related to carbohydrate metabolism and the
CC acquisition of desiccation tolerance (By similarity). May also be
CC involved in signal transduction (By similarity). {ECO:0000250,
CC ECO:0000269|PubMed:21169366}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=10 mM for butyraldehyde {ECO:0000269|PubMed:21169366};
CC KM=0.09 mM for (E)-2-pentenal {ECO:0000269|PubMed:21169366};
CC KM=4.4 mM for (E)-2-hexenal {ECO:0000269|PubMed:21169366};
CC KM=70 mM for (E)-2-nonenal {ECO:0000269|PubMed:21169366};
CC KM=4.7 mM for methylglyoxal {ECO:0000269|PubMed:21169366};
CC Note=kcat is 4.3 sec(-1) for butyraldehyde. kcat is 1.7 sec(-1) for
CC (E)-2-pentenal. kcat is 1.1 sec(-1) for (E)-2-hexenal. kcat is 7.3
CC sec(-1) for (E)-2-nonenal. kcat is 2.4 sec(-1) for methylglyoxal.
CC {ECO:0000269|PubMed:21169366};
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:21169366}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=2;
CC Name=1;
CC IsoId=Q9FZ42-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9FZ42-2; Sequence=VSP_041301;
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
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DR EMBL; AC064840; AAG00870.1; -; Genomic_DNA.
DR EMBL; AC069144; AAG51119.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE33158.1; -; Genomic_DNA.
DR EMBL; AF372931; AAK50071.1; -; mRNA.
DR EMBL; AY124852; AAM70561.1; -; mRNA.
DR EMBL; Z27012; CAA81564.1; -; mRNA.
DR PIR; C96590; C96590.
DR RefSeq; NP_564670.2; NM_104360.3. [Q9FZ42-2]
DR AlphaFoldDB; Q9FZ42; -.
DR SMR; Q9FZ42; -.
DR BioGRID; 27151; 1.
DR STRING; 3702.AT1G54870.1; -.
DR PaxDb; Q9FZ42; -.
DR PeptideAtlas; Q9FZ42; -.
DR EnsemblPlants; AT1G54870.1; AT1G54870.1; AT1G54870. [Q9FZ42-2]
DR GeneID; 841926; -.
DR Gramene; AT1G54870.1; AT1G54870.1; AT1G54870. [Q9FZ42-2]
DR KEGG; ath:AT1G54870; -.
DR Araport; AT1G54870; -.
DR TAIR; locus:2011005; AT1G54870.
DR eggNOG; KOG0725; Eukaryota.
DR HOGENOM; CLU_010194_4_1_1; -.
DR InParanoid; Q9FZ42; -.
DR OMA; AAYQMSQ; -.
DR PhylomeDB; Q9FZ42; -.
DR BioCyc; ARA:AT1G54870-MON; -.
DR BioCyc; MetaCyc:AT1G54870-MON; -.
DR SABIO-RK; Q9FZ42; -.
DR PRO; PR:Q9FZ42; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9FZ42; baseline and differential.
DR Genevisible; Q9FZ42; AT.
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; IPR020904; Sc_DH/Rdtase_CS.
DR InterPro; IPR002347; SDR_fam.
DR PRINTS; PR00081; GDHRDH.
DR PRINTS; PR00080; SDRFAMILY.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS00061; ADH_SHORT; 1.
PE 1: Evidence at protein level;
KW Alternative initiation; Chloroplast; NADP; Oxidoreductase; Plastid;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..?
FT /note="Chloroplast"
FT /evidence="ECO:0000305|PubMed:21169366"
FT CHAIN ?..288
FT /note="NADPH-dependent aldehyde reductase 1, chloroplastic"
FT /id="PRO_0000239257"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 18..32
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 192
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT BINDING 47..71
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q12634"
FT BINDING 179
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q12634"
FT VAR_SEQ 1
FT /note="M -> MNVLCRVFTSSRVLSSNVTFSFSQIPNNTKKPLLEKRRLSPRVCLRA
FT M (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_041301"
FT CONFLICT 37..38
FT /note="Missing (in Ref. 1; AAG51119)"
FT /evidence="ECO:0000305"
FT CONFLICT 193
FT /note="T -> A (in Ref. 4; CAA81564)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 288 AA; 31387 MW; 0359C488117CE518 CRC64;
MASEKQKQHA QPGKEHVMES SPQFSSSDYQ PSNKLRGKVA LITGGDSGIG RAVGYCFASE
GATVAFTYVK GQEEKDAQET LQMLKEVKTS DSKEPIAIPT DLGFDENCKR VVDEVVNAFG
RIDVLINNAA EQYESSTIEE IDEPRLERVF RTNIFSYFFL TRHALKHMKE GSSIINTTSV
NAYKGNASLL DYTATKGAIV AFTRGLALQL AEKGIRVNGV APGPIWTPLI PASFNEEKIK
NFGSEVPMKR AGQPIEVAPS YVFLACNHCS SYFTGQVLHP NGGAVVNA
