ADRC3_ARATH
ID ADRC3_ARATH Reviewed; 270 AA.
AC Q9SQR4;
DT 12-APR-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=NADPH-dependent aldehyde reductase-like protein, chloroplastic {ECO:0000250|UniProtKB:Q9SQR2};
DE EC=1.1.1.- {ECO:0000250|UniProtKB:Q9SQR2};
DE Flags: Precursor;
GN OrderedLocusNames=At3g03980 {ECO:0000312|Araport:AT3G03980};
GN ORFNames=T11I18.9 {ECO:0000312|EMBL:AAF05857.1};
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).
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. {ECO:0000250|UniProtKB:Q9SQR2}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000250|UniProtKB:Q9SQR2}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
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DR EMBL; AC011698; AAF05857.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE74022.1; -; Genomic_DNA.
DR RefSeq; NP_187048.1; NM_111269.2.
DR AlphaFoldDB; Q9SQR4; -.
DR SMR; Q9SQR4; -.
DR STRING; 3702.AT3G03980.1; -.
DR PaxDb; Q9SQR4; -.
DR PRIDE; Q9SQR4; -.
DR ProteomicsDB; 244907; -.
DR EnsemblPlants; AT3G03980.1; AT3G03980.1; AT3G03980.
DR GeneID; 819553; -.
DR Gramene; AT3G03980.1; AT3G03980.1; AT3G03980.
DR KEGG; ath:AT3G03980; -.
DR Araport; AT3G03980; -.
DR TAIR; locus:2095968; AT3G03980.
DR eggNOG; KOG0725; Eukaryota.
DR HOGENOM; CLU_010194_1_3_1; -.
DR InParanoid; Q9SQR4; -.
DR OMA; GICEFKE; -.
DR OrthoDB; 913128at2759; -.
DR PhylomeDB; Q9SQR4; -.
DR BioCyc; ARA:AT3G03980-MON; -.
DR PRO; PR:Q9SQR4; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9SQR4; baseline and differential.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
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 3: Inferred from homology;
KW Chloroplast; NADP; Oxidoreductase; Plastid; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..53
FT /note="Chloroplast"
FT /evidence="ECO:0000250|UniProtKB:Q9SQR2"
FT CHAIN 54..270
FT /note="NADPH-dependent aldehyde reductase-like protein,
FT chloroplastic"
FT /id="PRO_0000439505"
FT ACT_SITE 178
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 270 AA; 28146 MW; 0A76087F023A7635 CRC64;
MSTHSSISQP PLPLAGRVAI VTGSSRGIGR AIAIHLAELG ARIVINYTSK AADAERVASE
INDFPVREEI TGKGPRAIVV QANVSEPSQV KSMFDAAESA FEAPVHILVN SAGILDPKYP
TIADTSVEDF DHTFSVNTKG AFLCSKEAAN RLKQGGGGRI ILLTSSQTRS LKPGFGAYAA
SKAAVETMVK ILAKELKGTG ITANCVAPGP IATEMFFDGK TPELVEKIAA ESPFGRVGEA
KDVVPLVGFL AGDGGEWVNG QIIPVNGGYV
