SDRA_ARATH
ID SDRA_ARATH Reviewed; 254 AA.
AC Q9S9W2;
DT 01-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Short-chain dehydrogenase/reductase SDRA {ECO:0000305};
DE EC=1.1.-.- {ECO:0000305};
DE AltName: Full=Protein INDOLE-3-BUTYRIC ACID RESPONSE 1 {ECO:0000303|PubMed:18725356};
DE AltName: Full=Short-chain dehydrogenase/reductase A {ECO:0000305};
GN Name=SDRA {ECO:0000303|PubMed:19043666};
GN Synonyms=IBR1 {ECO:0000303|PubMed:18725356};
GN OrderedLocusNames=At4g05530 {ECO:0000312|Araport:AT4G05530};
GN ORFNames=T1J24.9 {ECO:0000312|EMBL:AAD48959.1};
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=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
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 SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=17951448; DOI=10.1105/tpc.107.050989;
RA Reumann S., Babujee L., Ma C., Wienkoop S., Siemsen T., Antonicelli G.E.,
RA Rasche N., Lueder F., Weckwerth W., Jahn O.;
RT "Proteome analysis of Arabidopsis leaf peroxisomes reveals novel targeting
RT peptides, metabolic pathways, and defense mechanisms.";
RL Plant Cell 19:3170-3193(2007).
RN [5]
RP DISRUPTION PHENOTYPE, AND MUTAGENESIS OF ARG-43 AND SER-140.
RX PubMed=18725356; DOI=10.1534/genetics.108.090399;
RA Zolman B.K., Martinez N., Millius A., Adham A.R., Bartel B.;
RT "Identification and characterization of Arabidopsis indole-3-butyric acid
RT response mutants defective in novel peroxisomal enzymes.";
RL Genetics 180:237-251(2008).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=19043666; DOI=10.1007/s11103-008-9431-4;
RA Wiszniewski A.A., Zhou W., Smith S.M., Bussell J.D.;
RT "Identification of two Arabidopsis genes encoding a peroxisomal
RT oxidoreductase-like protein and an acyl-CoA synthetase-like protein that
RT are required for responses to pro-auxins.";
RL Plant Mol. Biol. 69:503-515(2009).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=20562230; DOI=10.1104/pp.110.157461;
RA Strader L.C., Culler A.H., Cohen J.D., Bartel B.;
RT "Conversion of endogenous indole-3-butyric acid to indole-3-acetic acid
RT drives cell expansion in Arabidopsis seedlings.";
RL Plant Physiol. 153:1577-1586(2010).
CC -!- FUNCTION: Involved with IBR3 and IBR10 in the peroxisomal beta-
CC oxidation of indole-3-butyric acid (IBA) to form indole-3-acetic acid
CC (IAA), a biologically active auxin. May be responsible for catalyzing
CC the dehydrogenation step in the conversion of IBA (PubMed:20562230).
CC May be involved in the peroxisomal activation of 2,4-
CC dichlorophenoxybutyric acid (2,4-DB), a precursor of active auxins that
CC inhibit root growth (PubMed:19043666). {ECO:0000269|PubMed:19043666,
CC ECO:0000269|PubMed:20562230}.
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:19043666,
CC ECO:0000305|PubMed:17951448}.
CC -!- DISRUPTION PHENOTYPE: Defective in root hair expansion
CC (PubMed:20562230). Mutant plants are resistant to the inhibitory effect
CC of intermediate levels of indole-3-butyric acid (IBA) and 2,4-DB on
CC root elongation (PubMed:18725356, PubMed:19043666).
CC {ECO:0000269|PubMed:18725356, ECO:0000269|PubMed:19043666,
CC ECO:0000269|PubMed:20562230}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
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DR EMBL; AF147263; AAD48959.1; -; Genomic_DNA.
DR EMBL; AL161503; CAB81095.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE82532.1; -; Genomic_DNA.
DR EMBL; AY035106; AAK59611.1; -; mRNA.
DR EMBL; AY113900; AAM44948.1; -; mRNA.
DR EMBL; AY087807; AAM65343.1; -; mRNA.
DR PIR; E85069; E85069.
DR RefSeq; NP_567300.1; NM_116791.3.
DR AlphaFoldDB; Q9S9W2; -.
DR SMR; Q9S9W2; -.
DR STRING; 3702.AT4G05530.1; -.
DR PaxDb; Q9S9W2; -.
DR PRIDE; Q9S9W2; -.
DR ProMEX; Q9S9W2; -.
DR ProteomicsDB; 234499; -.
DR EnsemblPlants; AT4G05530.1; AT4G05530.1; AT4G05530.
DR GeneID; 825905; -.
DR Gramene; AT4G05530.1; AT4G05530.1; AT4G05530.
DR KEGG; ath:AT4G05530; -.
DR Araport; AT4G05530; -.
DR TAIR; locus:2135467; AT4G05530.
DR eggNOG; KOG0725; Eukaryota.
DR HOGENOM; CLU_010194_1_1_1; -.
DR InParanoid; Q9S9W2; -.
DR OMA; ICPGIIE; -.
DR OrthoDB; 1194344at2759; -.
DR PhylomeDB; Q9S9W2; -.
DR BioCyc; ARA:AT4G05530-MON; -.
DR PRO; PR:Q9S9W2; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9S9W2; baseline and differential.
DR Genevisible; Q9S9W2; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005777; C:peroxisome; IDA:TAIR.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0006631; P:fatty acid metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0080024; P:indolebutyric acid metabolic process; IMP:TAIR.
DR GO; GO:0080026; P:response to indolebutyric acid; IMP:TAIR.
DR GO; GO:0048767; P:root hair elongation; IMP: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 Fatty acid metabolism; Lipid metabolism; Oxidoreductase; Peroxisome;
KW Reference proteome.
FT CHAIN 1..254
FT /note="Short-chain dehydrogenase/reductase SDRA"
FT /id="PRO_0000432487"
FT MOTIF 252..254
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000305"
FT ACT_SITE 159
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P50162,
FT ECO:0000255|PROSITE-ProRule:PRU10001"
FT BINDING 15..39
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P50162"
FT BINDING 146
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P50162"
FT MUTAGEN 43
FT /note="R->C: In ibr1-1; resistance to the inhibitory effect
FT of intermediate levels of indole-3-butyric acid (IBA) on
FT root elongation."
FT /evidence="ECO:0000269|PubMed:18725356"
FT MUTAGEN 140
FT /note="S->F: In ibr1-8; resistance to the inhibitory effect
FT of intermediate levels of indole-3-butyric acid (IBA) on
FT root elongation."
FT /evidence="ECO:0000269|PubMed:18725356"
SQ SEQUENCE 254 AA; 26765 MW; 54297E4D1D095372 CRC64;
MEKKLPRRLE GKVAIVTAST QGIGFGITER FGLEGASVVV SSRKQANVDE AVAKLKSKGI
DAYGIVCHVS NAQHRRNLVE KTVQKYGKID IVVCNAAANP STDPILSSKE AVLDKLWEIN
VKSSILLLQD MAPHLEKGSS VIFITSIAGF SPQGAMAMYG VTKTALLGLT KALAAEMAPD
TRVNAVAPGF VPTHFASFIT GSSEVREGIE EKTLLNRLGT TGDMAAAAAF LASDDSSYIT
GETLVVAGGM PSRL
