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Short-chain dehydrogenase/reductase SDRA (EC 1.1.-.-) (Protein INDOLE-3-BUTYRIC ACID RESPONSE 1) (Short-chain dehydrogenase/reductase A)

 SDRA_ARATH              Reviewed;         254 AA.
Q9S9W2;
01-APR-2015, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
23-MAY-2018, entry version 129.
RecName: Full=Short-chain dehydrogenase/reductase SDRA {ECO:0000305};
EC=1.1.-.- {ECO:0000305};
AltName: Full=Protein INDOLE-3-BUTYRIC ACID RESPONSE 1 {ECO:0000303|PubMed:18725356};
AltName: Full=Short-chain dehydrogenase/reductase A {ECO:0000305};
Name=SDRA {ECO:0000303|PubMed:19043666};
Synonyms=IBR1 {ECO:0000303|PubMed:18725356};
OrderedLocusNames=At4g05530 {ECO:0000312|Araport:AT4G05530};
ORFNames=T1J24.9 {ECO:0000312|EMBL:AAD48959.1};
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=10617198; DOI=10.1038/47134;
Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G.,
Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N.,
Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M.,
Weichselgartner M., de Simone V., Obermaier B., Mache R., Mueller M.,
Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T.,
Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I.,
Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P.,
Langham S.-A., McCullagh B., Bilham L., Robben J.,
van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F.,
Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E.,
Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W.,
Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P.,
Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H.,
De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R.,
van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S.,
Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R.,
Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S.,
Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H.,
Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S.,
Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A.,
Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R.,
Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S.,
Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E.,
Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A.,
Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T.,
Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C.,
Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S.,
Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K.,
Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L.,
Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J.,
Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J.,
Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D.,
Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D.,
Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C.,
Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C.,
Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R.,
Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S.,
Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A.,
Chen E., Marra M.A., Martienssen R., McCombie W.R.;
"Sequence and analysis of chromosome 4 of the plant Arabidopsis
thaliana.";
Nature 402:769-777(1999).
[2]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
PubMed=27862469; DOI=10.1111/tpj.13415;
Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
Town C.D.;
"Araport11: a complete reannotation of the Arabidopsis thaliana
reference genome.";
Plant J. 89:789-804(2017).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[4]
SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=17951448; DOI=10.1105/tpc.107.050989;
Reumann S., Babujee L., Ma C., Wienkoop S., Siemsen T.,
Antonicelli G.E., Rasche N., Lueder F., Weckwerth W., Jahn O.;
"Proteome analysis of Arabidopsis leaf peroxisomes reveals novel
targeting peptides, metabolic pathways, and defense mechanisms.";
Plant Cell 19:3170-3193(2007).
[5]
DISRUPTION PHENOTYPE, AND MUTAGENESIS OF ARG-43 AND SER-140.
PubMed=18725356; DOI=10.1534/genetics.108.090399;
Zolman B.K., Martinez N., Millius A., Adham A.R., Bartel B.;
"Identification and characterization of Arabidopsis indole-3-butyric
acid response mutants defective in novel peroxisomal enzymes.";
Genetics 180:237-251(2008).
[6]
FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
PubMed=19043666; DOI=10.1007/s11103-008-9431-4;
Wiszniewski A.A., Zhou W., Smith S.M., Bussell J.D.;
"Identification of two Arabidopsis genes encoding a peroxisomal
oxidoreductase-like protein and an acyl-CoA synthetase-like protein
that are required for responses to pro-auxins.";
Plant Mol. Biol. 69:503-515(2009).
[7]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=20562230; DOI=10.1104/pp.110.157461;
Strader L.C., Culler A.H., Cohen J.D., Bartel B.;
"Conversion of endogenous indole-3-butyric acid to indole-3-acetic
acid drives cell expansion in Arabidopsis seedlings.";
Plant Physiol. 153:1577-1586(2010).
-!- FUNCTION: Involved with IBR3 and IBR10 in the peroxisomal beta-
oxidation of indole-3-butyric acid (IBA) to form indole-3-acetic
acid (IAA), a biologically active auxin. May be responsible for
catalyzing the dehydrogenation step in the conversion of IBA
(PubMed:20562230). May be involved in the peroxisomal activation
of 2,4-dichlorophenoxybutyric acid (2,4-DB), a precursor of active
auxins that inhibit root growth (PubMed:19043666).
{ECO:0000269|PubMed:19043666, ECO:0000269|PubMed:20562230}.
-!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:19043666,
ECO:0000305|PubMed:17951448}.
-!- DISRUPTION PHENOTYPE: Defective in root hair expansion
(PubMed:20562230). Mutant plants are resistant to the inhibitory
effect of intermediate levels of indole-3-butyric acid (IBA) and
2,4-DB on root elongation (PubMed:18725356, PubMed:19043666).
{ECO:0000269|PubMed:18725356, ECO:0000269|PubMed:19043666,
ECO:0000269|PubMed:20562230}.
-!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases
(SDR) family. {ECO:0000305}.
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EMBL; AF147263; AAD48959.1; -; Genomic_DNA.
EMBL; AL161503; CAB81095.1; -; Genomic_DNA.
EMBL; CP002687; AEE82532.1; -; Genomic_DNA.
EMBL; AY035106; AAK59611.1; -; mRNA.
EMBL; AY113900; AAM44948.1; -; mRNA.
EMBL; AY087807; AAM65343.1; -; mRNA.
PIR; E85069; E85069.
RefSeq; NP_567300.1; NM_116791.3.
UniGene; At.23984; -.
ProteinModelPortal; Q9S9W2; -.
SMR; Q9S9W2; -.
STRING; 3702.AT4G05530.1; -.
PaxDb; Q9S9W2; -.
PRIDE; Q9S9W2; -.
ProMEX; Q9S9W2; -.
EnsemblPlants; AT4G05530.1; AT4G05530.1; AT4G05530.
GeneID; 825905; -.
Gramene; AT4G05530.1; AT4G05530.1; AT4G05530.
KEGG; ath:AT4G05530; -.
Araport; AT4G05530; -.
TAIR; locus:2135467; AT4G05530.
eggNOG; KOG0725; Eukaryota.
eggNOG; COG1028; LUCA.
KO; K11147; -.
OMA; FELLGAY; -.
OrthoDB; EOG09360O1U; -.
PhylomeDB; Q9S9W2; -.
BioCyc; ARA:AT4G05530-MONOMER; -.
Reactome; R-ATH-5365859; RA biosynthesis pathway.
PRO; PR:Q9S9W2; -.
Proteomes; UP000006548; Chromosome 4.
ExpressionAtlas; Q9S9W2; differential.
Genevisible; Q9S9W2; AT.
GO; GO:0005777; C:peroxisome; IDA:TAIR.
GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
GO; GO:0006631; P:fatty acid metabolic process; IEA:UniProtKB-KW.
GO; GO:0080024; P:indolebutyric acid metabolic process; IMP:TAIR.
GO; GO:0080026; P:response to indolebutyric acid; IMP:TAIR.
GO; GO:0048767; P:root hair elongation; IMP:TAIR.
InterPro; IPR036291; NAD(P)-bd_dom_sf.
InterPro; IPR020904; Sc_DH/Rdtase_CS.
InterPro; IPR002347; SDR_fam.
PRINTS; PR00081; GDHRDH.
PRINTS; PR00080; SDRFAMILY.
SUPFAM; SSF51735; SSF51735; 1.
PROSITE; PS00061; ADH_SHORT; 1.
1: Evidence at protein level;
Complete proteome; Fatty acid metabolism; Lipid metabolism;
Oxidoreductase; Peroxisome; Reference proteome.
CHAIN 1 254 Short-chain dehydrogenase/reductase SDRA.
/FTId=PRO_0000432487.
NP_BIND 15 39 NADP. {ECO:0000250|UniProtKB:P50162}.
MOTIF 252 254 Microbody targeting signal.
{ECO:0000305}.
ACT_SITE 159 159 Proton acceptor.
{ECO:0000250|UniProtKB:P50162,
ECO:0000255|PROSITE-ProRule:PRU10001}.
BINDING 146 146 Substrate.
{ECO:0000250|UniProtKB:P50162}.
MUTAGEN 43 43 R->C: In ibr1-1; resistance to the
inhibitory effect of intermediate levels
of indole-3-butyric acid (IBA) on root
elongation.
{ECO:0000269|PubMed:18725356}.
MUTAGEN 140 140 S->F: In ibr1-8; resistance to the
inhibitory effect of intermediate levels
of indole-3-butyric acid (IBA) on root
elongation.
{ECO:0000269|PubMed:18725356}.
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


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