IBR3_ARATH
ID IBR3_ARATH Reviewed; 824 AA.
AC Q8RWZ3; Q0WM98; Q67ZU5; Q9M7Y6; Q9M7Y7;
DT 01-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Probable acyl-CoA dehydrogenase IBR3 {ECO:0000305};
DE EC=1.3.99.- {ECO:0000305};
DE AltName: Full=Protein INDOLE-3-BUTYRIC ACID RESPONSE 3 {ECO:0000303|PubMed:17277896};
GN Name=IBR3 {ECO:0000303|PubMed:17277896};
GN OrderedLocusNames=At3g06810/At3g06800 {ECO:0000312|Araport:AT3G06810};
GN ORFNames=F3E22.5/F3E22.6 {ECO:0000312|EMBL:AAF63817.1,
GN ECO:0000312|EMBL:AAF63818.1};
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Landsberg erecta;
RX PubMed=17272265; DOI=10.1074/mcp.m600408-mcp200;
RA Maor R., Jones A., Nuehse T.S., Studholme D.J., Peck S.C., Shirasu K.;
RT "Multidimensional protein identification technology (MudPIT) analysis of
RT ubiquitinated proteins in plants.";
RL Mol. Cell. Proteomics 6:601-610(2007).
RN [6]
RP FUNCTION, MUTAGENESIS OF HIS-229, AND DISRUPTION PHENOTYPE.
RX PubMed=17277896; DOI=10.1007/s11103-007-9134-2;
RA Zolman B.K., Nyberg M., Bartel B.;
RT "IBR3, a novel peroxisomal acyl-CoA dehydrogenase-like protein required for
RT indole-3-butyric acid response.";
RL Plant Mol. Biol. 64:59-72(2007).
RN [7]
RP DISRUPTION PHENOTYPE.
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 [8]
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).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT GLY-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [10]
RP FUNCTION, AND INDUCTION.
RX PubMed=23906045; DOI=10.1111/j.1438-8677.2012.00685.x;
RA Huang T.Y., Desclos-Theveniau M., Chien C.T., Zimmerli L.;
RT "Arabidopsis thaliana transgenics overexpressing IBR3 show enhanced
RT susceptibility to the bacterium Pseudomonas syringae.";
RL Plant Biol. 15:832-840(2013).
CC -!- FUNCTION: Involved with IBR1 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 (PubMed:20562230). May be
CC responsible for catalyzing the first step in IBA-CoA beta-oxidation
CC (PubMed:17277896). May play a role in defense response to pathogenic
CC bacteria (PubMed:23906045). {ECO:0000269|PubMed:17277896,
CC ECO:0000269|PubMed:20562230, ECO:0000269|PubMed:23906045}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=A + a 2,3-saturated acyl-CoA = a 2,3-dehydroacyl-CoA + AH2;
CC Xref=Rhea:RHEA:48608, ChEBI:CHEBI:13193, ChEBI:CHEBI:17499,
CC ChEBI:CHEBI:60015, ChEBI:CHEBI:65111; Evidence={ECO:0000305};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:Q709F0};
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000305}.
CC -!- INDUCTION: By infection with the bacterial pathogen P.syringae pv.
CC tomato strain DC3000. {ECO:0000269|PubMed:23906045}.
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:17277896, PubMed:18725356).
CC {ECO:0000269|PubMed:17277896, ECO:0000269|PubMed:18725356,
CC ECO:0000269|PubMed:20562230}.
CC -!- MISCELLANEOUS: Plants over-expressing IBR3 exhibit enhanced
CC susceptibility to the bacterial pathogen P.syringae pv. tomato strain
CC DC3000. {ECO:0000269|PubMed:23906045}.
CC -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF63817.1; Type=Erroneous gene model prediction; Note=Was originally thought to correspond to two different genes At3g06800 and At3g06810.; Evidence={ECO:0000305};
CC Sequence=AAF63818.1; Type=Erroneous gene model prediction; Note=Was originally thought to correspond to two different genes At3g06800 and At3g06810.; Evidence={ECO:0000305};
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DR EMBL; AC023912; AAF63817.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC023912; AAF63818.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE74461.1; -; Genomic_DNA.
DR EMBL; AY091014; AAM14036.1; -; mRNA.
DR EMBL; BT002365; AAN86198.1; -; mRNA.
DR EMBL; AK176022; BAD43785.1; -; mRNA.
DR EMBL; AK229932; BAF01758.1; -; mRNA.
DR RefSeq; NP_187337.2; NM_111561.5.
DR AlphaFoldDB; Q8RWZ3; -.
DR SMR; Q8RWZ3; -.
DR IntAct; Q8RWZ3; 3.
DR STRING; 3702.AT3G06810.1; -.
DR iPTMnet; Q8RWZ3; -.
DR PaxDb; Q8RWZ3; -.
DR PRIDE; Q8RWZ3; -.
DR ProteomicsDB; 248566; -.
DR DNASU; 819865; -.
DR EnsemblPlants; AT3G06810.1; AT3G06810.1; AT3G06810.
DR GeneID; 819865; -.
DR Gramene; AT3G06810.1; AT3G06810.1; AT3G06810.
DR KEGG; ath:AT3G06810; -.
DR Araport; AT3G06810; -.
DR TAIR; locus:2083328; AT3G06810.
DR eggNOG; KOG1469; Eukaryota.
DR HOGENOM; CLU_007526_3_0_1; -.
DR InParanoid; Q8RWZ3; -.
DR OMA; IWAPQIF; -.
DR OrthoDB; 1028522at2759; -.
DR PhylomeDB; Q8RWZ3; -.
DR BioCyc; ARA:AT3G06810-MON; -.
DR PRO; PR:Q8RWZ3; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q8RWZ3; baseline and differential.
DR Genevisible; Q8RWZ3; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
DR GO; GO:0003995; F:acyl-CoA dehydrogenase activity; IBA:GO_Central.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0033539; P:fatty acid beta-oxidation using acyl-CoA dehydrogenase; IBA:GO_Central.
DR GO; GO:0048767; P:root hair elongation; IMP:TAIR.
DR CDD; cd05154; ACAD10_11_N-like; 1.
DR Gene3D; 1.10.540.10; -; 1.
DR Gene3D; 2.40.110.10; -; 1.
DR InterPro; IPR041726; ACAD10_11_N.
DR InterPro; IPR006091; Acyl-CoA_Oxase/DH_mid-dom.
DR InterPro; IPR046373; Acyl-CoA_Oxase/DH_mid-dom_sf.
DR InterPro; IPR036250; AcylCo_DH-like_C.
DR InterPro; IPR009075; AcylCo_DH/oxidase_C.
DR InterPro; IPR013786; AcylCoA_DH/ox_N.
DR InterPro; IPR037069; AcylCoA_DH/ox_N_sf.
DR InterPro; IPR009100; AcylCoA_DH/oxidase_NM_dom.
DR InterPro; IPR002575; Aminoglycoside_PTrfase.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR Pfam; PF00441; Acyl-CoA_dh_1; 1.
DR Pfam; PF02770; Acyl-CoA_dh_M; 1.
DR Pfam; PF02771; Acyl-CoA_dh_N; 1.
DR Pfam; PF01636; APH; 1.
DR SUPFAM; SSF47203; SSF47203; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR SUPFAM; SSF56645; SSF56645; 1.
PE 1: Evidence at protein level;
KW Acetylation; FAD; Fatty acid metabolism; Flavoprotein; Lipid metabolism;
KW Oxidoreductase; Peroxisome; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..824
FT /note="Probable acyl-CoA dehydrogenase IBR3"
FT /id="PRO_0000432488"
FT MOTIF 822..824
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000305"
FT BINDING 555..565
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q709F0"
FT BINDING 589..591
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q709F0"
FT BINDING 706
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q709F0"
FT BINDING 776..780
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q709F0"
FT BINDING 776
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q709F0"
FT MOD_RES 2
FT /note="N-acetylglycine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT MUTAGEN 229
FT /note="H->Y: In ibr3-11; resistance to the inhibitory
FT effect of intermediate levels of indole-3-butyric acid
FT (IBA) on root elongation."
FT /evidence="ECO:0000269|PubMed:17277896"
FT CONFLICT 246
FT /note="V -> D (in Ref. 4; BAD43785)"
FT /evidence="ECO:0000305"
FT CONFLICT 558
FT /note="T -> A (in Ref. 4; BAF01758)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 824 AA; 91713 MW; 8EB06907C448F263 CRC64;
MGSSTGDLVT RIQSAHRFDH DALFRFAADN VSGFPTNPSQ FKVSQFGHGQ SNPTFLIEVG
SGSSLKRYVL RKKPPGKLLQ SAHAVDREFQ VLRALGEHTQ VPVPKVFCLC TDPAVIGTAF
YIMEFMEGRI FIDPKLPNVA PERRNAIYRA TAKALASLHS ADVDAIGLEK YGRRGNYCKR
QIDRWFKQYL ASTSEGKPER NPKMFELVDW LRKNIPAEDS TGATSGLVHG DFRIDNLVFH
PSEDRVIGII DWELSTLGNQ MCDVAYSCMH YIVNVQLDKE HVSEGFETTG LPEGMLSMPE
FLLEYCSASG KPWPAANWKF YVAFSLFRAA SIYTGVYSRW LMGNASAGER ARNTGVQANE
LVESALGYIA RENVLPEHPP SVQRDVSPSY ESLVDGSGRF IPNRKVLELR QKLIKFMETH
IYPMENEFSK LAQSDMRWTV HPQEEKLKEM AKREGLWNLF VPVDSAARAR RELAATENKH
NLSGKSFDQL FGEGLTNLEY GYLCEIMGRS VWAPQVFNCG APDTGNMEVI LRYGNKEQIS
EWLIPLLEGR IRSGFAMTEP QVASSDATNI ECSIRRQGDS YVINGTKWWT SGAMDPRCRV
LILMGKTDFN APKHKQQSMI LVDMRTPGIS VKRPLTVFGF DDAPHGHAEI SFENVVVPAK
NILLGEGRGF EIAQGRLGPG RLHHCMRLIG AAERGMELMA QRALSRKTFG KFIAQHGSFV
SDLAKLRVEL EGTRLLVLEA ADHLDKFGNK KARGILAMAK VAAPNMALKV LDTAIQVHGA
AGVSSDTVLA HLWATARTLR IADGPDEVHL GTIGKLELQR ASKL
