ECI2_ARATH
ID ECI2_ARATH Reviewed; 240 AA.
AC O23299; Q8LC07;
DT 01-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Enoyl-CoA delta isomerase 2, peroxisomal {ECO:0000305};
DE EC=5.3.3.8 {ECO:0000269|PubMed:18657232};
DE AltName: Full=Delta(3),Delta(2)-enoyl CoA isomerase 2 {ECO:0000303|PubMed:18657232};
DE Short=AtECI2 {ECO:0000303|PubMed:18657232};
DE AltName: Full=Indole-3-butyric acid response 10 {ECO:0000303|PubMed:18725356};
GN Name=ECI2 {ECO:0000303|PubMed:18657232};
GN Synonyms=IBR10 {ECO:0000303|PubMed:18725356};
GN OrderedLocusNames=At4g14430 {ECO:0000312|Araport:AT4G14430};
GN ORFNames=dl3255c {ECO:0000312|EMBL:CAB10222.1};
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=9461215; DOI=10.1038/35140;
RA Bevan M., Bancroft I., Bent E., Love K., Goodman H.M., Dean C.,
RA Bergkamp R., Dirkse W., van Staveren M., Stiekema W., Drost L., Ridley P.,
RA Hudson S.-A., Patel K., Murphy G., Piffanelli P., Wedler H., Wedler E.,
RA Wambutt R., Weitzenegger T., Pohl T., Terryn N., Gielen J., Villarroel R.,
RA De Clercq R., van Montagu M., Lecharny A., Aubourg S., Gy I., Kreis M.,
RA Lao N., Kavanagh T., Hempel S., Kotter P., Entian K.-D., Rieger M.,
RA Schaefer M., Funk B., Mueller-Auer S., Silvey M., James R., Monfort A.,
RA Pons A., Puigdomenech P., Douka A., Voukelatou E., Milioni D.,
RA Hatzopoulos P., Piravandi E., Obermaier B., Hilbert H., Duesterhoeft A.,
RA Moores T., Jones J.D.G., Eneva T., Palme K., Benes V., Rechmann S.,
RA Ansorge W., Cooke R., Berger C., Delseny M., Voet M., Volckaert G.,
RA Mewes H.-W., Klosterman S., Schueller C., Chalwatzis N.;
RT "Analysis of 1.9 Mb of contiguous sequence from chromosome 4 of Arabidopsis
RT thaliana.";
RL Nature 391:485-488(1998).
RN [2]
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 [3]
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 [4]
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 [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [7]
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 [8]
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 [9]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND GENE FAMILY.
RX PubMed=18657232; DOI=10.1111/j.1365-313x.2008.03635.x;
RA Goepfert S., Vidoudez C., Tellgren-Roth C., Delessert S., Hiltunen J.K.,
RA Poirier Y.;
RT "Peroxisomal Delta(3),Delta(2)-enoyl CoA isomerases and evolution of
RT cytosolic paralogues in embryophytes.";
RL Plant J. 56:728-742(2008).
RN [10]
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: Able to isomerize both 3-cis and 3-trans double bonds into
CC the 2-trans form in a range of enoyl-CoA species. Essential for the
CC beta oxidation of unsaturated fatty acids (PubMed:18657232). Involved
CC with IBR1 and IBR3 in the peroxisomal beta-oxidation of indole-3-
CC butyric acid (IBA) to form indole-3-acetic acid (IAA), a biologically
CC active auxin (PubMed:20562230). {ECO:0000269|PubMed:18657232,
CC ECO:0000269|PubMed:20562230}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a (3Z)-enoyl-CoA = a 4-saturated (2E)-enoyl-CoA;
CC Xref=Rhea:RHEA:45900, ChEBI:CHEBI:85097, ChEBI:CHEBI:85489;
CC EC=5.3.3.8; Evidence={ECO:0000269|PubMed:18657232};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a (3E)-enoyl-CoA = a 4-saturated (2E)-enoyl-CoA;
CC Xref=Rhea:RHEA:45228, ChEBI:CHEBI:58521, ChEBI:CHEBI:85097;
CC EC=5.3.3.8; Evidence={ECO:0000269|PubMed:18657232};
CC -!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:17951448,
CC ECO:0000269|PubMed:18657232}.
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). {ECO:0000269|PubMed:18725356,
CC ECO:0000269|PubMed:20562230}.
CC -!- SIMILARITY: Belongs to the enoyl-CoA hydratase/isomerase family.
CC {ECO:0000305}.
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DR EMBL; Z97336; CAB10222.1; -; Genomic_DNA.
DR EMBL; AL161539; CAB78485.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE83444.1; -; Genomic_DNA.
DR EMBL; AF380640; AAK55721.1; -; mRNA.
DR EMBL; AY056091; AAL06979.1; -; mRNA.
DR EMBL; AK229431; BAF01291.1; -; mRNA.
DR EMBL; AY086877; AAM63923.1; -; mRNA.
DR PIR; D71406; D71406.
DR RefSeq; NP_193179.1; NM_117522.3.
DR AlphaFoldDB; O23299; -.
DR SMR; O23299; -.
DR IntAct; O23299; 1.
DR STRING; 3702.AT4G14430.1; -.
DR PaxDb; O23299; -.
DR PRIDE; O23299; -.
DR ProMEX; O23299; -.
DR ProteomicsDB; 224722; -.
DR EnsemblPlants; AT4G14430.1; AT4G14430.1; AT4G14430.
DR GeneID; 827088; -.
DR Gramene; AT4G14430.1; AT4G14430.1; AT4G14430.
DR KEGG; ath:AT4G14430; -.
DR Araport; AT4G14430; -.
DR TAIR; locus:2129730; AT4G14430.
DR eggNOG; ENOG502QS1J; Eukaryota.
DR HOGENOM; CLU_009834_3_2_1; -.
DR InParanoid; O23299; -.
DR OMA; DYRIMNP; -.
DR OrthoDB; 974911at2759; -.
DR PhylomeDB; O23299; -.
DR BioCyc; ARA:AT4G14430-MON; -.
DR BioCyc; MetaCyc:AT4G14430-MON; -.
DR UniPathway; UPA00659; -.
DR PRO; PR:O23299; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; O23299; baseline and differential.
DR Genevisible; O23299; AT.
DR GO; GO:0005777; C:peroxisome; HDA:TAIR.
DR GO; GO:0004165; F:delta(3)-delta(2)-enoyl-CoA isomerase activity; IDA:TAIR.
DR GO; GO:0004300; F:enoyl-CoA hydratase activity; IBA:GO_Central.
DR GO; GO:0006635; P:fatty acid beta-oxidation; IBA:GO_Central.
DR GO; GO:0009062; P:fatty acid catabolic process; IMP:TAIR.
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; IPR029045; ClpP/crotonase-like_dom_sf.
DR InterPro; IPR001753; Enoyl-CoA_hydra/iso.
DR Pfam; PF00378; ECH_1; 1.
DR SUPFAM; SSF52096; SSF52096; 1.
PE 1: Evidence at protein level;
KW Fatty acid metabolism; Isomerase; Lipid metabolism; Peroxisome;
KW Reference proteome.
FT CHAIN 1..240
FT /note="Enoyl-CoA delta isomerase 2, peroxisomal"
FT /id="PRO_0000432485"
FT MOTIF 238..240
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000305"
FT SITE 135
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250|UniProtKB:P42126"
FT CONFLICT 226
FT /note="G -> E (in Ref. 6; AAM63923)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 240 AA; 25773 MW; 71E08246F9B34EEB CRC64;
MCTLEKRGDL FLLTLTGDGE HRFHPDTIAT ILSLLEQAKS QSTRGSILIT TANGKFFSNG
FDLAWAQTAG SKTGAANRLH QMVESFKPVV AALLDLPMPT IAALNGHAAA AGLILALSHD
YVFMRKDRGV LYMSEVDIGL SMPDYFSALV RAKIGTSAAR RELLLSGKKI RGEEAVGLGI
VDSAAYDSEE GVVVASVRLG EKLAAKKWSG EVYASIRKSL YPELCGILGL ETRVFATPKL
