ECI1_ARATH
ID ECI1_ARATH Reviewed; 240 AA.
AC O04469; Q0WPJ6;
DT 01-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Enoyl-CoA delta isomerase 1, peroxisomal {ECO:0000305};
DE EC=5.3.3.8 {ECO:0000269|PubMed:18657232};
DE AltName: Full=Delta(3),Delta(2)-enoyl CoA isomerase 1 {ECO:0000303|PubMed:18657232};
DE Short=AtECI1 {ECO:0000303|PubMed:18657232};
GN Name=ECI1 {ECO:0000303|PubMed:18657232};
GN OrderedLocusNames=At1g65520 {ECO:0000312|Araport:AT1G65520};
GN ORFNames=F5I14.5 {ECO:0000312|EMBL:AAB60906.1};
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(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;
RA Shinn P., Chen H., Cheuk R.F., Kim C.J., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2-240.
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.
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 [6]
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).
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.
CC {ECO:0000269|PubMed:18657232}.
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:18657232}.
CC -!- SIMILARITY: Belongs to the enoyl-CoA hydratase/isomerase family.
CC {ECO:0000305}.
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DR EMBL; AC001229; AAB60906.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE34392.1; -; Genomic_DNA.
DR EMBL; BT010695; AAR20752.1; -; mRNA.
DR EMBL; BT012425; AAS92341.1; -; mRNA.
DR EMBL; AK229072; BAF00953.1; -; mRNA.
DR PIR; A96680; A96680.
DR RefSeq; NP_176730.1; NM_105226.4.
DR AlphaFoldDB; O04469; -.
DR SMR; O04469; -.
DR STRING; 3702.AT1G65520.1; -.
DR PaxDb; O04469; -.
DR PRIDE; O04469; -.
DR ProteomicsDB; 224721; -.
DR EnsemblPlants; AT1G65520.1; AT1G65520.1; AT1G65520.
DR GeneID; 842864; -.
DR Gramene; AT1G65520.1; AT1G65520.1; AT1G65520.
DR KEGG; ath:AT1G65520; -.
DR Araport; AT1G65520; -.
DR TAIR; locus:2034178; AT1G65520.
DR eggNOG; ENOG502QSD1; Eukaryota.
DR HOGENOM; CLU_009834_3_2_1; -.
DR InParanoid; O04469; -.
DR OMA; MPFTVGM; -.
DR OrthoDB; 974911at2759; -.
DR PhylomeDB; O04469; -.
DR BioCyc; ARA:AT1G65520-MON; -.
DR BioCyc; MetaCyc:AT1G65520-MON; -.
DR UniPathway; UPA00659; -.
DR PRO; PR:O04469; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; O04469; baseline and differential.
DR Genevisible; O04469; AT.
DR GO; GO:0005777; C:peroxisome; HDA:TAIR.
DR GO; GO:0004165; F:delta(3)-delta(2)-enoyl-CoA isomerase activity; IBA:GO_Central.
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 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 1, peroxisomal"
FT /id="PRO_0000432484"
FT MOTIF 238..240
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000305"
FT SITE 130
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250|UniProtKB:P42126"
SQ SEQUENCE 240 AA; 25908 MW; E1F72C458830C0A1 CRC64;
MCSLEKRDRL FILKLTGDGE HRLNPTLLDS LRSTINQIRS DPSFSQSVLI TTSDGKFFSN
GYDLALAESN PSLSVVMDAK LRSLVADLIS LPMPTIAAVT GHASAAGCIL AMSHDYVLMR
RDRGFLYMSE LDIELIVPAW FMAVIRGKIG SPAARRDVML TAAKVTADVG VKMGIVDSAY
GSAAETVEAA IKLGEEIVQR GGDGHVYGKM RESLLREVLI HTIGEYESGS SVVRSTGSKL
