DCI1_ARATH
ID DCI1_ARATH Reviewed; 278 AA.
AC Q9FHR8; A8MRJ9;
DT 17-FEB-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Delta(3,5)-Delta(2,4)-dienoyl-CoA isomerase, peroxisomal {ECO:0000305};
DE Short=AtDCI1 {ECO:0000303|PubMed:16040662};
DE EC=5.3.3.21 {ECO:0000269|PubMed:16040662};
GN Name=DCI1 {ECO:0000303|PubMed:16040662};
GN OrderedLocusNames=At5g43280 {ECO:0000312|Araport:AT5G43280};
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=10470850; DOI=10.1093/dnares/6.3.183;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Kotani H.,
RA Miyajima N., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. IX. Sequence
RT features of the regions of 1,011,550 bp covered by seventeen P1 and TAC
RT clones.";
RL DNA Res. 6:183-195(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] (ISOFORM 1).
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] (ISOFORM 2).
RC STRAIN=cv. Columbia;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=16040662; DOI=10.1104/pp.105.064311;
RA Goepfert S., Vidoudez C., Rezzonico E., Hiltunen J.K., Poirier Y.;
RT "Molecular identification and characterization of the Arabidopsis
RT delta(3,5),delta(2,4)-dienoyl-coenzyme A isomerase, a peroxisomal enzyme
RT participating in the beta-oxidation cycle of unsaturated fatty acids.";
RL Plant Physiol. 138:1947-1956(2005).
CC -!- FUNCTION: Converts 3,5-dienoyl-CoAs to the corresponding 2,4-dienoyl-
CC CoAs. Involved in degradation of unsaturated fatty acids.
CC {ECO:0000269|PubMed:16040662}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a (3E,5Z)-dienoyl-CoA = a (2E,4E)-(5,6-saturated)-dienoyl-CoA;
CC Xref=Rhea:RHEA:45240, ChEBI:CHEBI:85110, ChEBI:CHEBI:85111;
CC EC=5.3.3.21; Evidence={ECO:0000269|PubMed:16040662};
CC -!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:16040662}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9FHR8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9FHR8-2; Sequence=VSP_058073, VSP_058074;
CC -!- TISSUE SPECIFICITY: Expressed in roots, leaves, stems and flowers.
CC {ECO:0000269|PubMed:16040662}.
CC -!- SIMILARITY: Belongs to the enoyl-CoA hydratase/isomerase family.
CC {ECO:0000305}.
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DR EMBL; AB017070; BAB10591.1; -; Genomic_DNA.
DR EMBL; CP002688; AED94936.1; -; Genomic_DNA.
DR EMBL; CP002688; AED94937.1; -; Genomic_DNA.
DR EMBL; AY072351; AAL62343.1; -; mRNA.
DR EMBL; BT002198; AAN72209.1; -; mRNA.
DR EMBL; AK316991; BAH19686.1; -; mRNA.
DR RefSeq; NP_001078698.1; NM_001085229.1. [Q9FHR8-2]
DR RefSeq; NP_199142.1; NM_123694.4. [Q9FHR8-1]
DR AlphaFoldDB; Q9FHR8; -.
DR SMR; Q9FHR8; -.
DR IntAct; Q9FHR8; 5.
DR MINT; Q9FHR8; -.
DR STRING; 3702.AT5G43280.1; -.
DR iPTMnet; Q9FHR8; -.
DR PaxDb; Q9FHR8; -.
DR PRIDE; Q9FHR8; -.
DR ProteomicsDB; 224683; -. [Q9FHR8-1]
DR EnsemblPlants; AT5G43280.1; AT5G43280.1; AT5G43280. [Q9FHR8-1]
DR EnsemblPlants; AT5G43280.2; AT5G43280.2; AT5G43280. [Q9FHR8-2]
DR GeneID; 834346; -.
DR Gramene; AT5G43280.1; AT5G43280.1; AT5G43280. [Q9FHR8-1]
DR Gramene; AT5G43280.2; AT5G43280.2; AT5G43280. [Q9FHR8-2]
DR KEGG; ath:AT5G43280; -.
DR Araport; AT5G43280; -.
DR TAIR; locus:2169258; AT5G43280.
DR eggNOG; KOG1681; Eukaryota.
DR HOGENOM; CLU_009834_7_0_1; -.
DR InParanoid; Q9FHR8; -.
DR OMA; QYVAHVE; -.
DR OrthoDB; 1094098at2759; -.
DR PhylomeDB; Q9FHR8; -.
DR BioCyc; ARA:AT5G43280-MON; -.
DR BioCyc; MetaCyc:AT5G43280-MON; -.
DR UniPathway; UPA00659; -.
DR PRO; PR:Q9FHR8; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FHR8; baseline and differential.
DR GO; GO:0005777; C:peroxisome; IDA:TAIR.
DR GO; GO:0051750; F:delta(3,5)-delta(2,4)-dienoyl-CoA isomerase activity; IDA:TAIR.
DR GO; GO:0006635; P:fatty acid beta-oxidation; IDA:UniProtKB.
DR GO; GO:0009062; P:fatty acid catabolic process; TAS:TAIR.
DR Gene3D; 1.10.12.10; -; 1.
DR InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR InterPro; IPR045002; Ech1-like.
DR InterPro; IPR018376; Enoyl-CoA_hyd/isom_CS.
DR InterPro; IPR001753; Enoyl-CoA_hydra/iso.
DR InterPro; IPR014748; Enoyl-CoA_hydra_C.
DR PANTHER; PTHR43149; PTHR43149; 1.
DR Pfam; PF00378; ECH_1; 1.
DR SUPFAM; SSF52096; SSF52096; 1.
DR PROSITE; PS00166; ENOYL_COA_HYDRATASE; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Fatty acid metabolism; Isomerase;
KW Lipid metabolism; Peroxisome; Reference proteome.
FT CHAIN 1..278
FT /note="Delta(3,5)-Delta(2,4)-dienoyl-CoA isomerase,
FT peroxisomal"
FT /id="PRO_0000435428"
FT MOTIF 276..278
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000305"
FT BINDING 69..73
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P42126"
FT BINDING 128
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P42126"
FT SITE 151
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250|UniProtKB:P42126"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q6NL24"
FT VAR_SEQ 216..220
FT /note="GIGGK -> DSGMI (in isoform 2)"
FT /id="VSP_058073"
FT VAR_SEQ 221..278
FT /note="Missing (in isoform 2)"
FT /id="VSP_058074"
SQ SEQUENCE 278 AA; 29920 MW; 5118850A71C4725B CRC64;
MTMESYKTLE IIRKNTDSSV FHLIINRPSH LNALSLDFFI EFPKALSSLD QNPDVSVIIL
SGAGKHFCSG IDLNSLSSIS TQSSSGNDRG RSSEQLRRKI KSMQAAITAI EQCRKPVIAA
IHGACIGGGV DLITACDIRY CSEDAFFSIK EVDLAIVADL GTLQRLPSIV GYANAMELAL
TARRFSGSEA KDLGLVSKVF GSKSELDNGV TTIAEGIGGK SPLAVTGTKA VLLRSREVSV
EQGLDYVATW NSAMLISDDL NEAVSAQMMK RKPRFAKL
