(data stored in ACNUC7421 zone)

SWISSPROT: 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   30-AUG-2017, entry version 121.
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.- {ECO:0000305};
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; Magnoliophyta; eudicotyledons; Gunneridae;
OC   Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
OC   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.
RT   Sequence features of the regions of 1,011,550 bp covered by seventeen
RT   P1 and TAC clones.";
RL   DNA Res. 6:183-195(1999).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RG   The Arabidopsis Information Portal (Araport);
RL   Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
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.,
RA   Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
RA   Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
RA   Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
RA   Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
RA   Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
RA   Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
RA   Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
RA   Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
RA   Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
RA   Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
RA   Yuan S., Shinozaki K., Davis R.W., Theologis A., 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.,
RA   Seki M., 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, 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
RT   enzyme participating in the beta-oxidation cycle of unsaturated fatty
RT   acids.";
RL   Plant Physiol. 138:1947-1956(2005).
CC   -!- FUNCTION: Converts 3,5-dienoyl-CoAs to the corresponding 2,4-
CC       dienoyl-CoAs. Involved in degradation of unsaturated fatty acids.
CC       {ECO:0000269|PubMed:16040662}.
CC   -!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation.
CC       {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         Note=No experimental confirmation available. {ECO:0000305};
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}.
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   UniGene; At.43208; -.
DR   UniGene; At.75361; -.
DR   ProteinModelPortal; Q9FHR8; -.
DR   SMR; Q9FHR8; -.
DR   IntAct; Q9FHR8; 5.
DR   STRING; 3702.AT5G43280.1; -.
DR   iPTMnet; Q9FHR8; -.
DR   PaxDb; Q9FHR8; -.
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.
DR   Gramene; AT5G43280.2; AT5G43280.2; AT5G43280.
DR   KEGG; ath:AT5G43280; -.
DR   Araport; AT5G43280; -.
DR   TAIR; locus:2169258; AT5G43280.
DR   eggNOG; KOG1681; Eukaryota.
DR   eggNOG; ENOG410XTHX; LUCA.
DR   HOGENOM; HOG000027939; -.
DR   KO; K12663; -.
DR   OMA; SWVKDVC; -.
DR   OrthoDB; EOG09360L0R; -.
DR   PhylomeDB; Q9FHR8; -.
DR   BioCyc; ARA:AT5G43280-MONOMER; -.
DR   BioCyc; MetaCyc:AT5G43280-MONOMER; -.
DR   UniPathway; UPA00659; -.
DR   PRO; PR:Q9FHR8; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   GO; GO:0005777; C:peroxisome; IDA:TAIR.
DR   GO; GO:0051750; F:delta3,5-delta2,4-dienoyl-CoA isomerase activity; IDA:TAIR.
DR   GO; GO:0006635; P:fatty acid beta-oxidation; IEA:UniProtKB-UniPathway.
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.
DR   InterPro; IPR014748; Crontonase_C.
DR   InterPro; IPR001753; Crotonase_core_superfam.
DR   InterPro; IPR018376; Enoyl-CoA_hyd/isom_CS.
DR   Pfam; PF00378; ECH_1; 1.
DR   SUPFAM; SSF52096; SSF52096; 1.
DR   PROSITE; PS00166; ENOYL_COA_HYDRATASE; 1.
PE   2: Evidence at transcript level;
DR   PRODOM; Q9FHR8.
DR   SWISS-2DPAGE; Q9FHR8.
KW   Acetylation; Alternative splicing; Complete proteome;
KW   Fatty acid metabolism; Isomerase; Lipid metabolism; Peroxisome;
KW   Reference proteome.
FT   CHAIN         1    278       Delta(3,5)-Delta(2,4)-dienoyl-CoA
FT                                isomerase, peroxisomal.
FT                                /FTId=PRO_0000435428.
FT   REGION       69     73       Substrate binding.
FT                                {ECO:0000250|UniProtKB:P42126}.
FT   MOTIF       276    278       Microbody targeting signal.
FT                                {ECO:0000305}.
FT   BINDING     128    128       Substrate; via amide nitrogen.
FT                                {ECO:0000250|UniProtKB:P42126}.
FT   SITE        151    151       Important for catalytic activity.
FT                                {ECO:0000250|UniProtKB:P42126}.
FT   MOD_RES       1      1       N-acetylmethionine.
FT                                {ECO:0000250|UniProtKB:Q6NL24}.
FT   VAR_SEQ     216    220       GIGGK -> DSGMI (in isoform 2).
FT                                /FTId=VSP_058073.
FT   VAR_SEQ     221    278       Missing (in isoform 2).
FT                                /FTId=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
//

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