DECR2_ARATH
ID DECR2_ARATH Reviewed; 298 AA.
AC Q9LTV6; Q67Y37; Q680G7;
DT 24-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Peroxisomal 2,4-dienoyl-CoA reductase [(3E)-enoyl-CoA-producing] {ECO:0000305};
DE EC=1.3.1.124 {ECO:0000305};
GN OrderedLocusNames=At3g12800; ORFNames=MBK21.23;
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=10819329; DOI=10.1093/dnares/7.2.131;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:131-135(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 (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP SUBCELLULAR LOCATION.
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).
CC -!- FUNCTION: Auxiliary enzyme of beta-oxidation. Participates in the
CC degradation of unsaturated fatty enoyl-CoA esters having double bonds
CC in both even- and odd-numbered positions in peroxisome. Catalyzes the
CC NADP-dependent reduction of 2,4-dienoyl-CoA to yield trans-3-enoyl-CoA
CC (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a (2E,4Z)-dienoyl-CoA + H(+) + NADPH = a 4,5-saturated-(3E)-
CC enoyl-CoA + NADP(+); Xref=Rhea:RHEA:61892, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:85099,
CC ChEBI:CHEBI:85493; EC=1.3.1.124; Evidence={ECO:0000305};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a (2E,4E)-dienoyl-CoA + H(+) + NADPH = a 4,5-saturated-(3E)-
CC enoyl-CoA + NADP(+); Xref=Rhea:RHEA:45912, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:85101,
CC ChEBI:CHEBI:85493; EC=1.3.1.124; Evidence={ECO:0000305};
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:17951448}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. 2,4-dienoyl-CoA reductase subfamily. {ECO:0000305}.
CC -!- CAUTION: Was originally assigned as At3g12790. {ECO:0000305}.
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DR EMBL; AB024033; BAB02424.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE75247.1; -; Genomic_DNA.
DR EMBL; AY072396; AAL62388.1; -; mRNA.
DR EMBL; AY114700; AAM48019.1; -; mRNA.
DR EMBL; AK175259; BAD43022.1; -; mRNA.
DR EMBL; AK175900; BAD43663.1; -; mRNA.
DR EMBL; AK176181; BAD43944.1; -; mRNA.
DR EMBL; AK176305; BAD44068.1; -; mRNA.
DR EMBL; AK176508; BAD44271.1; -; mRNA.
DR EMBL; AK176631; BAD44394.1; -; mRNA.
DR EMBL; AK176892; BAD44655.1; -; mRNA.
DR EMBL; AK176909; BAD44672.1; -; mRNA.
DR EMBL; AK176776; BAD44539.1; -; mRNA.
DR EMBL; AK221326; BAD94126.1; -; mRNA.
DR RefSeq; NP_187886.2; NM_112116.4.
DR AlphaFoldDB; Q9LTV6; -.
DR SMR; Q9LTV6; -.
DR STRING; 3702.AT3G12800.1; -.
DR PaxDb; Q9LTV6; -.
DR PRIDE; Q9LTV6; -.
DR ProteomicsDB; 222198; -.
DR EnsemblPlants; AT3G12800.1; AT3G12800.1; AT3G12800.
DR GeneID; 820462; -.
DR Gramene; AT3G12800.1; AT3G12800.1; AT3G12800.
DR KEGG; ath:AT3G12800; -.
DR Araport; AT3G12800; -.
DR TAIR; locus:2087770; AT3G12800.
DR eggNOG; KOG0725; Eukaryota.
DR HOGENOM; CLU_010194_1_2_1; -.
DR InParanoid; Q9LTV6; -.
DR OMA; GSICSAQ; -.
DR OrthoDB; 1105725at2759; -.
DR PhylomeDB; Q9LTV6; -.
DR BioCyc; ARA:AT3G12800-MON; -.
DR PRO; PR:Q9LTV6; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LTV6; baseline and differential.
DR Genevisible; Q9LTV6; AT.
DR GO; GO:0005777; C:peroxisome; HDA:TAIR.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0008670; F:2,4-dienoyl-CoA reductase (NADPH) activity; IEA:InterPro.
DR GO; GO:0016628; F:oxidoreductase activity, acting on the CH-CH group of donors, NAD or NADP as acceptor; IBA:GO_Central.
DR GO; GO:0009062; P:fatty acid catabolic process; IEA:InterPro.
DR GO; GO:0006631; P:fatty acid metabolic process; IBA:GO_Central.
DR InterPro; IPR045017; DECR2-like.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR002347; SDR_fam.
DR PANTHER; PTHR43296; PTHR43296; 1.
DR PRINTS; PR00081; GDHRDH.
DR PRINTS; PR00080; SDRFAMILY.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 2: Evidence at transcript level;
KW Fatty acid metabolism; Lipid metabolism; NADP; Oxidoreductase; Peroxisome;
KW Reference proteome.
FT CHAIN 1..298
FT /note="Peroxisomal 2,4-dienoyl-CoA reductase [(3E)-enoyl-
FT CoA-producing]"
FT /id="PRO_0000054564"
FT REGION 279..298
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 296..298
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000255"
FT BINDING 19..24
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 44
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 69
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 71
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 101
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 109..111
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 173
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 200..206
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT CONFLICT 127
FT /note="M -> L (in Ref. 4; BAD44394)"
FT /evidence="ECO:0000305"
FT CONFLICT 238..239
FT /note="MA -> IT (in Ref. 4; BAD43663)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 298 AA; 31796 MW; 5606E22FC53D4F0A CRC64;
MDSPFKPDVV RGQVALITGG GSGIGFEISS QFGKHGASIA IMGRRKQVLD DAVSALRSLG
IQAIGLEGDV RKQEDARRVV EATFQHFGKL DILVNAAAGN FLAAAEDLSP NGFRTVLDID
AVGTFNMCHA ALKYLKKGAP GRDSSSGGGS IINISATLHY TASWYQIHVS AAKAAVDATT
RNLALEWGTD YDIRVNGIAP GPIGGTPGMS KLVPEEIENK TREYMPLYKV GEKWDIAMAA
LYLSCDSGKY VSGLTMVVDG GLWLSKPRHL PKEAVKQLSR AVEKRSRAKP VGLPTSKL
