DECR2_DANRE
ID DECR2_DANRE Reviewed; 300 AA.
AC Q6NV34; Q7T004;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Peroxisomal 2,4-dienoyl-CoA reductase [(3E)-enoyl-CoA-producing];
DE EC=1.3.1.124 {ECO:0000250|UniProtKB:Q16698};
DE AltName: Full=2,4-dienoyl-CoA reductase 2;
GN Name=decr2; ORFNames=si:ch211-153c20.5, zgc:85626;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
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|UniProtKB:Q16698}.
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;
CC Evidence={ECO:0000250|UniProtKB:Q9NUI1};
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;
CC Evidence={ECO:0000250|UniProtKB:Q9NUI1};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,4E)-hexadienoyl-CoA + H(+) + NADPH = (3E)-hexenoyl-CoA +
CC NADP(+); Xref=Rhea:RHEA:44912, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:84788, ChEBI:CHEBI:84790;
CC Evidence={ECO:0000250|UniProtKB:Q9NUI1};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,4E)-decadienoyl-CoA + H(+) + NADPH = (3E)-decenoyl-CoA +
CC NADP(+); Xref=Rhea:RHEA:44916, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:62244, ChEBI:CHEBI:84793;
CC Evidence={ECO:0000250|UniProtKB:Q9NUI1};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,4Z,7Z,10Z,13Z,16Z,19Z)-docosaheptaenoyl-CoA + H(+) + NADPH
CC = (3E,7Z,10Z,13Z,16Z,19Z)-docosahexaenoyl-CoA + NADP(+);
CC Xref=Rhea:RHEA:44920, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:77559, ChEBI:CHEBI:84791;
CC Evidence={ECO:0000250|UniProtKB:Q9NUI1};
CC -!- SUBUNIT: Monomer, dimer and oligomer. {ECO:0000250|UniProtKB:Q9NUI1}.
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000250|UniProtKB:Q16698}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. 2,4-dienoyl-CoA reductase subfamily. {ECO:0000305}.
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DR EMBL; AL772148; CAE30389.2; -; Genomic_DNA.
DR EMBL; BX322798; CAE30389.2; JOINED; Genomic_DNA.
DR EMBL; BC068332; AAH68332.1; -; mRNA.
DR RefSeq; NP_998486.1; NM_213321.1.
DR AlphaFoldDB; Q6NV34; -.
DR SMR; Q6NV34; -.
DR STRING; 7955.ENSDARP00000066557; -.
DR PaxDb; Q6NV34; -.
DR Ensembl; ENSDART00000066558; ENSDARP00000066557; ENSDARG00000045257.
DR GeneID; 406623; -.
DR KEGG; dre:406623; -.
DR CTD; 26063; -.
DR ZFIN; ZDB-GENE-040426-2612; decr2.
DR eggNOG; KOG0725; Eukaryota.
DR GeneTree; ENSGT00940000153801; -.
DR HOGENOM; CLU_010194_1_2_1; -.
DR InParanoid; Q6NV34; -.
DR OMA; GSICSAQ; -.
DR OrthoDB; 1105725at2759; -.
DR PhylomeDB; Q6NV34; -.
DR TreeFam; TF315256; -.
DR Reactome; R-DRE-390247; Beta-oxidation of very long chain fatty acids.
DR Reactome; R-DRE-9033241; Peroxisomal protein import.
DR PRO; PR:Q6NV34; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 24.
DR Bgee; ENSDARG00000045257; Expressed in liver and 19 other tissues.
DR GO; GO:0005777; C:peroxisome; IBA:GO_Central.
DR GO; GO:0008670; F:2,4-dienoyl-CoA reductase (NADPH) activity; ISS:UniProtKB.
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..300
FT /note="Peroxisomal 2,4-dienoyl-CoA reductase [(3E)-enoyl-
FT CoA-producing]"
FT /id="PRO_0000054563"
FT MOTIF 298..300
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000255"
FT BINDING 42..47
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 67..71
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 67
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 93
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 95
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 125
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 133..135
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 189
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 215..221
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 226
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 300 AA; 31999 MW; CB6B9948986409BF CRC64;
MAEKPQLVNN LPEDVETDEC MNKYTHIYSP DLLSDQVAFI TGGGSGIGFR IAEVLMRHGC
DTVIASRNLE KISQAAKKLT STTGRRCLPI AMDVRQPETI LAAVDETLKT FGRVDILINN
AAGNFLCPAT SLSFNAFKTV MEIDTMGTFN TSKVIYDKWF KDHGGSIVNI SATLGYRGQA
LQVHAGSAKA ANDAMTRHLA VEWGPSGVRV NTVAPGPISG TEGYRRLGGS HAETAGAFHS
IPLQRAGNKT EMAHAVLFLA SRASSYVTGS VLVADGGAWL TSANDVERLL GIVSSRSAKL
