DECR_CAEEL
ID DECR_CAEEL Reviewed; 309 AA.
AC Q22230;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Probable 2,4-dienoyl-CoA reductase 3 [(3E)-enoyl-CoA-producing] {ECO:0000250|UniProtKB:Q16698};
DE EC=1.3.1.124 {ECO:0000250|UniProtKB:Q16698};
GN Name=decr-1.3 {ECO:0000312|WormBase:T05C12.3};
GN ORFNames=T05C12.3 {ECO:0000312|WormBase:T05C12.3};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
CC -!- FUNCTION: Auxiliary enzyme of beta-oxidation. It participates in the
CC metabolism of unsaturated fatty enoyl-CoA esters having double bonds in
CC both even- and odd-numbered positions. Catalyzes the NADP-dependent
CC reduction of 2,4-dienoyl-CoA to yield trans-3-enoyl-CoA.
CC {ECO:0000250|UniProtKB:Q16698}.
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: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: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; Z66500; CAA91310.1; -; Genomic_DNA.
DR PIR; T24510; T24510.
DR RefSeq; NP_495714.1; NM_063313.1.
DR AlphaFoldDB; Q22230; -.
DR SMR; Q22230; -.
DR BioGRID; 39645; 2.
DR STRING; 6239.T05C12.3; -.
DR PaxDb; Q22230; -.
DR PeptideAtlas; Q22230; -.
DR EnsemblMetazoa; T05C12.3.1; T05C12.3.1; WBGene00011467.
DR GeneID; 174316; -.
DR KEGG; cel:CELE_T05C12.3; -.
DR UCSC; T05C12.3; c. elegans.
DR CTD; 174316; -.
DR WormBase; T05C12.3; CE02315; WBGene00011467; decr-1.3.
DR eggNOG; KOG0725; Eukaryota.
DR GeneTree; ENSGT00940000153801; -.
DR HOGENOM; CLU_010194_1_2_1; -.
DR InParanoid; Q22230; -.
DR OMA; ILTTWVW; -.
DR OrthoDB; 1105725at2759; -.
DR PhylomeDB; Q22230; -.
DR PRO; PR:Q22230; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00011467; Expressed in adult organism and 1 other tissue.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0008670; F:2,4-dienoyl-CoA reductase (NADPH) activity; IBA:GO_Central.
DR GO; GO:0006635; P:fatty acid beta-oxidation; IBA:GO_Central.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR002347; SDR_fam.
DR PRINTS; PR00081; GDHRDH.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 3: Inferred from homology;
KW NADP; Oxidoreductase; Reference proteome.
FT CHAIN 1..309
FT /note="Probable 2,4-dienoyl-CoA reductase 3 [(3E)-enoyl-
FT CoA-producing]"
FT /evidence="ECO:0000305"
FT /id="PRO_0000054880"
FT ACT_SITE 166
FT /note="Proton acceptor"
FT /evidence="ECO:0000255"
FT BINDING 32..37
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q16698"
FT BINDING 57
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q16698"
FT BINDING 57
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9NUI1"
FT BINDING 83
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q16698"
FT BINDING 116
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q16698"
FT BINDING 124
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q16698"
FT BINDING 181
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q16698"
FT BINDING 207..210
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q16698"
FT BINDING 218
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9NUI1"
SQ SEQUENCE 309 AA; 33097 MW; 26C9459B8B33C778 CRC64;
MACKNPKKFF PICNSPILRD GALKGKVALV TGGGTGIGKA IATTFAHLGA SVAIAARRME
KLEQTAEEIM KTTGGICEPF RMDIKDPGMV SDTFDKIDKK FGKHPDILVN NAAGNFIMAT
ERLSPNAHGT IIDIVLKGTM NVTTELGKRC IQSKTGASVT SITAAYARSG APFIVPSAVS
KAGVEIMTKS LATEWSKYGL RFNAVSPGPI PTKGAWGRLF SGEMGDVAEK MKELNPEGRS
GTPEEVANLV AFISSDHMSF MNGVIIDLDG GQQHFNHGSH MGDFLHTWDQ DTWGDVENVI
RGRTGKEKP
