DEC12_CAEEL
ID DEC12_CAEEL Reviewed; 309 AA.
AC Q23116;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Probable 2,4-dienoyl-CoA reductase decr-1.2 [(3E)-enoyl-CoA-producing] {ECO:0000305};
DE EC=1.3.1.124 {ECO:0000250|UniProtKB:Q16698};
GN Name=decr-1.2 {ECO:0000312|WormBase:W01C9.4};
GN ORFNames=W01C9.4 {ECO:0000312|WormBase:W01C9.4};
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; Z49969; CAA90268.1; -; Genomic_DNA.
DR PIR; T26051; T26051.
DR RefSeq; NP_495805.1; NM_063404.1.
DR AlphaFoldDB; Q23116; -.
DR SMR; Q23116; -.
DR STRING; 6239.W01C9.4; -.
DR PaxDb; Q23116; -.
DR PeptideAtlas; Q23116; -.
DR PRIDE; Q23116; -.
DR EnsemblMetazoa; W01C9.4.1; W01C9.4.1; WBGene00012177.
DR GeneID; 189090; -.
DR KEGG; cel:CELE_W01C9.4; -.
DR UCSC; W01C9.4; c. elegans.
DR CTD; 189090; -.
DR WormBase; W01C9.4; CE02370; WBGene00012177; decr-1.2.
DR eggNOG; KOG0725; Eukaryota.
DR GeneTree; ENSGT00940000153801; -.
DR HOGENOM; CLU_010194_1_2_1; -.
DR InParanoid; Q23116; -.
DR OMA; FPTKGAW; -.
DR OrthoDB; 1105725at2759; -.
DR PhylomeDB; Q23116; -.
DR Reactome; R-CEL-77288; mitochondrial fatty acid beta-oxidation of unsaturated fatty acids.
DR PRO; PR:Q23116; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00012177; Expressed in pharyngeal muscle cell (C elegans) and 2 other tissues.
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 decr-1.2 [(3E)-
FT enoyl-CoA-producing]"
FT /evidence="ECO:0000305"
FT /id="PRO_0000054881"
FT ACT_SITE 166
FT /note="Proton acceptor"
FT /evidence="ECO:0000255"
FT BINDING 28..60
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
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; 33263 MW; 0B54284FA393DE61 CRC64;
MACKNPKKFF PIRKSPVLRD GAFKGKLVLV TGGGTGIGKA IATTFAHLRA TVVIAARRME
KLEQTARDIT KITGGTCEPF QMDIKDPGMV SDAFDKIDMK FGKVPEILVN NAAGNFIMAT
ELLSSNAYGT IIDIVLKGTF NVTTELGKRC IQNKTGASIT SITAGYARAG APFIVPSAVS
KAGVETMTKS LATEWSKYGL RFNAVSPGPI PTKGAWGRLN SGEMGDIAEK MKFLNPEGRV
GSPEEVANLV AFISSDHMSF LNGAIIDLDG GQQHFNHGSH MGDFLHSWDH KNWEDAENLI
RGRTGKEKA
