DECR2_PONAB
ID DECR2_PONAB Reviewed; 292 AA.
AC Q5RBV3;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Peroxisomal 2,4-dienoyl-CoA reductase [(3E)-enoyl-CoA-producing];
DE EC=1.3.1.124 {ECO:0000250|UniProtKB:Q9NUI1};
DE AltName: Full=2,4-dienoyl-CoA reductase 2;
GN Name=DECR2;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart;
RG The German cDNA consortium;
RL Submitted (NOV-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 Has activity towards short and medium chain 2,4-dienoyl-CoAs, but also
CC towards 2,4,7,10,13,16,19-docosaheptaenoyl-CoA, suggesting that it does
CC not constitute a rate limiting step in the peroxisomal degradation of
CC docosahexaenoic acid. {ECO:0000250|UniProtKB:Q9NUI1}.
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:Q9Z2M4}.
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; CR858530; CAH90757.1; -; mRNA.
DR RefSeq; NP_001125423.1; NM_001131951.1.
DR AlphaFoldDB; Q5RBV3; -.
DR SMR; Q5RBV3; -.
DR STRING; 9601.ENSPPYP00000007823; -.
DR GeneID; 100172330; -.
DR KEGG; pon:100172330; -.
DR CTD; 26063; -.
DR eggNOG; KOG0725; Eukaryota.
DR InParanoid; Q5RBV3; -.
DR OrthoDB; 1105725at2759; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
DR GO; GO:0008670; F:2,4-dienoyl-CoA reductase (NADPH) activity; ISS:UniProtKB.
DR GO; GO:0009062; P:fatty acid catabolic process; IEA:InterPro.
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 Acetylation; Fatty acid metabolism; Lipid metabolism; NADP; Oxidoreductase;
KW Peroxisome; Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9NUI1"
FT CHAIN 2..292
FT /note="Peroxisomal 2,4-dienoyl-CoA reductase [(3E)-enoyl-
FT CoA-producing]"
FT /id="PRO_0000054561"
FT MOTIF 290..292
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000250"
FT BINDING 35..40
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 60..64
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 60
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 86
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 88
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 118
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 126..128
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 182
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 208..214
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 219
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q9NUI1"
FT MOD_RES 151
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9NUI1"
FT MOD_RES 287
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NUI1"
FT MOD_RES 291
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9NUI1"
SQ SEQUENCE 292 AA; 30792 MW; D2B30390FC8B3D43 CRC64;
MAQPPPDVEG DDCLPAYRHL FCPDLLRDKV AFITGGGSGI GFRIAEIFMR HGCHTVIASR
SLPRVLTAAR KLAGATGRRC LPLSMDVRAP PAIVAAVDQA LKEFGRIDIL INCAAGNFLC
PAGALSFNAF KTVMDIDTSG TFNVSRVLYE KFFRDHGGVI VNITATLGNR GQALQVHAGS
AKAAVDAMTR HLAVEWGPQN IRVNSLAPGP ISGTEGLRRL GGPQASLSTK VTASPLQRLG
NKTEIAHSVL YLASPLASYV TGAVLVADGG AWLTFPNDVK GLADFASFSA KL
