PECR_PONAB
ID PECR_PONAB Reviewed; 303 AA.
AC Q5RCH8;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Peroxisomal trans-2-enoyl-CoA reductase {ECO:0000305};
DE Short=TERP;
DE EC=1.3.1.38 {ECO:0000250|UniProtKB:Q9JIF5};
GN Name=PECR;
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=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Participates in chain elongation of fatty acids. Catalyzes
CC the reduction of trans-2-enoyl-CoAs of varying chain lengths from 6:1
CC to 16:1, having maximum activity with 10:1 CoA. Has no 2,4-dienoyl-CoA
CC reductase activity. {ECO:0000250|UniProtKB:Q9JIF5}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a (2E)-enoyl-CoA + H(+) + NADPH = a 2,3-saturated acyl-CoA +
CC NADP(+); Xref=Rhea:RHEA:33763, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:58856, ChEBI:CHEBI:65111; EC=1.3.1.38;
CC Evidence={ECO:0000250|UniProtKB:Q9JIF5};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33764;
CC Evidence={ECO:0000250|UniProtKB:Q9JIF5};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-hexenoyl-CoA + H(+) + NADPH = hexanoyl-CoA + NADP(+);
CC Xref=Rhea:RHEA:44956, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:62077, ChEBI:CHEBI:62620;
CC Evidence={ECO:0000250|UniProtKB:Q9JIF5};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44957;
CC Evidence={ECO:0000250|UniProtKB:Q9JIF5};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-octenoyl-CoA + H(+) + NADPH = NADP(+) + octanoyl-CoA;
CC Xref=Rhea:RHEA:44952, ChEBI:CHEBI:15378, ChEBI:CHEBI:57386,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:62242;
CC Evidence={ECO:0000250|UniProtKB:Q9JIF5};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44953;
CC Evidence={ECO:0000250|UniProtKB:Q9JIF5};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-decenoyl-CoA + H(+) + NADPH = decanoyl-CoA + NADP(+);
CC Xref=Rhea:RHEA:44960, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:61406, ChEBI:CHEBI:61430;
CC Evidence={ECO:0000250|UniProtKB:Q9JIF5};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44961;
CC Evidence={ECO:0000250|UniProtKB:Q9JIF5};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-dodecenoyl-CoA + H(+) + NADPH = dodecanoyl-CoA + NADP(+);
CC Xref=Rhea:RHEA:44964, ChEBI:CHEBI:15378, ChEBI:CHEBI:57330,
CC ChEBI:CHEBI:57375, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC Evidence={ECO:0000250|UniProtKB:Q9JIF5};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44965;
CC Evidence={ECO:0000250|UniProtKB:Q9JIF5};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-tetradecenoyl-CoA + H(+) + NADPH = NADP(+) +
CC tetradecanoyl-CoA; Xref=Rhea:RHEA:44968, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57385, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:61405; Evidence={ECO:0000250|UniProtKB:Q9JIF5};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44969;
CC Evidence={ECO:0000250|UniProtKB:Q9JIF5};
CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC {ECO:0000250|UniProtKB:Q9JIF5}.
CC -!- SUBUNIT: Interacts with PEX5, probably required to target it into
CC peroxisomes. {ECO:0000250|UniProtKB:Q9BY49}.
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000250|UniProtKB:Q9JIF5}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
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DR EMBL; CR858292; CAH90529.1; -; mRNA.
DR RefSeq; NP_001127299.1; NM_001133827.2.
DR AlphaFoldDB; Q5RCH8; -.
DR SMR; Q5RCH8; -.
DR STRING; 9601.ENSPPYP00000014695; -.
DR GeneID; 100174357; -.
DR KEGG; pon:100174357; -.
DR CTD; 55825; -.
DR eggNOG; KOG0725; Eukaryota.
DR HOGENOM; CLU_010194_1_2_1; -.
DR InParanoid; Q5RCH8; -.
DR OrthoDB; 1194344at2759; -.
DR UniPathway; UPA00094; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
DR GO; GO:0019166; F:trans-2-enoyl-CoA reductase (NADPH) activity; IEA:UniProtKB-EC.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-UniPathway.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR002347; SDR_fam.
DR PRINTS; PR00081; GDHRDH.
DR PRINTS; PR00080; SDRFAMILY.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 2: Evidence at transcript level;
KW Fatty acid biosynthesis; Fatty acid metabolism; Lipid biosynthesis;
KW Lipid metabolism; NADP; Oxidoreductase; Peroxisome; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..303
FT /note="Peroxisomal trans-2-enoyl-CoA reductase"
FT /id="PRO_0000054742"
FT MOTIF 301..303
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000250"
FT ACT_SITE 179
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 23..47
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT MOD_RES 32
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q99MZ7"
FT MOD_RES 49
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BY49"
FT MOD_RES 179
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9BY49"
SQ SEQUENCE 303 AA; 32589 MW; 7B152CFB5C10A1E1 CRC64;
MASWAKGRSY LAPGLLQGQV AIVTGGATGI GKAIVKELLE LGSNVVIASR KLERLKSAAG
ELQANLPPTK QARVIPIQCN IRNEEEVNNL VKSTLDIFGK INFLVNNGGG QFLSLAEHIS
SKGWHAVLET NLTGTFYMCK AVYSSWMKEH GGSIVNIIVS IKTGLPLAVH SGAARAGVYN
LTKSLALEWA CSGVRINCVA PGVIYSQTAV ENYGSYGQSF FEESFQKIPA KRIGVPEEVS
SVVCFLLSPA ASFITGQSVD VDGGRSLYTH SYEIPDHDNW PKGAGDLSVV KRMKETFKEK
AKL
