PECR_CAVPO
ID PECR_CAVPO Reviewed; 302 AA.
AC Q9JIF5;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Peroxisomal trans-2-enoyl-CoA reductase {ECO:0000305};
DE EC=1.3.1.38 {ECO:0000269|PubMed:10811639};
GN Name=PECR;
OS Cavia porcellus (Guinea pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC Cavia.
OX NCBI_TaxID=10141;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 92-118, ENZYME ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP AND CATALYTIC ACTIVITY.
RC TISSUE=Liver;
RX PubMed=10811639; DOI=10.1074/jbc.m001168200;
RA Das A.K., Uhler M.D., Hajra A.K.;
RT "Molecular cloning and expression of mammalian peroxisomal trans-2-enoyl-
RT coenzyme A reductase cDNAs.";
RL J. Biol. Chem. 275:24333-24340(2000).
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:0000269|PubMed:10811639}.
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:0000269|PubMed:10811639};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33764;
CC Evidence={ECO:0000305|PubMed:10811639};
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:0000269|PubMed:10811639};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44957;
CC Evidence={ECO:0000305|PubMed:10811639};
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:0000269|PubMed:10811639};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44953;
CC Evidence={ECO:0000305|PubMed:10811639};
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:0000269|PubMed:10811639};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44961;
CC Evidence={ECO:0000305|PubMed:10811639};
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:0000269|PubMed:10811639};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44965;
CC Evidence={ECO:0000305|PubMed:10811639};
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:0000269|PubMed:10811639};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44969;
CC Evidence={ECO:0000305|PubMed:10811639};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=11 uM for decenoyl-CoA {ECO:0000269|PubMed:10811639};
CC KM=53 uM for NADPH {ECO:0000269|PubMed:10811639};
CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC {ECO:0000269|PubMed:10811639}.
CC -!- SUBUNIT: Interacts with PEX5, probably required to target it into
CC peroxisomes. {ECO:0000250|UniProtKB:Q9BY49}.
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:10811639}.
CC -!- TISSUE SPECIFICITY: Expressed in liver. {ECO:0000269|PubMed:10811639}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
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DR EMBL; AF232010; AAF69799.1; -; mRNA.
DR RefSeq; XP_003462124.1; XM_003462076.3.
DR AlphaFoldDB; Q9JIF5; -.
DR SMR; Q9JIF5; -.
DR STRING; 10141.ENSCPOP00000010538; -.
DR SwissLipids; SLP:000001093; -.
DR Ensembl; ENSCPOT00000011831; ENSCPOP00000010538; ENSCPOG00000011717.
DR GeneID; 100725791; -.
DR KEGG; cpoc:100725791; -.
DR CTD; 55825; -.
DR eggNOG; KOG0725; Eukaryota.
DR GeneTree; ENSGT00940000156882; -.
DR HOGENOM; CLU_010194_1_2_1; -.
DR InParanoid; Q9JIF5; -.
DR OMA; RIWDSKV; -.
DR OrthoDB; 1194344at2759; -.
DR TreeFam; TF315256; -.
DR BRENDA; 1.3.1.38; 1225.
DR SABIO-RK; Q9JIF5; -.
DR UniPathway; UPA00094; -.
DR Proteomes; UP000005447; Unassembled WGS sequence.
DR Bgee; ENSCPOG00000011717; Expressed in liver and 13 other tissues.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0005778; C:peroxisomal membrane; IDA:UniProtKB.
DR GO; GO:0005102; F:signaling receptor binding; IEA:Ensembl.
DR GO; GO:0019166; F:trans-2-enoyl-CoA reductase (NADPH) activity; IDA:UniProtKB.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0033306; P:phytol metabolic process; IEA:Ensembl.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR002347; SDR_fam.
DR PRINTS; PR00081; GDHRDH.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 1: Evidence at protein level;
KW Acetylation; Direct protein sequencing; Fatty acid biosynthesis;
KW Fatty acid metabolism; Lipid biosynthesis; Lipid metabolism; NADP;
KW Oxidoreductase; Peroxisome; Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q99MZ7"
FT CHAIN 2..302
FT /note="Peroxisomal trans-2-enoyl-CoA reductase"
FT /id="PRO_0000054739"
FT MOTIF 300..302
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000250"
FT ACT_SITE 178
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 2
FT /note="N-acetylglycine"
FT /evidence="ECO:0000250|UniProtKB:Q99MZ7"
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 83
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q99MZ7"
FT MOD_RES 178
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9BY49"
SQ SEQUENCE 302 AA; 32529 MW; 9C1430D90D4C07C2 CRC64;
MGSWTKCQSC LAPGLLQNRA AIVTGGGTGI GKAIAKELLH LGCNVVIASR KFDRLRAAAE
ELKATLPPSN KAEVTPIQCN IRKEEEVNNL MKSTLALYGK IDFLVNNGGG QFWSSPEHIS
SKGWHAVIET NLTGTFYMCK AAYNSWMKEH GGAIVNIIIL LNGQPFVAHS GAARGGVYNL
TKSLALGWAR SGIRINCVAP GTVYSQTAMD NYGDMGKTLF ADAFQKIPAK RLGVPEEVSS
LVCFLLSPAA SFITGQLVNV DGGQSLYCQN HDIPDHDNWP EGVGDLSTVK KMKESFKQKA
KL
