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   27-MAR-2024, entry version 122.
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; ENSCPOT00000011831.3; ENSCPOP00000010538.2; ENSCPOG00000011717.4.
DR   GeneID; 100725791; -.
DR   KEGG; cpoc:100725791; -.
DR   CTD; 55825; -.
DR   VEuPathDB; HostDB:ENSCPOG00000011717; -.
DR   eggNOG; KOG0725; Eukaryota.
DR   GeneTree; ENSGT00940000156882; -.
DR   HOGENOM; CLU_010194_1_2_1; -.
DR   InParanoid; Q9JIF5; -.
DR   OMA; GYRICIN; -.
DR   OrthoDB; 2731281at2759; -.
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 cell types or 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   CDD; cd05369; TER_DECR_SDR_a; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR002347; SDR_fam.
DR   PANTHER; PTHR24317; PEROXISOMAL TRANS-2-ENOYL-COA REDUCTASE; 1.
DR   PANTHER; PTHR24317:SF7; PEROXISOMAL TRANS-2-ENOYL-COA REDUCTASE; 1.
DR   Pfam; PF13561; adh_short_C2; 1.
DR   PRINTS; PR00081; GDHRDH.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 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
//