位置:首页 > 蛋白库 > PECR_PONAB
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024