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Database: UniProt
Entry: A0A024TAB3_9STRA
LinkDB: A0A024TAB3_9STRA
Original site: A0A024TAB3_9STRA 
ID   A0A024TAB3_9STRA        Unreviewed;       289 AA.
AC   A0A024TAB3;
DT   09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT   09-JUL-2014, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=Peroxisomal trans-2-enoyl-CoA reductase {ECO:0000256|ARBA:ARBA00041063};
DE            EC=1.3.1.38 {ECO:0000256|ARBA:ARBA00038849};
GN   ORFNames=H310_07822 {ECO:0000313|EMBL:ETV99770.1}, H310_14887
GN   {ECO:0000313|EMBL:ETV90287.1};
OS   Aphanomyces invadans.
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Saprolegniales; Saprolegniaceae;
OC   Aphanomyces.
OX   NCBI_TaxID=157072 {ECO:0000313|EMBL:ETV90287.1};
RN   [1] {ECO:0000313|EMBL:ETV90287.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NJM9701 {ECO:0000313|EMBL:ETV90287.1};
RG   The Broad Institute Genomics Platform;
RA   Russ C., Tyler B., van West P., Dieguez-Uribeondo J., Young S.K., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L., Chapman S.B.,
RA   Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA   Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C., Pearson M.,
RA   Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S., Wortman J.,
RA   Nusbaum C., Birren B.;
RT   "The Genome Sequence of Aphanomyces invadans NJM9701.";
RL   Submitted (DEC-2013) 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:0000256|ARBA:ARBA00037124}.
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:0000256|ARBA:ARBA00036396};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44961;
CC         Evidence={ECO:0000256|ARBA:ARBA00036396};
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:0000256|ARBA:ARBA00036112};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44965;
CC         Evidence={ECO:0000256|ARBA:ARBA00036112};
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:0000256|ARBA:ARBA00035816};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44957;
CC         Evidence={ECO:0000256|ARBA:ARBA00035816};
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:0000256|ARBA:ARBA00036220};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44953;
CC         Evidence={ECO:0000256|ARBA:ARBA00036220};
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:0000256|ARBA:ARBA00036815};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44969;
CC         Evidence={ECO:0000256|ARBA:ARBA00036815};
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:0000256|ARBA:ARBA00036518};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33764;
CC         Evidence={ECO:0000256|ARBA:ARBA00036518};
CC   -!- PATHWAY: Lipid metabolism. {ECO:0000256|ARBA:ARBA00005189}.
CC   -!- SUBUNIT: Interacts with PEX5, probably required to target it into
CC       peroxisomes. {ECO:0000256|ARBA:ARBA00038622}.
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DR   EMBL; KI914051; ETV90287.1; -; Genomic_DNA.
DR   EMBL; KI913966; ETV99770.1; -; Genomic_DNA.
DR   EMBL; KI913966; ETV99771.1; -; Genomic_DNA.
DR   RefSeq; XP_008871546.1; XM_008873324.1.
DR   RefSeq; XP_008871547.1; XM_008873325.1.
DR   RefSeq; XP_008881072.1; XM_008882850.1.
DR   AlphaFoldDB; A0A024TAB3; -.
DR   STRING; 157072.A0A024TAB3; -.
DR   EnsemblFungi; H310_07822-t26_1; H310_07822-t26_1-p1; H310_07822.
DR   EnsemblFungi; H310_07822-t26_3; H310_07822-t26_3-p1; H310_07822.
DR   EnsemblFungi; H310_14887-t26_1; H310_14887-t26_1-p1; H310_14887.
DR   EnsemblProtists; ETV90287; ETV90287; H310_14887.
DR   EnsemblProtists; ETV99770; ETV99770; H310_07822.
DR   EnsemblProtists; ETV99771; ETV99771; H310_07822.
DR   GeneID; 20084872; -.
DR   GeneID; 20091937; -.
DR   VEuPathDB; FungiDB:H310_07822; -.
DR   VEuPathDB; FungiDB:H310_14887; -.
DR   eggNOG; KOG0725; Eukaryota.
DR   OrthoDB; 2731281at2759; -.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
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   PRINTS; PR00080; SDRFAMILY.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   4: Predicted;
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}.
SQ   SEQUENCE   289 AA;  30687 MW;  BD9CF3E2CB826F6B CRC64;
     MTIRGATTVF RDGVFDGRVA VVTGGGTGIG KTIAHELCLL GCSVVLASRT LEMLVAAADE
     IKAQLPTKHS SRSNVVVPIA CDVRDEGQVK RLFERVMSVF HRVDYVVNNA GGQFVSPFEN
     LSLNGWNAVH RLNSTGTFLV TKYAFEAYLK DHGGAIVNVL VAMDKGFPYA SHSGASRAAV
     ENLTKSLAYE WASRGIRVNA VTPGTIESSG LKNYGPVAQQ VCESYSANTP ARRLGTVEEV
     SAAVVFLLSP AAAYTTGTNA LVDGGWNLAG ALVPLPQHIR YPVYGASKL
//
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