ID B2ACP6_PODAN Unreviewed; 317 AA.
AC B2ACP6;
DT 20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT 20-MAY-2008, sequence version 1.
DT 24-JAN-2024, entry version 74.
DE RecName: Full=2,4-dienoyl-CoA reductase [(3E)-enoyl-CoA-producing] {ECO:0000256|ARBA:ARBA00026117};
DE EC=1.3.1.124 {ECO:0000256|ARBA:ARBA00026117};
GN ORFNames=PODANS_3_1660 {ECO:0000313|EMBL:CAP61211.1};
OS Podospora anserina (strain S / ATCC MYA-4624 / DSM 980 / FGSC 10383)
OS (Pleurage anserina).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Podosporaceae; Podospora;
OC Podospora anserina.
OX NCBI_TaxID=515849 {ECO:0000313|EMBL:CAP61211.1};
RN [1] {ECO:0000313|EMBL:CAP61211.1, ECO:0000313|Proteomes:UP000001197}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S / ATCC MYA-4624 / DSM 980 / FGSC 10383
RC {ECO:0000313|Proteomes:UP000001197}, and S mat+
RC {ECO:0000313|EMBL:CAP61211.1};
RX PubMed=18460219; DOI=10.1186/gb-2008-9-5-r77;
RA Espagne E., Lespinet O., Malagnac F., Da Silva C., Jaillon O., Porcel B.M.,
RA Couloux A., Aury J.-M., Segurens B., Poulain J., Anthouard V.,
RA Grossetete S., Khalili H., Coppin E., Dequard-Chablat M., Picard M.,
RA Contamine V., Arnaise S., Bourdais A., Berteaux-Lecellier V., Gautheret D.,
RA de Vries R.P., Battaglia E., Coutinho P.M., Danchin E.G.J., Henrissat B.,
RA El Khoury R., Sainsard-Chanet A., Boivin A., Pinan-Lucarre B., Sellem C.H.,
RA Debuchy R., Wincker P., Weissenbach J., Silar P.;
RT "The genome sequence of the model ascomycete fungus Podospora anserina.";
RL Genome Biol. 9:R77.1-R77.22(2008).
RN [2] {ECO:0000313|EMBL:CAP61211.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=S mat+ {ECO:0000313|EMBL:CAP61211.1};
RA Genoscope - CEA;
RL Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Proteomes:UP000001197}
RP GENOME REANNOTATION.
RC STRAIN=S / ATCC MYA-4624 / DSM 980 / FGSC 10383
RC {ECO:0000313|Proteomes:UP000001197};
RX PubMed=24558260; DOI=10.1534/genetics.113.159988;
RA Grognet P., Bidard F., Kuchly C., Tong L.C.H., Coppin E., Benkhali J.A.,
RA Couloux A., Wincker P., Debuchy R., Silar P.;
RT "Maintaining two mating types: Structure of the mating type locus and its
RT role in heterokaryosis in Podospora anserina.";
RL Genetics 197:421-432(2014).
RN [4] {ECO:0000313|EMBL:CDP26657.1}
RP NUCLEOTIDE SEQUENCE.
RA Grognet P., Bidard F., Kuchly C., Chan Ho Tong L., Coppin E.,
RA Ait Benkhali J., Couloux A., Wincker P., Debuchy R., Silar P.;
RT "Maintaining two mating types: Structure of the mating type locus and its
RT role in heterokaryosis in Podospora anserina.";
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a (2E,4E)-dienoyl-CoA + H(+) + NADPH = a 4,5-saturated-(3E)-
CC enoyl-CoA + NADP(+); Xref=Rhea:RHEA:45912, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:85101,
CC ChEBI:CHEBI:85493; EC=1.3.1.124;
CC Evidence={ECO:0000256|ARBA:ARBA00024507};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a (2E,4Z)-dienoyl-CoA + H(+) + NADPH = a 4,5-saturated-(3E)-
CC enoyl-CoA + NADP(+); Xref=Rhea:RHEA:61892, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:85099,
CC ChEBI:CHEBI:85493; EC=1.3.1.124;
CC Evidence={ECO:0000256|ARBA:ARBA00024466};
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; CU633448; CAP61211.1; -; Genomic_DNA.
DR EMBL; FO904938; CDP26657.1; -; Genomic_DNA.
DR RefSeq; XP_001903436.1; XM_001903401.1.
DR AlphaFoldDB; B2ACP6; -.
DR STRING; 515849.B2ACP6; -.
DR GeneID; 6187469; -.
DR KEGG; pan:PODANSg451; -.
DR VEuPathDB; FungiDB:PODANS_3_1660; -.
DR eggNOG; KOG0725; Eukaryota.
DR HOGENOM; CLU_010194_1_2_1; -.
DR OrthoDB; 2092693at2759; -.
DR Proteomes; UP000001197; Chromosome 3.
DR GO; GO:0008670; F:2,4-dienoyl-CoA reductase (NADPH) activity; IEA:InterPro.
DR GO; GO:0009062; P:fatty acid catabolic process; IEA:InterPro.
DR CDD; cd05369; TER_DECR_SDR_a; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR045017; DECR2-like.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR002347; SDR_fam.
DR PANTHER; PTHR43296; PEROXISOMAL 2,4-DIENOYL-COA REDUCTASE; 1.
DR PANTHER; PTHR43296:SF2; PEROXISOMAL 2,4-DIENOYL-COA REDUCTASE [(3E)-ENOYL-COA-PRODUCING]; 1.
DR Pfam; PF13561; adh_short_C2; 1.
DR PRINTS; PR00081; GDHRDH.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 4: Predicted;
KW NADP {ECO:0000256|ARBA:ARBA00022857};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000001197}.
SQ SEQUENCE 317 AA; 33091 MW; 7F7326B039C20F11 CRC64;
MSVPRSEYLS TVWKDGIFAN RVLFITGGAG SIGSAQTRAM VHLGADACII GRSVEKTENA
AKEIAKVRNG ARVIGIGNVD VRSYDSLKAA ADRCVKELGS IDYVVAGAAG NFIAPIAGLS
PNAFKAVIDI DTIGTFNTIK ATMPYLVESA ARNPNPNDAG TTGGRFVSTS ATFHYTGMPL
QSHVSAAKAA IDALMGSVAL EYGPFGVTAN SIAPGAIEGT EGMERLASSK LDPKTRTKGV
PIGRWGSVRD IADATVYVFS DAGNYINGTT LVVDGAGWRR QGAAAVGVDD DMQYPDFLLA
GTISKHLKSG RKEKAKI
//