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Database: UniProt
Entry: B2ACP6_PODAN
LinkDB: B2ACP6_PODAN
Original site: B2ACP6_PODAN 
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};
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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
//
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