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Database: UniProt
Entry: A0A139HN00_9PEZI
LinkDB: A0A139HN00_9PEZI
Original site: A0A139HN00_9PEZI 
ID   A0A139HN00_9PEZI        Unreviewed;       365 AA.
AC   A0A139HN00;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=Enoyl reductase (ER) domain-containing protein {ECO:0000259|SMART:SM00829};
GN   ORFNames=AC578_760 {ECO:0000313|EMBL:KXT03772.1};
OS   Pseudocercospora eumusae.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Pseudocercospora.
OX   NCBI_TaxID=321146 {ECO:0000313|EMBL:KXT03772.1, ECO:0000313|Proteomes:UP000070133};
RN   [1] {ECO:0000313|EMBL:KXT03772.1, ECO:0000313|Proteomes:UP000070133}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 114824 {ECO:0000313|EMBL:KXT03772.1,
RC   ECO:0000313|Proteomes:UP000070133};
RA   Chang T.-C., Salvucci A., Crous P.W., Stergiopoulos I.;
RT   "Comparative genomics of the Sigatoka disease complex on banana suggests a
RT   link between parallel evolutionary changes in Pseudocercospora fijiensis
RT   and Pseudocercospora eumusae and increased virulence on the banana host.";
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245}.
CC   -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC       family. {ECO:0000256|ARBA:ARBA00008072}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KXT03772.1}.
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DR   EMBL; LFZN01000027; KXT03772.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A139HN00; -.
DR   STRING; 321146.A0A139HN00; -.
DR   OrthoDB; 2267374at2759; -.
DR   Proteomes; UP000070133; Unassembled WGS sequence.
DR   GO; GO:0016651; F:oxidoreductase activity, acting on NAD(P)H; IEA:InterPro.
DR   CDD; cd08249; enoyl_reductase_like; 1.
DR   Gene3D; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR013149; ADH-like_C.
DR   InterPro; IPR013154; ADH-like_N.
DR   InterPro; IPR011032; GroES-like_sf.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020843; PKS_ER.
DR   InterPro; IPR047122; Trans-enoyl_RdTase-like.
DR   PANTHER; PTHR45348; HYPOTHETICAL OXIDOREDUCTASE (EUROFUNG); 1.
DR   PANTHER; PTHR45348:SF2; ZINC-TYPE ALCOHOL DEHYDROGENASE-LIKE PROTEIN C2E1P3.01; 1.
DR   Pfam; PF08240; ADH_N; 1.
DR   Pfam; PF00107; ADH_zinc_N; 1.
DR   SMART; SM00829; PKS_ER; 1.
DR   SUPFAM; SSF50129; GroES-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000070133}.
FT   DOMAIN          16..349
FT                   /note="Enoyl reductase (ER)"
FT                   /evidence="ECO:0000259|SMART:SM00829"
SQ   SEQUENCE   365 AA;  39369 MW;  2315C5817D15D355 CRC64;
     MAASVPSKMK AITIHGNKAK ISEVPVPKLR PTYILTKVDS IALNPTDWKH INTKRAAEGC
     ISGSDFSGTV VEVGSEVSKA FKPGDRIACT THGANASEPE DGCFSEYAVA KGDLCVLLPD
     RLSFEAAATF PLGVSTVGQG LYQQGLKLNL PTDPTKNDET VLIYGGSSAT GSLAIQFAKL
     SGYKVLTTCS PHNNEFVKSL GADAVYDYKD SNCGKNINKD TKDSLKLIWD TISLEGSAKV
     CAEALSSDST GTKYWNIRPV KLPGRDGVDQ GFTLMYTIFN EAFSKAGRET PAKQEDFDFA
     KKFFNITQNL LAEGKLKTHP EKVGEKGLEG ALKGMEDMKN DKVSANKLVY RVRDTPSDSK
     AEVDL
//
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