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Database: UniProt
Entry: E3REX0_PYRTT
LinkDB: E3REX0_PYRTT
Original site: E3REX0_PYRTT 
ID   E3REX0_PYRTT            Unreviewed;       362 AA.
AC   E3REX0;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   24-JAN-2024, entry version 46.
DE   RecName: Full=Enoyl reductase (ER) domain-containing protein {ECO:0000259|SMART:SM00829};
GN   ORFNames=PTT_05272 {ECO:0000313|EMBL:EFQ95727.1};
OS   Pyrenophora teres f. teres (strain 0-1) (Barley net blotch fungus)
OS   (Drechslera teres f. teres).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae;
OC   Pyrenophora.
OX   NCBI_TaxID=861557 {ECO:0000313|Proteomes:UP000001067};
RN   [1] {ECO:0000313|EMBL:EFQ95727.1, ECO:0000313|Proteomes:UP000001067}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=0-1 {ECO:0000313|EMBL:EFQ95727.1,
RC   ECO:0000313|Proteomes:UP000001067};
RX   PubMed=21067574; DOI=10.1186/gb-2010-11-11-r109;
RA   Ellwood S.R., Liu Z., Syme R.A., Lai Z., Hane J.K., Keiper F., Moffat C.S.,
RA   Oliver R.P., Friesen T.L.;
RT   "A first genome assembly of the barley fungal pathogen Pyrenophora teres f.
RT   teres.";
RL   Genome Biol. 11:R109.1-R109.14(2010).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC       family. {ECO:0000256|ARBA:ARBA00008072}.
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DR   EMBL; GL532562; EFQ95727.1; -; Genomic_DNA.
DR   RefSeq; XP_003296175.1; XM_003296127.1.
DR   AlphaFoldDB; E3REX0; -.
DR   STRING; 861557.E3REX0; -.
DR   EnsemblFungi; EFQ95727; EFQ95727; PTT_05272.
DR   KEGG; pte:PTT_05272; -.
DR   eggNOG; KOG0023; Eukaryota.
DR   HOGENOM; CLU_026673_20_1_1; -.
DR   OrthoDB; 5295198at2759; -.
DR   Proteomes; UP000001067; Unassembled WGS sequence.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   CDD; cd08297; CAD3; 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   PANTHER; PTHR42940; ALCOHOL DEHYDROGENASE 1-RELATED; 1.
DR   PANTHER; PTHR42940:SF5; ALCOHOL DEHYDROGENASE 2; 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   Reference proteome {ECO:0000313|Proteomes:UP000001067}.
FT   DOMAIN          20..358
FT                   /note="Enoyl reductase (ER)"
FT                   /evidence="ECO:0000259|SMART:SM00829"
SQ   SEQUENCE   362 AA;  37465 MW;  CAD8C1570C935646 CRC64;
     MASSPEIPTK YKAVVYDAPG SISTKIETLD MPEPGAGEVL VNLTHSGVCH SDLGIMTNAW
     KTLPFPTQAG QVGGHEGVGK IVKMGPGMEN AAVKVGDRVG IKWMAGVCES CEACRAGIDA
     SCFSGKISGY YTPGTFQQYV LSPANYVTPI PDGLDSAAAA PLLCAGVTVY SALRKANAES
     GKWVVISGAG GGLGHLAVQF SARGIGHRVI GIDHSSKKDI VMESGAEHFV AVDGTDDVVG
     AVAALTNGLG AHAVVVCTAN NKAYGQGLDM LRFGGRLVCV GIPEGDALPI SSASPGIMVA
     KSLQIVGSAV GSRNEAIETM DFAARGILKT HFRVEKMDKL THVFEEMHAG KLQGRVVIDL
     SD
//
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