ID E4ZQN2_LEPMJ Unreviewed; 391 AA.
AC E4ZQN2;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 08-NOV-2023, entry version 55.
DE RecName: Full=Enoyl reductase (ER) domain-containing protein {ECO:0000259|SMART:SM00829};
GN ORFNames=LEMA_P037110.1 {ECO:0000313|EMBL:CBX94037.1};
OS Leptosphaeria maculans (strain JN3 / isolate v23.1.3 / race Av1-4-5-6-7-8)
OS (Blackleg fungus) (Phoma lingam).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Leptosphaeriaceae;
OC Plenodomus; Plenodomus lingam/Leptosphaeria maculans species complex.
OX NCBI_TaxID=985895 {ECO:0000313|Proteomes:UP000002668};
RN [1] {ECO:0000313|Proteomes:UP000002668}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JN3 / isolate v23.1.3 / race Av1-4-5-6-7-8
RC {ECO:0000313|Proteomes:UP000002668};
RX PubMed=21326234; DOI=10.1038/ncomms1189;
RA Rouxel T., Grandaubert J., Hane J.K., Hoede C., van de Wouw A.P.,
RA Couloux A., Dominguez V., Anthouard V., Bally P., Bourras S.,
RA Cozijnsen A.J., Ciuffetti L.M., Degrave A., Dilmaghani A., Duret L.,
RA Fudal I., Goodwin S.B., Gout L., Glaser N., Linglin J., Kema G.H.J.,
RA Lapalu N., Lawrence C.B., May K., Meyer M., Ollivier B., Poulain J.,
RA Schoch C.L., Simon A., Spatafora J.W., Stachowiak A., Turgeon B.G.,
RA Tyler B.M., Vincent D., Weissenbach J., Amselem J., Quesneville H.,
RA Oliver R.P., Wincker P., Balesdent M.-H., Howlett B.J.;
RT "Effector diversification within compartments of the Leptosphaeria maculans
RT genome affected by Repeat-Induced Point mutations.";
RL Nat. Commun. 2:202-202(2011).
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DR EMBL; FP929116; CBX94037.1; -; Genomic_DNA.
DR RefSeq; XP_003837477.1; XM_003837429.1.
DR AlphaFoldDB; E4ZQN2; -.
DR STRING; 985895.E4ZQN2; -.
DR EnsemblFungi; CBX94037; CBX94037; LEMA_P037110.1.
DR GeneID; 13285082; -.
DR eggNOG; KOG1197; Eukaryota.
DR HOGENOM; CLU_026673_3_1_1; -.
DR InParanoid; E4ZQN2; -.
DR OMA; THIATRE; -.
DR OrthoDB; 148501at2759; -.
DR Proteomes; UP000002668; Genome.
DR GO; GO:0003960; F:NADPH:quinone reductase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd05286; QOR2; 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; IPR047618; QOR-like.
DR InterPro; IPR002364; Quin_OxRdtase/zeta-crystal_CS.
DR PANTHER; PTHR48106; QUINONE OXIDOREDUCTASE PIG3-RELATED; 1.
DR PANTHER; PTHR48106:SF13; QUINONE OXIDOREDUCTASE-RELATED; 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.
DR PROSITE; PS01162; QOR_ZETA_CRYSTAL; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000002668}.
FT DOMAIN 75..389
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 391 AA; 42138 MW; C528C56345CDCC5A CRC64;
MTCAGKRGSP AIARGRVFII NEASKNSNTG AIAAVARLPS LKAHQHFTDT PQNIWKRTMA
SLPKTMKAVL IEQTGGTDVL QYKTDVPVPT PKDGEVLVKN DFIGINYIDT YFRSGVYQPP
HFPYILGREG AGTVAAVGPN VPSDLPVGAR VAYMGQYAYA EYTAAPSNYT VPIPDSIDSK
TAAASLLQAL TAVTLIRDAY AVQKGDWILV TAAAGGVGLW LCQLLKAVGA RVIATASTSE
KRALAKENGA EVLLEYHEDD RDVFVKKVLE VTGGEGVHAV FDSVGKATFD SSLAVVRRKG
TMVSFGNASG PVEGFSLARL SAKNVKLLRP TLFNYIATRE ELQQASKELW NFIDKDGLKV
KIHDVYPLSD IVRATEDIQS RKTTGKLVLK P
//