ID A0A0P7BV16_9HYPO Unreviewed; 372 AA.
AC A0A0P7BV16;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Enoyl reductase (ER) domain-containing protein {ECO:0000259|SMART:SM00829};
GN ORFNames=AK830_g1391 {ECO:0000313|EMBL:KPM45223.1};
OS Neonectria ditissima.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Neonectria.
OX NCBI_TaxID=78410 {ECO:0000313|EMBL:KPM45223.1, ECO:0000313|Proteomes:UP000050424};
RN [1] {ECO:0000313|EMBL:KPM45223.1, ECO:0000313|Proteomes:UP000050424}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R09/05 {ECO:0000313|EMBL:KPM45223.1,
RC ECO:0000313|Proteomes:UP000050424};
RA Gomez-Cortecero A., Harrison R.J., Armitage A.D.;
RT "Draft genome of a European isolate of the apple canker pathogen Neonectria
RT ditissima.";
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947,
CC ECO:0000256|RuleBase:RU361277};
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. {ECO:0000256|RuleBase:RU361277}.
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:KPM45223.1}.
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DR EMBL; LKCW01000010; KPM45223.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0P7BV16; -.
DR STRING; 78410.A0A0P7BV16; -.
DR OrthoDB; 2619844at2759; -.
DR Proteomes; UP000050424; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd08278; benzyl_alcohol_DH; 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; IPR002328; ADH_Zn_CS.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020843; PKS_ER.
DR PANTHER; PTHR43350:SF11; ENOYL REDUCTASE (ER) DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR43350; NAD-DEPENDENT ALCOHOL DEHYDROGENASE; 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; PS00059; ADH_ZINC; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|RuleBase:RU361277};
KW NADP {ECO:0000256|ARBA:ARBA00022857};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000050424};
KW Zinc {ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 14..369
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 372 AA; 39334 MW; 8C3A84E83142A9FD CRC64;
MTTTTALVLK EIKGPFSLEE VTIDKIRDDE AMIEIHATGI CHTDLSCAEG TLPASAPAVL
GHEGGGIVKE VGSSITDLVP GDKVLLSFAH CSTCEQCKSG HPAYCYSFVP LNFGGKRIDG
SATLSIQNKG EKENMYSSFF GQSSFARHTI AHRSSLVKVK SDTDLALFSP LGCGLQTGAG
AILNTLNVEA GKTVAIFGVG SVGMSAVMAA KMRGAKEIIA IDLQQSRLDL ATKLGATQTI
LGNDPDLISK IQQISPPNGV HYAVDCSGVP AVIQNMVDSL GTRGKAATVG APAPGRRAGI
DVFAHVTHGR QYVGCCEGDA IPSKLIPFLM EEHAKGNYPL ENLISVYDMK DFDQAIKDTK
SGKTLKAVLR WR
//
