ID M7UC90_BOTF1 Unreviewed; 338 AA.
AC M7UC90;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Putative alcohol zinc-protein {ECO:0000313|EMBL:EMR81017.1};
GN ORFNames=BcDW1_10328 {ECO:0000313|EMBL:EMR81017.1};
OS Botryotinia fuckeliana (strain BcDW1) (Noble rot fungus) (Botrytis
OS cinerea).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Sclerotiniaceae; Botrytis.
OX NCBI_TaxID=1290391 {ECO:0000313|EMBL:EMR81017.1, ECO:0000313|Proteomes:UP000012045};
RN [1] {ECO:0000313|Proteomes:UP000012045}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BcDW1 {ECO:0000313|Proteomes:UP000012045};
RX PubMed=23704180; DOI=10.1128/genomea.00252-13;
RA Blanco-Ulate B., Allen G., Powell A.L., Cantu D.;
RT "Draft genome sequence of Botrytis cinerea BcDW1, inoculum for noble rot of
RT grape berries.";
RL Genome Announc. 1:E0025213-E0025213(2013).
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. {ECO:0000256|ARBA:ARBA00008072}.
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DR EMBL; KB708089; EMR81017.1; -; Genomic_DNA.
DR AlphaFoldDB; M7UC90; -.
DR STRING; 1290391.M7UC90; -.
DR HOGENOM; CLU_026673_16_5_1; -.
DR Proteomes; UP000012045; 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}.
FT DOMAIN 3..256
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 338 AA; 36794 MW; EDD58E33012B8A2F CRC64;
MASTQQSLVV QETGKPVVKV TRPIPTPKEN EVLIKTTSVG INPHDAKSRD INLFQLPIPT
TLCNDVAGVI TAKGDKVSGF ELNDHVFGYP KFGVDSQASQ QYAVLEVGSF AKVPSNITDD
EAATIPVNLF ASALSFWSDK SFGFPAPWAD NKTFNASSQA IVILGGGTSC GKFAVQVAKI
TGFGKIVVVA SKSNTDELKS YGATHVIDRH DTDSEVKARV QEAVGDEIIY VYDPINREHS
FAISLLSEKK RGKIITLLRV QPSSGNYDIA QTLGLPQMHM EFSKEFFKLL PSWIISGEIK
TLGFKVFEGG LDVDAFNKIL DDHLAGRNPG KWHFHPNA
//
