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Database: UniProt
Entry: M1W008_CLAP2
LinkDB: M1W008_CLAP2
Original site: M1W008_CLAP2 
ID   M1W008_CLAP2            Unreviewed;       360 AA.
AC   M1W008;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   24-JAN-2024, entry version 36.
DE   SubName: Full=Probable alcohol dehydrogenase (NADP+) {ECO:0000313|EMBL:CCE28626.1};
GN   ORFNames=CPUR_02314 {ECO:0000313|EMBL:CCE28626.1};
OS   Claviceps purpurea (strain 20.1) (Ergot fungus) (Sphacelia segetum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Clavicipitaceae; Claviceps.
OX   NCBI_TaxID=1111077 {ECO:0000313|EMBL:CCE28626.1, ECO:0000313|Proteomes:UP000016801};
RN   [1] {ECO:0000313|EMBL:CCE28626.1, ECO:0000313|Proteomes:UP000016801}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=20.1 {ECO:0000313|EMBL:CCE28626.1,
RC   ECO:0000313|Proteomes:UP000016801};
RX   PubMed=23468653; DOI=10.1371/journal.pgen.1003323;
RA   Schardl C.L., Young C.A., Hesse U., Amyotte S.G., Andreeva K., Calie P.J.,
RA   Fleetwood D.J., Haws D.C., Moore N., Oeser B., Panaccione D.G.,
RA   Schweri K.K., Voisey C.R., Farman M.L., Jaromczyk J.W., Roe B.A.,
RA   O'Sullivan D.M., Scott B., Tudzynski P., An Z., Arnaoudova E.G.,
RA   Bullock C.T., Charlton N.D., Chen L., Cox M., Dinkins R.D., Florea S.,
RA   Glenn A.E., Gordon A., Gueldener U., Harris D.R., Hollin W., Jaromczyk J.,
RA   Johnson R.D., Khan A.K., Leistner E., Leuchtmann A., Li C., Liu J., Liu J.,
RA   Liu M., Mace W., Machado C., Nagabhyru P., Pan J., Schmid J., Sugawara K.,
RA   Steiner U., Takach J.E., Tanaka E., Webb J.S., Wilson E.V., Wiseman J.L.,
RA   Yoshida R., Zeng Z.;
RT   "Plant-symbiotic fungi as chemical engineers: Multi-genome analysis of the
RT   Clavicipitaceae reveals dynamics of alkaloid loci.";
RL   PLoS Genet. 9:E1003323-E1003323(2013).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={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:CCE28626.1}.
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DR   EMBL; CAGA01000009; CCE28626.1; -; Genomic_DNA.
DR   AlphaFoldDB; M1W008; -.
DR   STRING; 1111077.M1W008; -.
DR   VEuPathDB; FungiDB:CPUR_02314; -.
DR   eggNOG; KOG0023; Eukaryota.
DR   HOGENOM; CLU_026673_20_2_1; -.
DR   OrthoDB; 5353053at2759; -.
DR   PhylomeDB; M1W008; -.
DR   Proteomes; UP000016801; Unassembled WGS sequence.
DR   GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   CDD; cd05283; CAD1; 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; IPR047109; CAD-like.
DR   InterPro; IPR011032; GroES-like_sf.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020843; PKS_ER.
DR   PANTHER; PTHR42683; ALDEHYDE REDUCTASE; 1.
DR   PANTHER; PTHR42683:SF14; NADP-DEPENDENT ALCOHOL DEHYDROGENASE C; 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   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000016801};
KW   Zinc {ECO:0000256|RuleBase:RU361277}.
FT   DOMAIN          16..344
FT                   /note="Enoyl reductase (ER)"
FT                   /evidence="ECO:0000259|SMART:SM00829"
SQ   SEQUENCE   360 AA;  38836 MW;  CA20BE66D4B8C1E5 CRC64;
     MGYPDTFTGF CVDGPKTWNK FSKQELKPKP FGDHDIDVEI AACSLCSSDL HTVTGGWGDF
     DGPLCVGHEV VGKAIKVGQH VKNLKVGDRV GVGAQVWACL ECDLCKDKNE NYCPKQVATY
     NSQYTDGSQA HGGFASHIRA HEYFTFKIPD KLETNIAAPL LCAGITTYSP MVRAGVGPGK
     KVAVVGIGGL GHLGLQWGKA LGAETYALSH SPDKKEDALK LGAKEVILTT EDNWAEPWKA
     KFDFVLNCAD ATHKFDMSQY LSILKPGSDF HMVGIPDHPL PELSAGLFAG GAPKLTGSHL
     GNHQEMEAML KLAADKGVAP WIEVMQISEE NCGAAFEAQK ANKFRYRCTL SGFDKAFGKA
//
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