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Database: UniProt
Entry: R1G305_BOTPV
LinkDB: R1G305_BOTPV
Original site: R1G305_BOTPV 
ID   R1G305_BOTPV            Unreviewed;       335 AA.
AC   R1G305;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   SubName: Full=Putative nadp-dependent alcohol dehydrogenase protein {ECO:0000313|EMBL:EOD45805.1};
GN   ORFNames=UCRNP2_7438 {ECO:0000313|EMBL:EOD45805.1};
OS   Botryosphaeria parva (strain UCR-NP2) (Grapevine canker fungus)
OS   (Neofusicoccum parvum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetes incertae sedis; Botryosphaeriales; Botryosphaeriaceae;
OC   Neofusicoccum.
OX   NCBI_TaxID=1287680 {ECO:0000313|EMBL:EOD45805.1, ECO:0000313|Proteomes:UP000013521};
RN   [1] {ECO:0000313|Proteomes:UP000013521}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCR-NP2 {ECO:0000313|Proteomes:UP000013521};
RX   PubMed=23766404; DOI=10.1128/genomea.00339-13;
RA   Blanco-Ulate B., Rolshausen P., Cantu D.;
RT   "Draft genome sequence of Neofusicoccum parvum isolate UCR-NP2, a fungal
RT   vascular pathogen associated with grapevine cankers.";
RL   Genome Announc. 1:E0033913-E0033913(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}.
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DR   EMBL; KB916543; EOD45805.1; -; Genomic_DNA.
DR   RefSeq; XP_007586693.1; XM_007586631.1.
DR   AlphaFoldDB; R1G305; -.
DR   STRING; 1287680.R1G305; -.
DR   KEGG; npa:UCRNP2_7438; -.
DR   eggNOG; KOG0023; Eukaryota.
DR   HOGENOM; CLU_026673_20_2_1; -.
DR   OMA; SGMCFTD; -.
DR   OrthoDB; 820313at2759; -.
DR   Proteomes; UP000013521; 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:SF18; NADP-DEPENDENT ALCOHOL DEHYDROGENASE (AFU_ORTHOLOGUE AFUA_6G00510); 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:UP000013521};
KW   Zinc {ECO:0000256|RuleBase:RU361277}.
FT   DOMAIN          10..329
FT                   /note="Enoyl reductase (ER)"
FT                   /evidence="ECO:0000259|SMART:SM00829"
SQ   SEQUENCE   335 AA;  36233 MW;  CBB1706A2C1AAE5E CRC64;
     MPHTFTVYKG SSSGAIVEAQ TTRPDLTDDQ VYVRVTASGL CGTDLHYRGA DMALGHEGVG
     VVESVGPKVK ALKAGDRVGW GYQHDECGHC QQCFTGQDVY CKERAMYGFA DLDQGSFATG
     AVWREAFLFK IPDGLTDEDA APLQCGGATV WTCFDDYNIA PTARVGIMGI GGLGHLAIQF
     SAKRGCDTVV FSGTNSKKEE AIKLGAHEFY ATKDQKDLDI GAPLDALLVC TSAHIDWSLY
     MPLLAPGAII FPLSVESGNL VIPYMPLLQA GLRIQGSIVA NRATHNRMLE FAARHQIKPL
     LNKFPMSVEG IEEAMKVLNE GKMRYRGVVV PADKL
//
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