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Database: UniProt
Entry: R1GKY4_BOTPV
LinkDB: R1GKY4_BOTPV
Original site: R1GKY4_BOTPV 
ID   R1GKY4_BOTPV            Unreviewed;       362 AA.
AC   R1GKY4;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   SubName: Full=Putative zinc-binding dehydrogenase family protein {ECO:0000313|EMBL:EOD46644.1};
GN   ORFNames=UCRNP2_6617 {ECO:0000313|EMBL:EOD46644.1};
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:EOD46644.1, 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   -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245}.
CC   -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC       family. {ECO:0000256|ARBA:ARBA00008072}.
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DR   EMBL; KB916424; EOD46644.1; -; Genomic_DNA.
DR   RefSeq; XP_007585874.1; XM_007585812.1.
DR   AlphaFoldDB; R1GKY4; -.
DR   KEGG; npa:UCRNP2_6617; -.
DR   eggNOG; KOG1198; Eukaryota.
DR   HOGENOM; CLU_026673_16_1_1; -.
DR   OMA; KGSIDIC; -.
DR   OrthoDB; 2267374at2759; -.
DR   Proteomes; UP000013521; Unassembled WGS sequence.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
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:SF1; TRANS-ENOYL REDUCTASE STHE; 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   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000013521}.
FT   DOMAIN          17..360
FT                   /note="Enoyl reductase (ER)"
FT                   /evidence="ECO:0000259|SMART:SM00829"
SQ   SEQUENCE   362 AA;  38054 MW;  E29757C340DD59D3 CRC64;
     MADLPTKQTA LTFQEDGTLG ISHDAPVPEL KPDMIIVKTA AVSVNPVDTK MESGFAKPGC
     IGGCDFAGTV VAVGSAVRRP VSVGDRVTGA VMGSDPHDPS SGSFATYVSA PADITLTLPA
     DVPWTVGTSL STVWFTVGQA LFHHLLAADL PAVKPSTPYA GDKAPPTVLV YGGSTSVGTA
     AIQLLKLAGL RPIATCSPRN FDLVKSYGAE EVYDYKSPTC AEDIKKATKN NLRYALDCIT
     TKDSIALCYA ALGRAGGRYT ALDPFWEATA ATRKTVKPNW TLGITMLGKD IAWPPPYGRD
     GSEEARSFGA GWAGELQALL EAGKIRPHPL RAKEGAGWED VLGGLKEVKE GKVSGEKLVF
     AF
//
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