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Database: UniProt
Entry: G2XCP1_VERDV
LinkDB: G2XCP1_VERDV
Original site: G2XCP1_VERDV 
ID   G2XCP1_VERDV            Unreviewed;       361 AA.
AC   G2XCP1;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   24-JAN-2024, entry version 47.
DE   SubName: Full=TOXD protein {ECO:0000313|EMBL:EGY16759.1};
GN   ORFNames=VDAG_07923 {ECO:0000313|EMBL:EGY16759.1};
OS   Verticillium dahliae (strain VdLs.17 / ATCC MYA-4575 / FGSC 10137)
OS   (Verticillium wilt).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Plectosphaerellaceae; Verticillium.
OX   NCBI_TaxID=498257 {ECO:0000313|EMBL:EGY16759.1};
RN   [1] {ECO:0000313|EMBL:EGY16759.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=VdLs.17 {ECO:0000313|EMBL:EGY16759.1};
RG   The Broad Institute Genome Sequencing Platform;
RA   Ma L.-J.J., Klosterman S.J., Subbarao K., Dobinson K., Veronese P.,
RA   Kang S., Gold S.E., Young S., Jaffe D., Gnerre S., Berlin A., Heiman D.,
RA   Hepburn T., Sykes S., Alvarado L., Kodira C.D., Lander E., Galagan J.,
RA   Nusbaum C., Birren B.;
RT   "The Genome Sequence of Verticillium dahliae VdLs.17.";
RL   Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC       family. {ECO:0000256|ARBA:ARBA00008072}.
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DR   EMBL; DS572712; EGY16759.1; -; Genomic_DNA.
DR   RefSeq; XP_009650984.1; XM_009652689.1.
DR   AlphaFoldDB; G2XCP1; -.
DR   STRING; 498257.G2XCP1; -.
DR   EnsemblFungi; EGY16759; EGY16759; VDAG_07923.
DR   GeneID; 20709386; -.
DR   KEGG; vda:VDAG_07923; -.
DR   eggNOG; KOG1198; Eukaryota.
DR   HOGENOM; CLU_026673_16_1_1; -.
DR   InParanoid; G2XCP1; -.
DR   OMA; CLEMYPD; -.
DR   OrthoDB; 2267374at2759; -.
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; 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   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   NADP {ECO:0000256|ARBA:ARBA00022857};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT   DOMAIN          18..281
FT                   /note="Enoyl reductase (ER)"
FT                   /evidence="ECO:0000259|SMART:SM00829"
SQ   SEQUENCE   361 AA;  38821 MW;  CE0D78B7233D52C5 CRC64;
     MAVHTQFTPP PTQTAIITQP DLQLGIAKDV PVPRITADNM ILIRTRSVAL NPSDFKMYAA
     FPSPGAVDGT DFAGDVVAVG TAVTQWKVGD RVFGAVQGGN PSNHQSGAFQ EYVPTFELEV
     VRIPDSMSYE TAASIGGACI TTAAVVIYGS LGLRPLPFNK GPEDPATVLV YGGSTASGAM
     IIQLLKLSGH VPIATCSPHN FELVRSRGAE TVFDYHSPTC AADIKSHTNN RLKYAVDCIT
     SPSSVKICHE ALGRMGGKYT AIERIPDLPG LRSVVKREWV MGMTMVGRPI DLGKGYTFPV
     VPEHVKLGFE WRPVCQRLID EGHLLPHPIR MLAGGWNSIL KGLDDLKMQK VSGEKLVSTV
     C
//
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