ID F9F3J9_FUSOF Unreviewed; 381 AA.
AC F9F3J9;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 24-JAN-2024, entry version 47.
DE RecName: Full=Enoyl reductase (ER) domain-containing protein {ECO:0000259|SMART:SM00829};
GN ORFNames=FOXB_00974 {ECO:0000313|EMBL:EGU88484.1};
OS Fusarium oxysporum (strain Fo5176) (Fusarium vascular wilt).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium oxysporum species complex.
OX NCBI_TaxID=660025 {ECO:0000313|EMBL:EGU88484.1};
RN [1] {ECO:0000313|EMBL:EGU88484.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Fo5176 {ECO:0000313|EMBL:EGU88484.1};
RX PubMed=21942452; DOI=10.1094/mpmi-08-11-0212;
RA Thatcher L.F., Gardiner D.M., Kazan K., Manners J.;
RT "A highly conserved effector in Fusarium oxysporum is required for full
RT virulence on Arabidopsis.";
RL Mol. Plant Microbe Interact. 25:180-190(2012).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947,
CC ECO:0000256|RuleBase:RU361277};
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. {ECO:0000256|ARBA:ARBA00008072, 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:EGU88484.1}.
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DR EMBL; AFQF01000390; EGU88484.1; -; Genomic_DNA.
DR AlphaFoldDB; F9F3J9; -.
DR STRING; 660025.F9F3J9; -.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd08233; butanediol_DH_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; IPR002328; ADH_Zn_CS.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020843; PKS_ER.
DR PANTHER; PTHR43161:SF23; (R,R)-BUTANEDIOL DEHYDROGENASE-RELATED; 1.
DR PANTHER; PTHR43161; SORBITOL DEHYDROGENASE; 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|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU361277}; NADP {ECO:0000256|ARBA:ARBA00022857};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 14..379
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 381 AA; 40741 MW; 147FBE353FDB9425 CRC64;
MADTMQAVVF HGKGDIRIEE VNVPKPGAKE VQLKPAFVGI CGTDIHEYLE GAFLIPTTPH
PVTGQSAPVI IGHEYSGVVS DVGDEVDDLK PGDRVVVQPI IFDGTCSSCQ RGLINCCSNS
GFIGLSGMEF RKDIHADAAA DIIIGIGGGL ATYTTVPRYA VFKIPDNIPL QVAAQALVEP
LAVAWNAVQQ SNFQPGDTAL ILGAGPIGLA ILQVLKSKGS SQIIVTETAD KRREFATNFG
ATTVLDPTKT NVGEECKKLC AGEGVQVVFD CAGVQSTLET ALAASRPRSV IVNVALWATE
VTISPNYFML NERTFKGSAT YTASVFQEVI DALARDFLTK IGDLNPEPMI TSLIEMDQIE
EKGFKALINY KDTQVKILVR V
//
