ID A0A0D2A3D7_9EURO Unreviewed; 363 AA.
AC A0A0D2A3D7;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Enoyl reductase (ER) domain-containing protein {ECO:0000259|SMART:SM00829};
GN ORFNames=PV08_03702 {ECO:0000313|EMBL:KIW19407.1};
OS Exophiala spinifera.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=91928 {ECO:0000313|EMBL:KIW19407.1, ECO:0000313|Proteomes:UP000053328};
RN [1] {ECO:0000313|EMBL:KIW19407.1, ECO:0000313|Proteomes:UP000053328}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 89968 {ECO:0000313|EMBL:KIW19407.1,
RC ECO:0000313|Proteomes:UP000053328};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Exophiala spinifera CBS89968.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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|RuleBase:RU361277}.
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DR EMBL; KN847493; KIW19407.1; -; Genomic_DNA.
DR RefSeq; XP_016239623.1; XM_016378053.1.
DR AlphaFoldDB; A0A0D2A3D7; -.
DR STRING; 91928.A0A0D2A3D7; -.
DR GeneID; 27330785; -.
DR VEuPathDB; FungiDB:PV08_03702; -.
DR HOGENOM; CLU_026673_20_2_1; -.
DR OrthoDB; 5353053at2759; -.
DR Proteomes; UP000053328; 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:SF85; CINNAMYL ALCOHOL DEHYDROGENASE 6-RELATED; 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:UP000053328};
KW Zinc {ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 17..354
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 363 AA; 39404 MW; 7ED3E51C7E740606 CRC64;
MSTDYKFHGW VGLGKDSANG HMVWREFTPK PFEETDVDIK ITHCGICGSD LHTLRSGWGP
TLYPVVVGHE IVGTVVRVGP KAEGGIVVGD RVGVGAQSMS CLRPDCDECS HDFENYCQNG
QTGTYNSKYR DGSKSYGGYA DYWRGPSHFV FRIPDALPSD IAAPMLCGGI TAFSPLLHHK
AGPGKTVGII GVGGLGHFGI MGAKVLGADK VVAISRTSTK KADALKMGAD DFIATDEDKG
WNRDHRKSLD IIVSTVSSPK MPLQQYLQLL RVGGVFVQIG APEDKLPAVN GFQLLGKRCS
ITGSSIGSPK EIRYMLDLFA EKGVRTWNNN VPMKDANRAI VDMEAGKARY RYVLVNEQHA
SRL
//