ID A0A0D2C121_9EURO Unreviewed; 329 AA.
AC A0A0D2C121;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=Enoyl reductase (ER) domain-containing protein {ECO:0000259|SMART:SM00829};
GN ORFNames=PV05_02962 {ECO:0000313|EMBL:KIW58441.1};
OS Exophiala xenobiotica.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=348802 {ECO:0000313|EMBL:KIW58441.1, ECO:0000313|Proteomes:UP000054342};
RN [1] {ECO:0000313|EMBL:KIW58441.1, ECO:0000313|Proteomes:UP000054342}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 118157 {ECO:0000313|EMBL:KIW58441.1,
RC ECO:0000313|Proteomes:UP000054342};
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 xenobiotica CBS118157.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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; KN847318; KIW58441.1; -; Genomic_DNA.
DR RefSeq; XP_013319025.1; XM_013463571.1.
DR AlphaFoldDB; A0A0D2C121; -.
DR STRING; 348802.A0A0D2C121; -.
DR GeneID; 25324870; -.
DR HOGENOM; CLU_026673_20_2_1; -.
DR OrthoDB; 820313at2759; -.
DR Proteomes; UP000054342; 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:UP000054342};
KW Zinc {ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 13..326
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 329 AA; 35581 MW; 481523691D4BEEF6 CRC64;
MVEIKVFKGS KDGIVEGTTH RDIGSDEVLL RVTHSGLCGT DIHFKSSDLV LGHEGVGIVE
QVGPNVTMFK KGDRAGWGYE HDCCGHCKQC LRGMETFCPE RQMYGLADLD QGSMASHAIW
KESFLFQIPE GLSSEAAAPL MCGGATVFTA LQLHGLKSTD RVGVIGIGGL GHLAILFAAR
MGCEVVVFSG TESKKEEAMK LGASEFYAVK GLKELEVKAP IDHLLVTTAQ QPDWDMYLPV
MAPSGTVYPL TVTTGNLTVP YMPVILKGLK IQGSLVAPRQ VHREMLEFAA AKNINPIVQT
FPLDLDGINK AFETLEGGNM RYRGVLVAQ
//
