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Database: UniProt
Entry: A0A0N1P1K5_9EURO
LinkDB: A0A0N1P1K5_9EURO
Original site: A0A0N1P1K5_9EURO 
ID   A0A0N1P1K5_9EURO        Unreviewed;       331 AA.
AC   A0A0N1P1K5;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=NADP-dependent alcohol dehydrogenase 7 {ECO:0000313|EMBL:KPI45330.1};
GN   ORFNames=AB675_2295 {ECO:0000313|EMBL:KPI45330.1};
OS   Phialophora attinorum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Phialophora.
OX   NCBI_TaxID=1664694 {ECO:0000313|EMBL:KPI45330.1, ECO:0000313|Proteomes:UP000038010};
RN   [1] {ECO:0000313|EMBL:KPI45330.1, ECO:0000313|Proteomes:UP000038010}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 131958 {ECO:0000313|EMBL:KPI45330.1,
RC   ECO:0000313|Proteomes:UP000038010};
RA   Moreno L.F., Stielow B.J., de Hoog S., Vicente V.A., Weiss V.A.,
RA   de Vries M., Cruz L.M., Souza E.M.;
RT   "Draft genome of the ant-associated black yeast Phialophora attae CBS
RT   131958.";
RL   Submitted (JUN-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}.
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:KPI45330.1}.
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DR   EMBL; LFJN01000002; KPI45330.1; -; Genomic_DNA.
DR   RefSeq; XP_018005293.1; XM_018142254.1.
DR   AlphaFoldDB; A0A0N1P1K5; -.
DR   STRING; 1664694.A0A0N1P1K5; -.
DR   GeneID; 28734134; -.
DR   OrthoDB; 5353053at2759; -.
DR   Proteomes; UP000038010; 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; 2.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
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:UP000038010};
KW   Zinc {ECO:0000256|RuleBase:RU361277}.
FT   DOMAIN          17..328
FT                   /note="Enoyl reductase (ER)"
FT                   /evidence="ECO:0000259|SMART:SM00829"
SQ   SEQUENCE   331 AA;  36088 MW;  A71532A7E3C3F1A2 CRC64;
     MAGQSPQFQG WLAHDKNSIG NLQWGSFEPK PWEETDVDIR ITHCGICGSD LHTLSSGWGP
     TNYPCVVGHE IVGEAIRVGS QVKHVKVGDR VGVGAQSDSC QGRKQKCDDC ANDRPNICTN
     RGRADTYNST FLTGGKSYGG YATHNRCPGA FVIPIPDGVD TADAAPMLCG GITTYAPLKN
     NGCGPGKRVG IKREAQRRPP TRRGRYIATE DDEGWHKKHA SSLDIIICTV SSPKMPLRQY
     LGLLRSHGVF IQVGAPEEPL PPISAFDLMS KERKIGGSSI GPPSQIREML QLAAEKGIKP
     WVEKRSMRDA NQAVVDMDAG RARYRYTLCN E
//
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