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Database: UniProt
Entry: A0A397H7F2_9EURO
LinkDB: A0A397H7F2_9EURO
Original site: A0A397H7F2_9EURO 
ID   A0A397H7F2_9EURO        Unreviewed;       344 AA.
AC   A0A397H7F2;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   24-JAN-2024, entry version 13.
DE   RecName: Full=Enoyl reductase (ER) domain-containing protein {ECO:0000259|SMART:SM00829};
GN   ORFNames=CDV56_100489 {ECO:0000313|EMBL:RHZ59015.1};
OS   Aspergillus thermomutatus.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=41047 {ECO:0000313|EMBL:RHZ59015.1, ECO:0000313|Proteomes:UP000215305};
RN   [1] {ECO:0000313|EMBL:RHZ59015.1, ECO:0000313|Proteomes:UP000215305}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HMR AF 39 {ECO:0000313|EMBL:RHZ59015.1,
RC   ECO:0000313|Proteomes:UP000215305};
RA   Parent-Michaud M., Dufresne P.J., Fournier E., Martineau C., Moreira S.,
RA   Perkins V., De Repentigny L., Dufresne S.F.;
RT   "Draft genome sequence of azole-resistant Aspergillus thermomutatus
RT   (Neosartorya pseudofischeri) strain HMR AF 39, isolated from a human nasal
RT   aspirate.";
RL   Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
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:RHZ59015.1}.
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DR   EMBL; NKHU02000063; RHZ59015.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A397H7F2; -.
DR   STRING; 41047.A0A397H7F2; -.
DR   VEuPathDB; FungiDB:CDV56_100489; -.
DR   OrthoDB; 179761at2759; -.
DR   Proteomes; UP000215305; Unassembled WGS sequence.
DR   GO; GO:0016628; F:oxidoreductase activity, acting on the CH-CH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR   CDD; cd05288; PGDH; 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; IPR041694; ADH_N_2.
DR   InterPro; IPR011032; GroES-like_sf.
DR   InterPro; IPR045010; MDR_fam.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020843; PKS_ER.
DR   PANTHER; PTHR43205; PROSTAGLANDIN REDUCTASE; 1.
DR   PANTHER; PTHR43205:SF7; PROSTAGLANDIN REDUCTASE 1; 1.
DR   Pfam; PF16884; ADH_N_2; 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.
PE   4: Predicted;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000215305}.
FT   DOMAIN          20..342
FT                   /note="Enoyl reductase (ER)"
FT                   /evidence="ECO:0000259|SMART:SM00829"
SQ   SEQUENCE   344 AA;  37423 MW;  8B0B2204800BDD8D CRC64;
     MSSNKALFFK KVPEGYPVPG EHLTIESVDY DANTPAPENG VVLQSLYTSF DPYMRGRMRP
     AHVKSYSPAF ELGKPIDSST IAKVLRSNNA SFKEGDLVIG FVPIQEYIVL DGSQVASIRP
     LENPLGLEDI RVFLGPLGMP GLTAYSSLYE IGKPKKGETI FVSAASGAVG QLVGQLAKHE
     GLKVIGSVGS DEKLEYITKD LGFDGGFNYK KEKPADALAR LAPQGIDIYY ENVGGEHLEA
     ALDAMNNFGR VVVCGLISQY NAAPYPIKNI HNVLVKRIDM RGFIVSDPGM GDKYTEEHQK
     NVQKWIKEGS FKALLHETTG IDNAAEGLVG IFHGKNKGKA VLKF
//
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