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Database: UniProt
Entry: A0A317V9H5_9EURO
LinkDB: A0A317V9H5_9EURO
Original site: A0A317V9H5_9EURO 
ID   A0A317V9H5_9EURO        Unreviewed;       356 AA.
AC   A0A317V9H5;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   24-JAN-2024, entry version 11.
DE   SubName: Full=NAD(P)-binding protein {ECO:0000313|EMBL:PWY69522.1};
GN   ORFNames=BO70DRAFT_400041 {ECO:0000313|EMBL:PWY69522.1};
OS   Aspergillus heteromorphus CBS 117.55.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1448321 {ECO:0000313|EMBL:PWY69522.1, ECO:0000313|Proteomes:UP000247233};
RN   [1] {ECO:0000313|EMBL:PWY69522.1, ECO:0000313|Proteomes:UP000247233}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 117.55 {ECO:0000313|EMBL:PWY69522.1,
RC   ECO:0000313|Proteomes:UP000247233};
RG   DOE Joint Genome Institute;
RA   Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA   Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA   Salamov A., Henrissat B., Wiebenga A., De Vries R.P., Grigoriev I.V.,
RA   Mortensen U.H., Andersen M.R., Baker S.E.;
RT   "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT   speciation.";
RL   Submitted (DEC-2016) 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:PWY69522.1}.
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DR   EMBL; MSFL01000033; PWY69522.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A317V9H5; -.
DR   STRING; 1448321.A0A317V9H5; -.
DR   VEuPathDB; FungiDB:BO70DRAFT_400041; -.
DR   OrthoDB; 179761at2759; -.
DR   Proteomes; UP000247233; 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:SF42; ALCOHOL DEHYDROGENASE, ZINC-CONTAINING (AFU_ORTHOLOGUE AFUA_7G04530); 1.
DR   PANTHER; PTHR43205; PROSTAGLANDIN REDUCTASE; 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:UP000247233}.
FT   DOMAIN          25..341
FT                   /note="Enoyl reductase (ER)"
FT                   /evidence="ECO:0000259|SMART:SM00829"
SQ   SEQUENCE   356 AA;  38549 MW;  5EDB2753523D223E CRC64;
     MTITNRQLLY ANTPTPAIDP SPTSGTFKIN TITLPDDVPD DKLLLRIHYL ALEPAMRQWL
     TAKRSYIAPV ELGAVMRGQS IAQVIRVGSG LTSQYQVGDW VVAYSGWQEY AVLGAKEAQK
     IAVPTGCRPT DAMSVLGMTG LTAYFGMMEV GQPKAGDTVV VSGAAGATGM VAGQIAKIHG
     AKRVIGIAGS ADKCDFLRNE LGFDYAINYK DEDWMKQLKD ATPEYIDVFF DNVGGEILDA
     CLGRAAQFSR FVICGAISQY NVAKPQGPSN IMQVISQRVK MQGFIVFDYA KQYPEALKNL
     GLWLTQGKIQ RKEHIVQGGL EATPQGLVDL YGGANTGKMM VEVVPVSEAI DDKAKL
//
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