ID   A0A395I6S1_ASPHC        Unreviewed;       366 AA.
AC   A0A395I6S1;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   24-JAN-2024, entry version 13.
DE   SubName: Full=Alcohol dehydrogenase {ECO:0000313|EMBL:RAL13954.1};
GN   ORFNames=BO97DRAFT_15528 {ECO:0000313|EMBL:RAL13954.1};
OS   Aspergillus homomorphus (strain CBS 101889).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1450537 {ECO:0000313|EMBL:RAL13954.1, ECO:0000313|Proteomes:UP000248961};
RN   [1] {ECO:0000313|EMBL:RAL13954.1, ECO:0000313|Proteomes:UP000248961}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 101889 {ECO:0000313|EMBL:RAL13954.1,
RC   ECO:0000313|Proteomes:UP000248961};
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 (FEB-2018) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; KZ824276; RAL13954.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A395I6S1; -.
DR   STRING; 1450537.A0A395I6S1; -.
DR   VEuPathDB; FungiDB:BO97DRAFT_15528; -.
DR   OrthoDB; 1788094at2759; -.
DR   Proteomes; UP000248961; Unassembled WGS sequence.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   CDD; cd05289; MDR_like_2; 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; 1.
DR   InterPro; IPR011032; GroES-like_sf.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020843; PKS_ER.
DR   PANTHER; PTHR43482:SF4; ALCOHOL DEHYDROGENASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_7G06260)-RELATED; 1.
DR   PANTHER; PTHR43482; PROTEIN AST1-RELATED; 1.
DR   Pfam; PF13602; ADH_zinc_N_2; 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   Reference proteome {ECO:0000313|Proteomes:UP000248961}.
FT   DOMAIN          24..364
FT                   /note="Enoyl reductase (ER)"
FT                   /evidence="ECO:0000259|SMART:SM00829"
FT   REGION          1..40
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          165..191
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        172..188
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   366 AA;  39377 MW;  30835B8ABFFB8F6B CRC64;
     MQAIRLHPAS PSPTTTPYSP SNPAPPSALH LDTNIPIPKP SKPDELVIRV KATTVVRDML
     TWPETYSHEY AIPGNDVAGI VTAVFDEQTS DLKPGDEVFG MTHPDRAGAW AEYALVRAPD
     EVARKPAALS WEQAAALPLS ALTAYEALFV HAGLTAPFPE AAAASRLKKK KKKKKEEEEE
     EAQAPAHKHP HRRLLITGAA GAVGVHLVQL AAAVKGLHVV AASSSNARNA EFLLGLGADE
     AVEYAELGGV RHAEFDVVVD AVGGEVLARC WEYVRADGPG VLVSVDSASY DFVQRHTERG
     IRKDGVRALF FIVQGSGTAL RYLAELAERG LLLSLVNCVF PFERVQEAYE LASGRYTGRG
     KVVLTN
//