ID G7XYG2_ASPKW Unreviewed; 360 AA.
AC G7XYG2;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 24-JAN-2024, entry version 41.
DE SubName: Full=Alcohol dehydrogenase {ECO:0000313|EMBL:GAA91958.1};
GN ORFNames=AKAW_10072 {ECO:0000313|EMBL:GAA91958.1};
OS Aspergillus kawachii (strain NBRC 4308) (White koji mold) (Aspergillus
OS awamori var. kawachi).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1033177 {ECO:0000313|EMBL:GAA91958.1};
RN [1] {ECO:0000313|EMBL:GAA91958.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IFO 4308 {ECO:0000313|EMBL:GAA91958.1};
RX PubMed=22045919; DOI=10.1128/EC.05224-11;
RA Futagami T., Mori K., Yamashita A., Wada S., Kajiwara Y., Takashita H.,
RA Omori T., Takegawa K., Tashiro K., Kuhara S., Goto M.;
RT "Genome sequence of the white koji mold Aspergillus kawachii IFO 4308, used
RT for brewing the Japanese distilled spirit shochu.";
RL Eukaryot. Cell 10:1586-1587(2011).
CC -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245}.
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. {ECO:0000256|ARBA:ARBA00008072}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; DF126486; GAA91958.1; -; Genomic_DNA.
DR AlphaFoldDB; G7XYG2; -.
DR STRING; 1033177.G7XYG2; -.
DR VEuPathDB; FungiDB:AKAW_10072; -.
DR eggNOG; KOG1198; Eukaryota.
DR InParanoid; G7XYG2; -.
DR Proteomes; UP000006812; Unassembled WGS sequence.
DR GO; GO:0016651; F:oxidoreductase activity, acting on NAD(P)H; IEA:InterPro.
DR CDD; cd08249; enoyl_reductase_like; 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; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020843; PKS_ER.
DR InterPro; IPR047122; Trans-enoyl_RdTase-like.
DR PANTHER; PTHR45348; HYPOTHETICAL OXIDOREDUCTASE (EUROFUNG); 1.
DR PANTHER; PTHR45348:SF1; TRANS-ENOYL REDUCTASE STHE; 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.
PE 3: Inferred from homology;
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT DOMAIN 19..356
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 360 AA; 38227 MW; 512B58B99973105C CRC64;
MHAPIPKTQT AIIAADEEGT LRISHDVPVI DLEPDSVLVK TAALALNPVD SKMAKGFAVP
DAILGFDFAG VVVAIGTGVT RKDLKVGDRV LGTADSMDRK RPSGGGFCQY ASTVATQALR
LPDDMSFTDA ACIGTSLSSA GIALFRSMKL PGSLTAPNTA ANPPYVLVNG GSTSTGTMAL
QLLKLAGFRP IATCSPSHEE LVLSYGAEKT FDYRSADCAK DIKAYTKNAL AYAIDCITVT
SSMKLCYEAI GRAGGRYTAL DPYPEAQATR RVVKPDWILG STVKGRGSTW TAPYGRDADP
DARIFADELY AGAQKHLLEG NLKNHPAKVM SGGFPGILEG LEMIRRKEVS GFKLVYEVEQ
//