ID A1C9J4_ASPCL Unreviewed; 359 AA.
AC A1C9J4;
DT 23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 23-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 81.
DE SubName: Full=Enoyl reductase, putative {ECO:0000313|EMBL:EAW13518.1};
GN ORFNames=ACLA_055660 {ECO:0000313|EMBL:EAW13518.1};
OS Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS NRRL 1 / QM 1276 / 107).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=344612 {ECO:0000313|EMBL:EAW13518.1, ECO:0000313|Proteomes:UP000006701};
RN [1] {ECO:0000313|EMBL:EAW13518.1, ECO:0000313|Proteomes:UP000006701}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1
RC {ECO:0000313|Proteomes:UP000006701};
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. {ECO:0000256|ARBA:ARBA00008072}.
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DR EMBL; DS027048; EAW13518.1; -; Genomic_DNA.
DR RefSeq; XP_001274944.1; XM_001274943.1.
DR AlphaFoldDB; A1C9J4; -.
DR EnsemblFungi; EAW13518; EAW13518; ACLA_055660.
DR GeneID; 4707203; -.
DR KEGG; act:ACLA_055660; -.
DR VEuPathDB; FungiDB:ACLA_055660; -.
DR eggNOG; KOG1198; Eukaryota.
DR HOGENOM; CLU_026673_16_1_1; -.
DR OMA; SDTKMRG; -.
DR OrthoDB; 2267374at2759; -.
DR Proteomes; UP000006701; Unassembled WGS sequence.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
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; 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 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};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000006701}.
FT DOMAIN 23..355
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 359 AA; 37906 MW; E36E896C0459D531 CRC64;
MGSVDTAALV PPTTQRAVIV EAGDRVRVRD DVPLPTLEKT QFLIRTEAVA VNPSDTKMRG
AFVTPGGVLG TDYAGTVVAC GPEVTEVEVG DRVCGAQHAM NANTPHRGSF GEYNISAGKV
WLKLPASVST EGGATFGAGI STAGLALKLL GLPLPDAPVQ KPAYILVNGG STATATIAIQ
LLRLANMIPI ATCSPKNSDQ VKAYGVEATF DYRDPDCATK IKAYTKNNLR YALDCITTAE
STSLCFAALG RAGGKYVSLD PFAQHAATRA TVKTDWVLGP SIFGDGSTWP NPYGRPPSEE
IRAYGEKLWA VAQKLVDDGK LRHHPVRILD GGLDQVLVGM ELVRSGKLSG EKCVVRLVS
//
