ID A0A168L1Z0_CORDF Unreviewed; 344 AA.
AC A0A168L1Z0;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=Alcohol dehydrogenase {ECO:0000313|EMBL:OAA82601.1};
GN ORFNames=LEL_02146 {ECO:0000313|EMBL:OAA82601.1};
OS Akanthomyces lecanii RCEF 1005.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Cordycipitaceae; Akanthomyces;
OC Cordyceps confragosa.
OX NCBI_TaxID=1081108 {ECO:0000313|EMBL:OAA82601.1, ECO:0000313|Proteomes:UP000076881};
RN [1] {ECO:0000313|EMBL:OAA82601.1, ECO:0000313|Proteomes:UP000076881}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RCEF 1005 {ECO:0000313|EMBL:OAA82601.1,
RC ECO:0000313|Proteomes:UP000076881};
RX PubMed=27071652; DOI=10.1093/gbe/evw082;
RA Shang Y., Xiao G., Zheng P., Cen K., Zhan S., Wang C.;
RT "Divergent and convergent evolution of fungal pathogenicity.";
RL Genome Biol. Evol. 8:1374-1387(2016).
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000256|ARBA:ARBA00005179}.
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:OAA82601.1}.
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DR EMBL; AZHF01000001; OAA82601.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A168L1Z0; -.
DR STRING; 1081108.A0A168L1Z0; -.
DR OrthoDB; 1065708at2759; -.
DR Proteomes; UP000076881; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR CDD; cd08276; MDR7; 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 PANTHER; PTHR45033; -; 1.
DR PANTHER; PTHR45033:SF2; ZINC-TYPE ALCOHOL DEHYDROGENASE-LIKE PROTEIN C1773.06C; 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 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000076881}.
FT DOMAIN 22..341
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 344 AA; 35700 MW; 10FCBE12369456EB CRC64;
MAQVIPQTAK QWNVTAQDCK DGFNALKLSN VALPELGASQ YRDLIIPLGK YPFATSDNVI
PGSDGAGTVI AIGSQVSRFK PGDKVVTLFN QEHIGGPLTA AAAGSGLGGA IDGTLRSVGA
FNEQGLVHQP AGLSAVEAAT LPCAGLTAWN ALHGLADNRV TAGQWVLTQG SGGVSVFALQ
FAKAAGARVI ATTSSPGKAA ALRALGADYV IDSKQNPDWG AEARKITGGV GVDHVVEVVG
PRSMAQGLRA IRVGGVISIV GFVGGGDADD EPSFLDCLTN LCTARGLMVG SRAQMEDMCR
AIEANPDALR PVVDKKRFKL EDVKEAYEYQ WSGKHFGKVC VEIS
//
