ID A0A167BT68_9HYPO Unreviewed; 388 AA.
AC A0A167BT68;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=DmbC {ECO:0000313|EMBL:OAA40385.1};
GN ORFNames=BBO_05969 {ECO:0000313|EMBL:OAA40385.1};
OS Beauveria brongniartii RCEF 3172.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Cordycipitaceae; Beauveria;
OC Beauveria brongniartii.
OX NCBI_TaxID=1081107 {ECO:0000313|EMBL:OAA40385.1};
RN [1] {ECO:0000313|EMBL:OAA40385.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RCEF 3172 {ECO:0000313|EMBL:OAA40385.1};
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 -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. {ECO:0000256|ARBA:ARBA00008072}.
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:OAA40385.1}.
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DR EMBL; AZHA01000019; OAA40385.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A167BT68; -.
DR OrthoDB; 2267374at2759; -.
DR Proteomes; UP000076863; 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; 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:SF6; TRANS-ENOYL REDUCTASE APDC; 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 NADP {ECO:0000256|ARBA:ARBA00022857};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 17..298
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 388 AA; 41489 MW; 27F20C37AAEF6C47 CRC64;
MAAISALPLT QKALKVASPD ALHLVTDAPL PTLDQDDSVL IRVVCVAINP VDGKSAEMSP
TPGATSGTDF AGIVVALRSD SKHRTEMADT IKTGDRVMGF VFGNNPHVLG NGAFAEYVTL
PRRFLWRVPD HMSLEAAASL PVGIASVGMA LHYLHISMSS LLKAVSRSIA APSASHHHDG
AVDSDANVFI LVYGGGTSTG AIAIQILKAA GFTPITCCSS ESASRAKHLG AAATFDYQAA
TCGRDIREYT NDSLTFAIDC LSESASMAIC YEAIGSAGGR YVSLDPFPVR GCVRRSIVPD
WICSFTQFGQ SITWAPPYNL DERPDDYCFA EEWYHLAQKL LDAELIEAPT LEIRSGGLLH
VPEGVSAVKL GQIKRRKLVY HISEEVLL
//
