TENC_BEABA
ID TENC_BEABA Reviewed; 388 AA.
AC A0JJU0;
DT 30-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 1.
DT 03-AUG-2022, entry version 51.
DE RecName: Full=Trans-enoyl reductase tenC {ECO:0000303|PubMed:20575135};
DE EC=1.-.-.- {ECO:0000269|PubMed:18266306};
DE AltName: Full=Tenellin biosynthesis protein C {ECO:0000303|PubMed:20575135};
GN Name=tenC {ECO:0000303|PubMed:20575135};
GN Synonyms=ORF3 {ECO:0000303|PubMed:17216664};
OS Beauveria bassiana (White muscardine disease fungus) (Tritirachium
OS shiotae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Cordycipitaceae; Beauveria.
OX NCBI_TaxID=176275;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND PATHWAY.
RC STRAIN=CBS 110.25;
RX PubMed=17216664; DOI=10.1002/cbic.200600398;
RA Eley K.L., Halo L.M., Song Z., Powles H., Cox R.J., Bailey A.M.,
RA Lazarus C.M., Simpson T.J.;
RT "Biosynthesis of the 2-pyridone tenellin in the insect pathogenic fungus
RT Beauveria bassiana.";
RL ChemBioChem 8:289-297(2007).
RN [2]
RP FUNCTION, AND PATHWAY.
RX PubMed=18266306; DOI=10.1002/cbic.200700390;
RA Halo L.M., Marshall J.W., Yakasai A.A., Song Z., Butts C.P., Crump M.P.,
RA Heneghan M., Bailey A.M., Simpson T.J., Lazarus C.M., Cox R.J.;
RT "Authentic heterologous expression of the tenellin iterative polyketide
RT synthase nonribosomal peptide synthetase requires coexpression with an
RT enoyl reductase.";
RL ChemBioChem 9:585-594(2008).
RN [3]
RP FUNCTION, AND PATHWAY.
RX PubMed=20575135; DOI=10.1002/cbic.201000259;
RA Heneghan M.N., Yakasai A.A., Halo L.M., Song Z., Bailey A.M., Simpson T.J.,
RA Cox R.J., Lazarus C.M.;
RT "First heterologous reconstruction of a complete functional fungal
RT biosynthetic multigene cluster.";
RL ChemBioChem 11:1508-1512(2010).
RN [4]
RP FUNCTION, INDUCTION, AND PATHWAY.
RX PubMed=34903054; DOI=10.1128/mbio.03279-21;
RA Chen B., Sun Y., Li S., Yin Y., Wang C.;
RT "Inductive production of the iron-chelating 2-pyridones benefits the
RT producing fungus to compete for diverse niches.";
RL MBio 12:e0327921-e0327921(2021).
CC -!- FUNCTION: Trans-enoyl reductase; part of the gene cluster that mediates
CC the biosynthesis of tenellin-type 2-pyridones, iron-chelating compounds
CC involved in iron stress tolerance, competition with the natural
CC competitor fungus Metarhizium robertsii and insect hosts infection
CC (PubMed:17216664, PubMed:18266306, PubMed:20575135, PubMed:34903054).
CC TenC collaborates with the hybrid PKS-NRPS synthetase tenS to catalyze
CC the assembly of the polyketide-amino acid backbone, since tenS lacks a
CC designated enoylreductase (ER) domain (PubMed:18266306,
CC PubMed:34903054). Upon formation of the polyketide backbone on the
CC thiotemplate of tenS, the triketide is transferred to the NRPS module
CC and linked to tyrosine to produce the pyrrolidine-2-dione
CC intermediates, including pretellinin A, 11-hydropretellenin A, 12-
CC hydropretellenin A, 13-hydropretellenin A, 14-hydropretellenin A, 12-
CC oxopretellenin A and prototellinin D (PubMed:18266306,
CC PubMed:34903054). The pathway begins with the assembly of the
CC polyketide-amino acid backbone by the hybrid PKS-NRPS tenS with the
CC help of the enoyl reductase tenC. These enzymes catalyze the synthesis
CC of the pyrrolidine-2-dione intermediates pretellinin A, 11-
CC hydropretellenin A, 12-hydropretellenin A, 13-hydropretellenin A, 14-
CC hydropretellenin A, 12-oxopretellenin A and prototellinin D. The
CC cytochrome P450 monooxygenase tenA then catalyzes an oxidative ring
CC expansion of pretenellin A and 14-hydropretellenin A to form the 2-
CC pyridone core, leading to pretenellin B and pyridovericin,
CC respectively. The cytochrome P450 monooxygenase tenB is then required
CC for the selective N-hydroxylation of the 2-pyridone nitrogen of yield
CC tellinin and 15-hydroxytellenin (15-HT), respectively. The UDP-
CC glucosyltransferase GT1 and the methyltransferase MT1, located outside
CC the tenS gene cluster, contribute to the stepwise glycosylation and
CC methylation of 15-HT to obtain the glycoside pyridovericin-N-O-(4-O-
CC methyl-beta-D-glucopyranoside) (PMGP). Additional related compounds
CC such as 1-O-methyl-15-HT, (8Z)-1-O-methyl-15-HT, and O-methyltenellin A
CC are also produced but the enzymes involved in their biosynthesis have
CC still to be determined (PubMed:34903054). {ECO:0000269|PubMed:17216664,
CC ECO:0000269|PubMed:18266306, ECO:0000269|PubMed:20575135,
CC ECO:0000269|PubMed:34903054}.
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000269|PubMed:17216664, ECO:0000269|PubMed:18266306,
CC ECO:0000269|PubMed:20575135, ECO:0000269|PubMed:34903054}.
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q9Y7D0}.
CC -!- INDUCTION: Expression is positively regulated by the cluster-specific
CC transcription factor tenR and is induced during cocultures with the
CC natural competitor fungus Metarhizium robertsii.
CC {ECO:0000269|PubMed:34903054}.
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. {ECO:0000305}.
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DR EMBL; AM409327; CAL69596.1; -; Genomic_DNA.
DR AlphaFoldDB; A0JJU0; -.
DR SMR; A0JJU0; -.
DR STRING; 176275.XP_008600656.1; -.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
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 Pfam; PF00107; ADH_zinc_N; 1.
DR SMART; SM00829; PKS_ER; 1.
DR SUPFAM; SSF50129; SSF50129; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 2: Evidence at transcript level;
KW NADP; Nucleotide-binding; Oxidoreductase.
FT CHAIN 1..388
FT /note="Trans-enoyl reductase tenC"
FT /id="PRO_0000438446"
FT BINDING 51..54
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9Y7D0"
FT BINDING 142..149
FT /ligand="substrate"
FT /evidence="ECO:0000255"
FT BINDING 219..222
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9Y7D0"
FT BINDING 237
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9Y7D0"
FT BINDING 284..285
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9Y7D0"
FT BINDING 304..308
FT /ligand="substrate"
FT /evidence="ECO:0000255"
FT BINDING 373..374
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9Y7D0"
SQ SEQUENCE 388 AA; 41318 MW; 422564D8E6F2A466 CRC64;
MAAISSPPLT QKALKVASPD TLHLVTDAPL PTLGQDDSVL IRVVCVAINP VDGKSAEMSP
TPGATSGTDF AGIVVALHGD AKSRTETADT IKTGDRVMGF VFGNNPHVLG NGAFAEYVTL
PRRFLWRVPD HMSLEAAASL PVGVASVGMA LHYLRISMSS LLKAVSRSIA APSASQPHDG
AFDSDANVFI LVYGGGTSTG AIAIQILKAA GFHPITCCSS ESASRAKRLG AVATFDYQSA
TCGRDIRDYT NDSLTLAIDC LSESASMAIC YEAMGSAGGR YVSLDPFPVR GCVRRSIVPD
WICSFTQFGQ SIPWAPPYNL DERPDDHRLA EEWYHLAQKL LDAELIEAPT LEIRSGGLLH
VPEGVAAVKL GQIKRRKLVY HISEEALP
