TENA_BEABA
ID TENA_BEABA Reviewed; 508 AA.
AC A0JJT8;
DT 30-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 1.
DT 03-AUG-2022, entry version 42.
DE RecName: Full=Cytochrome P450 monooxygenase tenA {ECO:0000303|PubMed:17216664};
DE EC=1.-.-.- {ECO:0000269|PubMed:19067514};
DE AltName: Full=Tenellin biosynthesis protein A {ECO:0000303|PubMed:17216664};
GN Name=tenA {ECO:0000303|PubMed:20575135};
GN Synonyms=ORF1 {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, DISRUPTION PHENOTYPE, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=19067514; DOI=10.1021/ja807052c;
RA Halo L.M., Heneghan M.N., Yakasai A.A., Song Z., Williams K., Bailey A.M.,
RA Cox R.J., Lazarus C.M., Simpson T.J.;
RT "Late stage oxidations during the biosynthesis of the 2-pyridone tenellin
RT in the entomopathogenic fungus Beauveria bassiana.";
RL J. Am. Chem. Soc. 130:17988-17996(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, DISRUPTION PHENOTYPE, 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: Cytochrome P450 monooxygenase; part of the gene cluster that
CC mediates the biosynthesis of tenellin-type 2-pyridones, iron-chelating
CC compounds involved in iron stress tolerance, competition with the
CC natural competitor fungus Metarhizium robertsii and insect hosts
CC infection (PubMed:17216664, PubMed:19067514, PubMed:20575135,
CC PubMed:34903054). TenA catalyzes an oxidative ring expansion of
CC pretenellin A and 14-hydropretellenin A to form the 2-pyridone core,
CC leading to the production of pretenellin B and pyridovericin,
CC respectively (PubMed:19067514, PubMed:34903054). The pathway begins
CC with the assembly of the polyketide-amino acid backbone by the hybrid
CC PKS-NRPS tenS with the help of the enoyl reductase tenC. These enzymes
CC catalyze the synthesis of the pyrrolidine-2-dione intermediates
CC pretellinin A, 11-hydropretellenin A, 12-hydropretellenin A, 13-
CC hydropretellenin A, 14-hydropretellenin A, 12-oxopretellenin A and
CC prototellinin D. The cytochrome P450 monooxygenase tenA then catalyzes
CC an oxidative ring expansion of pretenellin A and 14-hydropretellenin A
CC to form the 2-pyridone core, leading to pretenellin B and
CC pyridovericin, respectively. The cytochrome P450 monooxygenase tenB is
CC then required for the selective N-hydroxylation of the 2-pyridone
CC nitrogen of yield tellinin and 15-hydroxytellenin (15-HT),
CC respectively. The UDP-glucosyltransferase GT1 and the methyltransferase
CC MT1, located outside the tenS gene cluster, contribute to the stepwise
CC glycosylation and methylation of 15-HT to obtain the glycoside
CC pyridovericin-N-O-(4-O-methyl-beta-D-glucopyranoside) (PMGP).
CC Additional related compounds such as 1-O-methyl-15-HT, (8Z)-1-O-methyl-
CC 15-HT, and O-methyltenellin A are also produced but the enzymes
CC involved in their biosynthesis have still to be determined
CC (PubMed:34903054). {ECO:0000269|PubMed:17216664,
CC ECO:0000269|PubMed:19067514, ECO:0000269|PubMed:20575135,
CC ECO:0000269|PubMed:34903054}.
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000250|UniProtKB:P04798};
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000269|PubMed:17216664, ECO:0000269|PubMed:19067514,
CC ECO:0000269|PubMed:20575135, ECO:0000269|PubMed:34903054}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC protein {ECO:0000255}.
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 -!- DISRUPTION PHENOTYPE: Fails to produce tenellin, and leads to the
CC accumulation of 11-hydropretellenin A, 12-hydropretellenin A, 13-
CC hydropretellenin A, 14-hydropretellenin A, 12-oxopretellenin A and
CC prototellinin D. {ECO:0000269|PubMed:19067514,
CC ECO:0000269|PubMed:34903054}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; AM409327; CAL69594.1; -; Genomic_DNA.
DR AlphaFoldDB; A0JJT8; -.
DR SMR; A0JJT8; -.
DR KEGG; ag:CAL69594; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0016712; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen; IEA:InterPro.
DR Gene3D; 1.10.630.10; -; 1.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR002974; Cyt_P450_E_CYP52.
DR InterPro; IPR036396; Cyt_P450_sf.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR01239; EP450IICYP52.
DR SUPFAM; SSF48264; SSF48264; 1.
PE 1: Evidence at protein level;
KW Iron; Membrane; Metal-binding; Monooxygenase; Oxidoreductase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..508
FT /note="Cytochrome P450 monooxygenase tenA"
FT /id="PRO_0000438451"
FT TRANSMEM 8..24
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 456
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:P04798"
SQ SEQUENCE 508 AA; 58450 MW; FBAA33729C62BA58 CRC64;
MLPLLDSVSL PYLILSACLS VILLRRFLAH DKGGSKSIAQ GCLPEPRLRQ WDPIFGFGIV
ISQARALRGH RYLEWLRDLH ASMPHTKTFS ANYGGYRWIF SIEPEILKAV YATNLQNFGV
EPIRQHPPGF QPFAHKGVST SDGDDWSFSR TLIKPFFERS VYISTDRIKP FADKFMTLLP
DDGETFDIQP LLQRWFLDIT SEFIFGKSQD SMTHADRAEV TWAMADVLRG GRQRAQTHRI
LWAFNWDWWF EAVEKVHGFL NPYIRSTLKE LEERQQRIKD GLPVDEERTD LLWSMATMLP
DEEELRSQVC LIFVPNNDTT SMFIGHCLYF LARNSNAWKR LRDEVDAVGD APITFEMLRN
MKYLNGILNE THRLIPNNVT QVRAALSDVV LPLGGGPNGK APLDVRKGDI VSVTKTVMYR
DPEQWGPDAN EYRPERWDGM RGGWHFLPYG GGPRRCPAQM MVQNESAYML FRLAQKYSTI
VARDPEPFRA RMRIGPSSMH GVKIAFYK
