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TENA_BEAB2
ID   TENA_BEAB2              Reviewed;         529 AA.
AC   J5JKC1;
DT   25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2012, sequence version 1.
DT   03-AUG-2022, entry version 30.
DE   RecName: Full=Cytochrome P450 monooxygenase tenA {ECO:0000303|PubMed:34903054};
DE            EC=1.-.-.- {ECO:0000269|PubMed:19067514, ECO:0000269|PubMed:34903054};
DE   AltName: Full=Tenellin biosynthesis protein A {ECO:0000303|PubMed:34903054};
GN   Name=tenA {ECO:0000303|PubMed:34903054}; ORFNames=BBA_07335;
OS   Beauveria bassiana (strain ARSEF 2860) (White muscardine disease fungus)
OS   (Tritirachium shiotae).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Cordycipitaceae; Beauveria.
OX   NCBI_TaxID=655819;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ARSEF 2860;
RX   PubMed=22761991; DOI=10.1038/srep00483;
RA   Xiao G., Ying S.-H., Zheng P., Wang Z.-L., Zhang S., Xie X.-Q., Shang Y.,
RA   St Leger R.J., Zhao G.-P., Wang C., Feng M.-G.;
RT   "Genomic perspectives on the evolution of fungal entomopathogenicity in
RT   Beauveria bassiana.";
RL   Sci. Rep. 2:483-483(2012).
RN   [2]
RP   FUNCTION, AND PATHWAY.
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   [3]
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   [4]
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   [5]
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; JH725173; EJP63691.1; -; Genomic_DNA.
DR   RefSeq; XP_008600654.1; XM_008602432.1.
DR   EnsemblFungi; EJP63691; EJP63691; BBA_07335.
DR   GeneID; 19890347; -.
DR   HOGENOM; CLU_001570_27_0_1; -.
DR   InParanoid; J5JKC1; -.
DR   Proteomes; UP000002762; Unassembled WGS sequence.
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:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR   Gene3D; 1.10.630.10; -; 1.
DR   InterPro; IPR001128; Cyt_P450.
DR   InterPro; IPR002401; Cyt_P450_E_grp-I.
DR   InterPro; IPR036396; Cyt_P450_sf.
DR   Pfam; PF00067; p450; 2.
DR   PRINTS; PR00463; EP450I.
DR   SUPFAM; SSF48264; SSF48264; 1.
PE   1: Evidence at protein level;
KW   Iron; Membrane; Metal-binding; Monooxygenase; Oxidoreductase;
KW   Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..529
FT                   /note="Cytochrome P450 monooxygenase tenA"
FT                   /id="PRO_0000455688"
FT   TRANSMEM        8..24
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         477
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   529 AA;  60680 MW;  F9E65B60BA2535D2 CRC64;
     MLSLLDSVSL PYLILSACLS VILLRRFLAH DKGGSKSIAQ GCLPEPRLRQ WDPIFGFGIV
     ISQARALRGH RYLEWLRDLH ASMPHTKTFS ANYGGYRWIF SIEPEILKAV YATNFQNFGV
     EPIRQHPPGF QPFAHKGVST SDGDDWSFSR TLIKPFFERS VYVSTDRIKP FADKFMTLLP
     DDGETFDIQP LLQRWFLDIT SEFIFGRSQD SMTHADRAEV TWAMADVLRG GRQRAQTHRI
     LWAFNWDWWF EAVEKVHGFL NPYIRSTLKE LEERQQRIKD GLPVDEERTD LLWSMATMLP
     DEEELRSQVC LIFVPNNDTT SMFIGHCLYF LARHSNAWKR LRDEVDAVGD APITFEMLRN
     MKYLNGILNE SMKPKPLSSK LTLALTTLCT PAHRLIPNNV TQVRAALSDV VLPLGGGPNG
     KAPLDVRKGD IVSVTKTVMY RDPDQWGPDA NEYRPERWDG MRGGWHFLPY GGGPRRCPAQ
     MMVQNESAYM LFRLAQKYST IVARDPEPFR ARMRIGPSSM HGVKIAFYK
 
 
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