TENB_BEABA
ID TENB_BEABA Reviewed; 539 AA.
AC A0JJT9; E2GC97;
DT 30-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 1.
DT 03-AUG-2022, entry version 61.
DE RecName: Full=Cytochrome P450 monooxygenase tenB {ECO:0000303|PubMed:17216664};
DE EC=1.-.-.- {ECO:0000269|PubMed:19067514};
DE AltName: Full=Tenellin biosynthesis protein B {ECO:0000303|PubMed:17216664};
GN Name=tenB {ECO:0000303|PubMed:20575135};
GN Synonyms=ORF2 {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 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=992.05;
RA Heneghan M.N., Yakasai A.A., Bailey A.M., Cox R.J., Simpson T.J.,
RA Lazarus C.M.;
RT "Isolation of the desmethylbassianin gene cluster from the insect
RT pathogenic fungus Beauveria bassiana.";
RL Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases.
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, INDUCTION, DISRUPTION PHENOTYPE, 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). TenB catalyzes the selective N-hydroxylation of the
CC 2-pyridone nitrogen of yield tellinin and 15-hydroxytellenin (15-HT),
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 accumulates
CC pretenellin B (PubMed:19067514). Leads also to the accumulation of
CC pyridovericin (PubMed:34903054). {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; HM243222; ADN43683.1; -; Genomic_DNA.
DR EMBL; AM409327; CAL69595.1; -; Genomic_DNA.
DR AlphaFoldDB; A0JJT9; -.
DR SMR; A0JJT9; -.
DR PRIDE; A0JJT9; -.
DR KEGG; ag:CAL69595; -.
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; IPR017972; Cyt_P450_CS.
DR InterPro; IPR002403; Cyt_P450_E_grp-IV.
DR InterPro; IPR036396; Cyt_P450_sf.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00465; EP450IV.
DR SUPFAM; SSF48264; SSF48264; 1.
DR PROSITE; PS00086; CYTOCHROME_P450; 1.
PE 1: Evidence at protein level;
KW Heme; Iron; Membrane; Metal-binding; Monooxygenase; Oxidoreductase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..539
FT /note="Cytochrome P450 monooxygenase tenB"
FT /id="PRO_0000438452"
FT TRANSMEM 13..33
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 439..460
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 439..458
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 481
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 539 AA; 61065 MW; FDCF0430D15A2C82 CRC64;
MALFQAMSMV AQLGYYEKVA GVLGFLSIAL LFWKLNHKPF YPALPLAGEP PQRRWFSLSN
RLRYYNDCAA LFDEAYHTAY AKKGKAVLVP SMGVHTAMIM PESAMNWAMS QPDDSLSIKK
AFSELNQTKY SLGHGRYWED PWQLDLVKAH LSSILQNLIP QLNEELAAAF SKHLGTDAEN
WKEIELEVIM RRIIAQATSR FIVGLPLCRD DGYLDLSYKV ILGMVTTIWA TLPFPDLIRA
ITGPIASWQT RRNIARIQEY LEPLYQERIS ILESRDGPES DPEPQDLFMM MLRFAQKKRP
DEYANLGIMT RRVCAANFVA MHQSTVSVTN LILNIIGSDA EFNTTATLRD EITQVMRGTD
AKSWTKDTFT RMRKCDSVAR EAMRLNFPLG TRGSMRAVLK DGLESPEGIK LQKGTTISWL
ASCAQVDADR FDNPQKFDPF RFSRASKDDD DDGKSTSSHA KDAFVTTSPQ YLPFGHGKHA
CPGRFMVDLM FKILLAQLLT HYDLGWPEDY QGKQPPSVWQ GELSEPPPGA RILVKRRKV
