TENB_BEAB2
ID TENB_BEAB2 Reviewed; 544 AA.
AC J4UJ10;
DT 25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT 25-MAY-2022, sequence version 2.
DT 03-AUG-2022, entry version 40.
DE RecName: Full=Cytochrome P450 monooxygenase tenB {ECO:0000303|PubMed:34903054};
DE EC=1.-.-.- {ECO:0000269|PubMed:19067514};
DE AltName: Full=Tenellin biosynthesis protein B {ECO:0000303|PubMed:34903054};
GN Name=tenB {ECO:0000303|PubMed:34903054}; ORFNames=BBA_07336;
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, 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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EJP63692.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JH725173; EJP63692.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_008600655.1; XM_008602433.1.
DR EnsemblFungi; EJP63692; EJP63692; BBA_07336.
DR GeneID; 19890348; -.
DR HOGENOM; CLU_022195_9_0_1; -.
DR InParanoid; J4UJ10; -.
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; 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 Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..544
FT /note="Cytochrome P450 monooxygenase tenB"
FT /id="PRO_0000455687"
FT TRANSMEM 13..33
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 440..467
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 486
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 544 AA; 61625 MW; DE749DE3B6E3B625 CRC64;
MALSEVLSMV AQLGYYEKVT GILGVVSIIL LFWKLNHEPF YPALPLAGEP PQRRWFSLSN
RLRYYNDCAA LFDEAYHTAY AKKGKAVLVP SMGVHTAMIM PESAMNWAMS QPDDSLSIKK
AFSELNQTKY SLGHSRYWED PWQLDLVKAH LSSILQNLIP QLNEELAAAF SKHLGTDAEN
WKEIELEVIM RRVIAQATSR FIVGLPLCRD DGYLDLSYKV ILGMVTTIWA TLPFPDLIRA
VTGPLASWQT RRNISRIQEH LEPLYQERIS ILESRDGQKS DPGPQDLFMM MLRFAQKKRP
DEYANLGIMT RRVCAANFVA MHQSTVSVTN LILNIIGSDA EFNTIATLRD EITQVMRGTD
AKGCWTKDTF TRMRKCDSVA REAMRLNFPL GTRGSMRTVL KDGLESPEGI KLQKGTTISW
LASCAQVDAD RFDNPQKFDP FRFSRASKDD DDDDDDDGRS TSSHTKDAFV TTSPQYLPFG
HGKHACPGRF MVDLMFKIIL AQLLTHYDLG WPEDYQGKQP PSVWQGELSE PPPGARILVK
RRKV
