ID   BUAF_ASPBU              Reviewed;         412 AA.
AC   A0A411KZU9;
DT   11-DEC-2019, integrated into UniProtKB/Swiss-Prot.
DT   08-MAY-2019, sequence version 1.
DT   25-MAY-2022, entry version 7.
DE   RecName: Full=Burnettramic acids biosynthesis cluster protein E {ECO:0000303|PubMed:30735051};
GN   Name=buaE {ECO:0000303|PubMed:30735051};
OS   Aspergillus burnettii.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=2508778;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND PATHWAY.
RC   STRAIN=FRR 5400;
RX   PubMed=30735051; DOI=10.1021/acs.orglett.8b04042;
RA   Li H., Gilchrist C.L.M., Lacey H.J., Crombie A., Vuong D., Pitt J.I.,
RA   Lacey E., Chooi Y.H., Piggott A.M.;
RT   "Discovery and Heterologous Biosynthesis of the Burnettramic Acids: Rare
RT   PKS-NRPS-Derived Bolaamphiphilic Pyrrolizidinediones from an Australian
RT   Fungus, Aspergillus burnettii.";
RL   Org. Lett. 21:1287-1291(2019).
CC   -!- FUNCTION: Part of the gene cluster that mediates the biosynthesis of
CC       burnettramic acids, an unusual class of bolaamphiphilic
CC       pyrrolizidinediones that display potent antibacterial, antifungal, and
CC       cytotoxic activities (PubMed:30735051). The first step of the
CC       biosynthesis of burnettramic acids is the hydroxylation of proline by
CC       the proline hydroxylase buaE to generate 4-hydroxyproline
CC       (PubMed:30735051). The PKS-NRPS buaA and trans-enoyl reductase buaC
CC       construct the highly reduced polyketide chain, and the condensation (C)
CC       domain of buaA then catalyzes the amide bond formation with the
CC       activated 4-hydroxyproline (PubMed:30735051). This is followed by the R
CC       domain releasing the nascent polyketide-peptide directly via a
CC       Dieckmann condensation to afford a tetramic acid fused to the
CC       hydroxyproline, generating the bicyclic pyrrolidinedione moiety
CC       (PubMed:30735051). The cytochrome P450 monooxygenases buaD and buaG are
CC       likely responsible for the multiple hydroxylations on the polyketide
CC       chain and its terminus, although in the heterologous context, buaD does
CC       not appear to be required. Therefore, while buaG may be a
CC       multifunctional cytochrome P450 monooxygenase, it cannot be ruled out
CC       that the two secondary alcohols on the polyketide chain could have an
CC       acetate origin (PubMed:30735051). Finally, the glycosyltransferase buaB
CC       transfers beta-D-mannose to the aglycone burnettramic acid A to form
CC       burnettramic acid A (PubMed:30735051). Burnettramic acid B is a minor
CC       cis-pyrrolizidine epimer of burnettramic acid A and it is likely that
CC       small amounts of it form naturally in acidic environments
CC       (PubMed:30735051). The role of the uncharacterized protein buaF in the
CC       biosynthesis of burnettramic acids has still to be determined
CC       (Probable). {ECO:0000269|PubMed:30735051, ECO:0000305|PubMed:30735051}.
CC   -!- PATHWAY: Mycotoxin biosynthesis. {ECO:0000269|PubMed:30735051}.
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DR   EMBL; MK425157; QBE85646.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A411KZU9; -.
DR   GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
PE   4: Predicted;
KW   Antibiotic biosynthesis.
FT   CHAIN           1..412
FT                   /note="Burnettramic acids biosynthesis cluster protein E"
FT                   /id="PRO_0000448734"
FT   REGION          1..66
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          308..342
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          386..412
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        14..39
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        40..54
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        327..342
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   412 AA;  45296 MW;  0F7E6A6BF13D740D CRC64;
     MAIASSIGLV AEAIHRHKTP ERPIESENDI ARYPAEDEQW ALDELQDELC QEEPSDSEDQ
     PKKKIRNPAK LADDFLKRYP PPPSGSAPAG RLPLPVIIPQ RRPGVRVRGF VRAYAPDLQA
     CGIDQDTFMD FLVTMTRAGR APQWMGAANL TAAAAFALPG HAIGCGVGFA IQVVNAIAME
     MRGRVQANGF LQKLNQGFFQ PRGLYCLVLS FDNTHEEAMT DESLATAIAT TTDPKTGVRK
     YTDKLRSHSG TTGPSEFPES APLVFPVLDW LETNANAEQA EKLGRYKKFR KFVADYYDRR
     AQAEYAARNP TSPLAAPPRR GFTSKLADPN DDTNKSPISL ATGGLVPYNT TWRETRNSEG
     RRPPRKIADK VLYMIIVNMP SDDDMSRAES IMATEATTEP SVQSDDAEAA KG