ID   AGN5_PAEDI              Reviewed;         161 AA.
AC   A0A411PQL6;
DT   26-FEB-2020, integrated into UniProtKB/Swiss-Prot.
DT   08-MAY-2019, sequence version 1.
DT   25-MAY-2022, entry version 8.
DE   RecName: Full=Monooxygenase AgnL5 {ECO:0000303|PubMed:30746079};
DE            EC=1.-.-.- {ECO:0000305|PubMed:30746079};
DE   AltName: Full=Agnestins biosynthesis cluster protein L5 {ECO:0000303|PubMed:30746079};
GN   Name=AgnL5 {ECO:0000303|PubMed:30746079};
OS   Paecilomyces divaricatus (Penicillium divaricatum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Thermoascaceae; Paecilomyces.
OX   NCBI_TaxID=644132;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND PATHWAY.
RC   STRAIN=K5013;
RX   PubMed=30746079; DOI=10.1039/c8sc03778g;
RA   Szwalbe A.J., Williams K., Song Z., de Mattos-Shipley K., Vincent J.L.,
RA   Bailey A.M., Willis C.L., Cox R.J., Simpson T.J.;
RT   "Characterisation of the biosynthetic pathway to agnestins A and B reveals
RT   the reductive route to chrysophanol in fungi.";
RL   Chem. Sci. 10:233-238(2019).
CC   -!- FUNCTION: Monooxygenase; part of the gene cluster that mediates the
CC       biosynthesis of agnestins, dihydroxy-xanthone metabolites
CC       (PubMed:30746079). The pathway begins with the assembly and cyclization
CC       of atrochrysone thioester by the non-reducing polyketide synthase
CC       Agnpks1 (PubMed:30746079). The atrochrysone carboxyl ACP thioesterase
CC       AgnL7 then breaks the thioester bond and releases the atrochrysone
CC       carboxylic acid as the first enzyme-free intermediate
CC       (PubMed:30746079). The decarboxylase AgnL1 then catalyzes the concerted
CC       decarboxylation-elimination required to convert atochrysone carboxylic
CC       acid into emodin anthrone, which is further oxidized to emodin by the
CC       anthrone oxygenase AgnL2 (PubMed:30746079). Emodin then undergoes
CC       reduction catalyzed by the oxidoreductase AgnL4 to yield the
CC       dihydroquinone tautomer which is the substrate for reduction by the
CC       short chain dehydrogenase AgnL6 reduction to produce hydroxyketone,
CC       followed by AgnL8 dehydration and likely spontaneous autoxidation to
CC       chrysophanol (PubMed:30746079). Baeyer-Villiger oxidation by the
CC       oxidase AgnL3 leads to monodictyphenone via cleavage of the C-10/C-10a
CC       bond of chrysophanol (PubMed:30746079). Alternative cleavage at the C-
CC       4a/C-10 bond of chrysophanol leads also to the formation some cephalone
CC       F (PubMed:30746079). Further conversion to agnestins A and B, requires
CC       reduction to dihydro-monodictyphenone, oxidation to agnestin C probably
CC       via an epoxide, and rearrangement to either agnestin A or agnestin B
CC       directly, although agnestin A or agnestin B can also interconvert
CC       (PubMed:30746079). Within the cluster, AgnR1 is the only unassigned
CC       oxidoreductase present which could be involved in this conversion.
CC       However, AgnR1 seems not to be involved in this step, and thus genes
CC       involved in the proposed oxidation/reduction may be located elsewhere
CC       on the genome (PubMed:30746079). Further agnestin A derivatives are
CC       probably formed by spontaneous decarboxylations, dehydrations and
CC       methanolysis reactions (PubMed:30746079).
CC       {ECO:0000269|PubMed:30746079}.
CC   -!- PATHWAY: Secondary metabolite biosynthesis.
CC       {ECO:0000305|PubMed:30746079}.
CC   -!- SIMILARITY: Belongs to the avfA family. {ECO:0000305}.
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DR   EMBL; MH898872; QBG38883.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A411PQL6; -.
DR   SMR; A0A411PQL6; -.
DR   GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR   InterPro; IPR032710; NTF2-like_dom_sf.
DR   SUPFAM; SSF54427; SSF54427; 1.
PE   3: Inferred from homology;
KW   Monooxygenase; Oxidoreductase.
FT   CHAIN           1..161
FT                   /note="Monooxygenase AgnL5"
FT                   /id="PRO_0000449014"
SQ   SEQUENCE   161 AA;  17425 MW;  3AA760AB853F7201 CRC64;
     MPAPAEVQAA TLQRFLAAWQ KWDAQEWLDG FADDFTQITL PLSLGIPSRS RAEVEQVLPA
     LVATVKSYQL TIRTVVHDPE RNKAAVYALS TGTLPWGPWE LEYSVFITFS EAGDQVAVLE
     EMMDSAFLQE FGPKFGQYLQ ANGGPRAVAA GVGAGGATAV H