AGN2_PAEDI
ID AGN2_PAEDI Reviewed; 164 AA.
AC A0A411PQQ5;
DT 26-FEB-2020, integrated into UniProtKB/Swiss-Prot.
DT 08-MAY-2019, sequence version 1.
DT 25-MAY-2022, entry version 9.
DE RecName: Full=Anthrone oxygenase AgnL2 {ECO:0000303|PubMed:30746079};
DE EC=1.10.3.- {ECO:0000305|PubMed:30746079};
DE AltName: Full=Agnestins biosynthesis cluster protein L2 {ECO:0000303|PubMed:30746079};
GN Name=AgnL2 {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: Anthrone oxygenase; part of the gene cluster that mediates
CC the 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 -!- CATALYTIC ACTIVITY:
CC Reaction=emodin anthrone + O2 = emodin + H(+) + H2O;
CC Xref=Rhea:RHEA:64268, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:77659, ChEBI:CHEBI:150013;
CC Evidence={ECO:0000305|PubMed:30746079};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64269;
CC Evidence={ECO:0000305|PubMed:30746079};
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000305|PubMed:30746079}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the anthrone oxygenase family. {ECO:0000305}.
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DR EMBL; MH898872; QBG38886.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A411PQQ5; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
PE 3: Inferred from homology;
KW Membrane; Monooxygenase; Oxidoreductase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..164
FT /note="Anthrone oxygenase AgnL2"
FT /id="PRO_0000449016"
FT TRANSMEM 11..31
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 48..70
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 85..105
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 164 AA; 17992 MW; 29E802C80D85D7C7 CRC64;
MSTTSAQATA VVTGSFLSGA MISLSLMAVP VLLDTTTEPT QLFFQWRRMY HYGHQVLPTM
AVATTLLYAY TASKRRRAQK PSWAVFALAG TITVSMIPFT WLCMVPTNNV LFGLEAATRL
GEPSGMGIEE AQALLVKWSW LHFTRSLMPL MGAILGSLGE TVWN