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PRHF_PENBI
ID   PRHF_PENBI              Reviewed;         476 AA.
AC   A0A1E1FFL6;
DT   26-FEB-2020, integrated into UniProtKB/Swiss-Prot.
DT   18-JAN-2017, sequence version 1.
DT   03-AUG-2022, entry version 15.
DE   RecName: Full=FAD-dependent monooxygenase prhF {ECO:0000303|PubMed:27602587};
DE            EC=1.-.-.- {ECO:0000305|PubMed:27602587};
DE   AltName: Full=Paraherquonin biosynthesis cluster protein F {ECO:0000303|PubMed:27602587};
GN   Name=prhF {ECO:0000303|PubMed:27602587};
OS   Penicillium brasilianum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=104259;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND PATHWAY.
RC   STRAIN=ATCC 22354 / NBRC 6234 / CBS 338.59 / FRR 3454 / IMI 68220;
RX   PubMed=27602587; DOI=10.1021/jacs.6b08424;
RA   Matsuda Y., Iwabuchi T., Fujimoto T., Awakawa T., Nakashima Y., Mori T.,
RA   Zhang H., Hayashi F., Abe I.;
RT   "Discovery of key dioxygenases that diverged the paraherquonin and
RT   acetoxydehydroaustin pathways in Penicillium brasilianum.";
RL   J. Am. Chem. Soc. 138:12671-12677(2016).
RN   [2]
RP   FUNCTION.
RX   PubMed=28759016; DOI=10.1038/nchembio.2443;
RA   Mori T., Iwabuchi T., Hoshino S., Wang H., Matsuda Y., Abe I.;
RT   "Molecular basis for the unusual ring reconstruction in fungal
RT   meroterpenoid biogenesis.";
RL   Nat. Chem. Biol. 13:1066-1073(2017).
RN   [3]
RP   FUNCTION.
RX   PubMed=29317628; DOI=10.1038/s41467-017-02371-w;
RA   Nakashima Y., Mori T., Nakamura H., Awakawa T., Hoshino S., Senda M.,
RA   Senda T., Abe I.;
RT   "Structure function and engineering of multifunctional non-heme iron
RT   dependent oxygenases in fungal meroterpenoid biosynthesis.";
RL   Nat. Commun. 9:104-104(2018).
CC   -!- FUNCTION: FAD-dependent monooxygenase; part of the gene cluster that
CC       mediates the biosynthesis of paraherquonin, a meroterpenoid with a
CC       unique, highly congested hexacyclic molecular architecture
CC       (PubMed:27602587). The first step of the pathway is the synthesis of
CC       3,5-dimethylorsellinic acid (DMOA) by the polyketide synthase prhL (By
CC       similarity). Synthesis of DMOA is followed by farnesylation by the
CC       prenyltransferase prhE, methylesterification by the methyl-transferase
CC       prhM, epoxidation of the prenyl chain by the flavin-dependent
CC       monooxygenase prhF, and cyclization of the farnesyl moiety by the
CC       terpene cyclase prhH, to yield the tetracyclic intermediate,
CC       protoaustinoid A (By similarity). The short chain dehydrogenase prhI
CC       then oxidizes the C-3 alcohol group of the terpene cyclase product to
CC       transform protoaustinoid A into protoaustinoid B (PubMed:27602587). The
CC       FAD-binding monooxygenase prhJ catalyzes the oxidation of
CC       protoaustinoid B into preaustinoid A which is further oxidized into
CC       preaustinoid A1 by FAD-binding monooxygenase phrK (PubMed:27602587).
CC       Finally, prhA leads to berkeleydione via the berkeleyone B intermediate
CC       (PubMed:27602587, PubMed:29317628). PrhA is a multifunctional
CC       dioxygenase that first desaturates at C5-C6 to form berkeleyone B,
CC       followed by rearrangement of the A/B-ring to form the cycloheptadiene
CC       moiety in berkeleydione (PubMed:27602587, PubMed:29317628).
CC       Berkeleydione serves as the key intermediate for the biosynthesis of
CC       paraherquonin as well as many other meroterpenoids (Probable). The
CC       cytochrome P450 monooxygenases prhB, prhD, and prhN, as well as the
CC       isomerase prhC, are probably involved in the late stage of
CC       paraherquonin biosynthesis, after the production of berkeleydione
CC       (Probable). Especially prhC might be a multifunctional enzyme that
CC       catalyzes the D-ring expansion via intramolecular methoxy
CC       rearrangement, as well as the hydrolysis of the expanded D-ring
CC       (Probable). {ECO:0000250|UniProtKB:Q5ATJ7, ECO:0000269|PubMed:27602587,
CC       ECO:0000269|PubMed:29317628, ECO:0000305|PubMed:27602587,
CC       ECO:0000305|PubMed:28759016, ECO:0000305|PubMed:29317628}.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000305};
CC   -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC       {ECO:0000305|PubMed:27602587}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC       protein {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the paxM FAD-dependent monooxygenase family.
CC       {ECO:0000305}.
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DR   EMBL; LC127182; BAV69307.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1E1FFL6; -.
DR   SMR; A0A1E1FFL6; -.
DR   UniPathway; UPA00213; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR   GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
DR   GO; GO:0016114; P:terpenoid biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.50.50.60; -; 1.
DR   InterPro; IPR002938; FAD-bd.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   Pfam; PF01494; FAD_binding_3; 2.
DR   SUPFAM; SSF51905; SSF51905; 1.
PE   3: Inferred from homology;
KW   FAD; Flavoprotein; Glycoprotein; Membrane; Monooxygenase; Oxidoreductase;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..476
FT                   /note="FAD-dependent monooxygenase prhF"
FT                   /id="PRO_0000449171"
FT   TRANSMEM        447..467
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         42..43
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:A6T923"
FT   BINDING         137
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:A6T923"
FT   BINDING         314
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:A6T923"
FT   BINDING         324..328
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:A6T923"
FT   CARBOHYD        343
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        471
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   476 AA;  53220 MW;  F6E09B49CC2E6B9B CRC64;
     MSQATVEEKS KLRVIIVGGS VAGLTLAHCL AKANIDHIVL EKRAEISPQE GAFIGIWPNG
     ARILDQLGLY DDFESLMPPV HRMNVRFPDG FTFSSFLPRT IQERFGYPII SIDRQKVLET
     LYERYPHKSN VLVNKKVMNV RLLGKGVSVV TEDGSAYNGD IVVGADGIHS RIRSEMWRLA
     DENHPGLITS EDKQAFTVEY ACVFGISEQL PSLRAGEHIN SYSNGLCVIT FHGEKGRIFW
     FLLVKLPKKT TYPNTPRFSA GDAASVCNNF ATFRVSEDVC VSDLWMHKLC ASMTALEEGI
     LERWHYDRIV LLGDSVHKMT PNIGQGANTA LEDASVLASL LNNLSKLSTE DGTSAYAMTK
     LLDEFQSTRY ERAKNTHDKS RFGARLHTRD DMIKTLIGRY VFPYAGPRVL ERSVKSLATA
     HSVEYLPFSK RLGPAWGEYS SRTKSTLGST PIQMLTLLLP CLFYFMYSKL NLSLSS
 
 
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