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AUSE_PENBI
ID   AUSE_PENBI              Reviewed;         301 AA.
AC   A0A0F7TZD6;
DT   29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT   22-JUL-2015, sequence version 1.
DT   03-AUG-2022, entry version 15.
DE   RecName: Full=Multifunctional dioxygenase ausE {ECO:0000303|PubMed:29076725};
DE            EC=1.14.11.- {ECO:0000305|PubMed:29076725};
DE   AltName: Full=Austinoid biosynthesis clusters protein E {ECO:0000303|PubMed:29076725};
GN   Name=ausE {ECO:0000303|PubMed:29076725}; ORFNames=PMG11_09847;
OS   Penicillium brasilianum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=104259;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MG11;
RX   PubMed=26337871; DOI=10.1128/genomea.00724-15;
RA   Horn F., Linde J., Mattern D.J., Walther G., Guthke R., Brakhage A.A.,
RA   Valiante V.;
RT   "Draft genome sequence of the fungus Penicillium brasilianum MG11.";
RL   Genome Announc. 3:0-0(2015).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
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   [3]
RP   FUNCTION.
RX   PubMed=29076725; DOI=10.1021/acschembio.7b00814;
RA   Mattern D.J., Valiante V., Horn F., Petzke L., Brakhage A.A.;
RT   "Rewiring of the austinoid biosynthetic pathway in filamentous fungi.";
RL   ACS Chem. Biol. 12:2927-2933(2017).
CC   -!- FUNCTION: Multifunctional dioxygenase; part of the gene cluster A that
CC       mediates the biosynthesis of the fungal meroterpenoid
CC       acetoxydehydroaustin (PubMed:29076725). The first step of the pathway
CC       is the synthesis of 3,5-dimethylorsellinic acid by the polyketide
CC       synthase ausA (By similarity). 3,5-dimethylorsellinic acid is then
CC       prenylated by the polyprenyl transferase ausN (By similarity). Further
CC       epoxidation by the FAD-dependent monooxygenase ausM and cyclization by
CC       the probable terpene cyclase ausL lead to the formation of
CC       protoaustinoid A (By similarity). Protoaustinoid A is then oxidized to
CC       spiro-lactone preaustinoid A3 by the combined action of the FAD-binding
CC       monooxygenases ausB and ausC, and the dioxygenase ausE (By similarity).
CC       Acid-catalyzed keto-rearrangement and ring contraction of the
CC       tetraketide portion of preaustinoid A3 by ausJ lead to the formation of
CC       preaustinoid A4 (By similarity). The aldo-keto reductase ausK, with the
CC       help of ausH, is involved in the next step by transforming preaustinoid
CC       A4 into isoaustinone which is in turn hydroxylated by the P450
CC       monooxygenase ausI to form austinolide (By similarity). The cytochrome
CC       P450 monooxygenase ausG then modifies austinolide to austinol (By
CC       similarity). Austinol is further acetylated to austin by the O-
CC       acetyltransferase ausP, which spontaneously changes to dehydroaustin
CC       (PubMed:29076725). The cytochrome P450 monooxygenase then converts
CC       dehydroaustin is into 7-dehydrodehydroaustin (PubMed:29076725). The
CC       hydroxylation catalyzed by ausR permits the second O-acetyltransferase
CC       ausQ to add an additional acetyl group to the molecule, leading to the
CC       formation of acetoxydehydroaustin (PubMed:29076725). Due to genetic
CC       rearrangements of the clusters and the subsequent loss of some enzymes,
CC       the end product of the Penicillium brasilianum austinoid biosynthesis
CC       clusters is acetoxydehydroaustin (PubMed:29076725).
CC       {ECO:0000250|UniProtKB:Q5AR34, ECO:0000269|PubMed:29076725}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxoglutarate + O2 + preaustinoid A1 = CO2 + H2O +
CC         preaustinoid A2 + succinate; Xref=Rhea:RHEA:65132, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810,
CC         ChEBI:CHEBI:30031, ChEBI:CHEBI:69026, ChEBI:CHEBI:156343;
CC         Evidence={ECO:0000250|UniProtKB:Q5AR34};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65133;
CC         Evidence={ECO:0000250|UniProtKB:Q5AR34};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxoglutarate + O2 + preaustinoid A2 = CO2 + H2O +
CC         preaustinoid A3 + succinate; Xref=Rhea:RHEA:65156, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810,
CC         ChEBI:CHEBI:30031, ChEBI:CHEBI:156343, ChEBI:CHEBI:156346;
CC         Evidence={ECO:0000250|UniProtKB:Q5AR34};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65157;
CC         Evidence={ECO:0000250|UniProtKB:Q5AR34};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxoglutarate + berkeleyone A + O2 = CO2 + H2O + preaustinoid
CC         A + succinate; Xref=Rhea:RHEA:65144, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810,
CC         ChEBI:CHEBI:30031, ChEBI:CHEBI:69023, ChEBI:CHEBI:69024;
CC         Evidence={ECO:0000250|UniProtKB:Q5AR34};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65145;
CC         Evidence={ECO:0000250|UniProtKB:Q5AR34};
CC   -!- COFACTOR:
CC       Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC         Evidence={ECO:0000250|UniProtKB:Q5AR34};
CC   -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC       {ECO:0000305|PubMed:29076725}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q5AR34}.
CC   -!- MISCELLANEOUS: In A.calidoustus, the austinoid gene cluster lies on a
CC       contiguous DNA region, while clusters from E.nidulans and P.brasilianum
CC       are split in their respective genomes. Genetic rearrangements provoked
CC       variability among the clusters and E.nidulans produces the least number
CC       of austionoid derivatives with the end products austinol and
CC       dehydroaustinol, while P.brasilianum can produce until
CC       acetoxydehydroaustin, and A.calidoustus produces the highest number of
CC       identified derivatives. {ECO:0000305|PubMed:29076725}.
CC   -!- SIMILARITY: Belongs to the PhyH family. {ECO:0000305}.
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DR   EMBL; CDHK01000010; CEJ61311.1; -; Genomic_DNA.
DR   SMR; A0A0F7TZD6; -.
DR   EnsemblFungi; CEJ61311; CEJ61311; PMG11_09847.
DR   OrthoDB; 623398at2759; -.
DR   UniPathway; UPA00213; -.
DR   Proteomes; UP000042958; Unassembled WGS sequence.
DR   GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016114; P:terpenoid biosynthetic process; IEA:UniProtKB-UniPathway.
DR   InterPro; IPR008775; Phytyl_CoA_dOase.
DR   Pfam; PF05721; PhyH; 1.
PE   1: Evidence at protein level;
KW   Dioxygenase; Iron; Metal-binding; Oxidoreductase; Reference proteome.
FT   CHAIN           1..301
FT                   /note="Multifunctional dioxygenase ausE"
FT                   /id="PRO_0000453853"
FT   BINDING         72
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q5AR34"
FT   BINDING         127
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q5AR34"
FT   BINDING         130
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250|UniProtKB:Q5AR34"
FT   BINDING         132
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250|UniProtKB:Q5AR34"
FT   BINDING         167
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q5AR34"
FT   BINDING         214
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250|UniProtKB:Q5AR34"
FT   BINDING         226
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q5AR34"
FT   SITE            232
FT                   /note="Important for reaction specificity"
FT                   /evidence="ECO:0000250|UniProtKB:Q5AR34"
SQ   SEQUENCE   301 AA;  33594 MW;  CC553D13F9C5F916 CRC64;
     MAPMNPPRLQ RFPATASADQ IFAAFKEDGC VVIEGFIPPD QVARFSQEVN PAMEKITVEV
     TNDGNSNDRT KRFSKCAIAS PTFRNEIIES DLMHELCDRI FSNPGEGMGY HFNDTMVIEV
     QPGAPAQRLH RDQELYPWWN SMGPAGPECI MNFFCAVTPF TEENGATRLA PGSHLWPEFT
     QINERDCPQF GKIETAPAIM QPGDCYLMSG KVVHGAGHNT TTTDQRRALA LSIIRRELRP
     VQAFSLSVPM KLAREMSERS QTMFGFRSAV QHCDGDMVHF WGNDGKDIAH HLGLEAPSVH
     I
 
 
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