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AUSI_ASPCI
ID   AUSI_ASPCI              Reviewed;         517 AA.
AC   A0A0U5CJM3;
DT   29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT   16-MAR-2016, sequence version 1.
DT   03-AUG-2022, entry version 25.
DE   RecName: Full=Cytochrome P450 monooxygenase ausI {ECO:0000303|PubMed:28233494};
DE            EC=1.-.-.- {ECO:0000305|PubMed:28233494};
DE   AltName: Full=Austinoid biosynthesis cluster protein I {ECO:0000303|PubMed:28233494};
GN   Name=ausI {ECO:0000303|PubMed:29076725}; ORFNames=ASPCAL14363;
OS   Aspergillus calidoustus.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Nidulantes.
OX   NCBI_TaxID=454130;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SF006504;
RX   PubMed=26966204; DOI=10.1128/genomea.00102-16;
RA   Horn F., Linde J., Mattern D.J., Walther G., Guthke R., Scherlach K.,
RA   Martin K., Brakhage A.A., Petzke L., Valiante V.;
RT   "Draft genome sequences of fungus Aspergillus calidoustus.";
RL   Genome Announc. 4:0-0(2016).
RN   [2]
RP   FUNCTION, AND PATHWAY.
RX   PubMed=28233494; DOI=10.1021/acschembio.7b00003;
RA   Valiante V., Mattern D.J., Schueffler A., Horn F., Walther G.,
RA   Scherlach K., Petzke L., Dickhaut J., Guthke R., Hertweck C., Nett M.,
RA   Thines E., Brakhage A.A.;
RT   "Discovery of an Extended Austinoid Biosynthetic Pathway in Aspergillus
RT   calidoustus.";
RL   ACS Chem. Biol. 12:1227-1234(2017).
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: Cytochrome P450 monooxygenase; part of the gene cluster that
CC       mediates the biosynthesis of calidodehydroaustin, a fungal
CC       meroterpenoid (PubMed:28233494, PubMed:29076725). The first step of the
CC       pathway is the synthesis of 3,5-dimethylorsellinic acid by the
CC       polyketide synthase ausA (PubMed:28233494). 3,5-dimethylorsellinic acid
CC       is then prenylated by the polyprenyl transferase ausN
CC       (PubMed:28233494). Further epoxidation by the FAD-dependent
CC       monooxygenase ausM and cyclization by the probable terpene cyclase ausL
CC       lead to the formation of protoaustinoid A (By similarity).
CC       Protoaustinoid A is then oxidized to spiro-lactone preaustinoid A3 by
CC       the combined action of the FAD-binding monooxygenases ausB and ausC,
CC       and the dioxygenase ausE (By similarity). Acid-catalyzed keto-
CC       rearrangement and ring contraction of the tetraketide portion of
CC       preaustinoid A3 by ausJ lead to the formation of preaustinoid A4 (By
CC       similarity). The aldo-keto reductase ausK, with the help of ausH, is
CC       involved in the next step by transforming preaustinoid A4 into
CC       isoaustinone which is in turn hydroxylated by the P450 monooxygenase
CC       ausI to form austinolide (By similarity). The cytochrome P450
CC       monooxygenase ausG modifies austinolide to austinol (By similarity).
CC       Austinol is further acetylated to austin by the O-acetyltransferase
CC       ausP, which spontaneously changes to dehydroaustin (PubMed:28233494).
CC       The cytochrome P450 monooxygenase ausR then converts dehydroaustin is
CC       into 7-dehydrodehydroaustin (PubMed:28233494). The hydroxylation
CC       catalyzed by ausR permits the O-acetyltransferase ausQ to add an
CC       additional acetyl group to the molecule, leading to the formation of
CC       acetoxydehydroaustin (PubMed:28233494). The short chain dehydrogenase
CC       ausT catalyzes the reduction of the double bond present between carbon
CC       atoms 1 and 2 to convert 7-dehydrodehydroaustin into 1,2-dihydro-7-
CC       hydroxydehydroaustin (PubMed:28233494). AusQ catalyzes not only an
CC       acetylation reaction but also the addition of the PKS ausV diketide
CC       product to 1,2-dihydro-7-hydroxydehydroaustin, forming
CC       precalidodehydroaustin (PubMed:28233494). Finally, the iron/alpha-
CC       ketoglutarate-dependent dioxygenase converts precalidodehydroaustin
CC       into calidodehydroaustin (PubMed:28233494).
CC       {ECO:0000250|UniProtKB:Q5AR27, ECO:0000269|PubMed:28233494,
CC       ECO:0000269|PubMed:29076725}.
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000250|UniProtKB:P04798};
CC   -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC       {ECO:0000305|PubMed:28233494}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC       protein {ECO:0000255}.
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 cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; CDMC01000024; CEL11260.1; -; Genomic_DNA.
DR   SMR; A0A0U5CJM3; -.
DR   EnsemblFungi; CEL11260; CEL11260; ASPCAL14363.
DR   OrthoDB; 614788at2759; -.
DR   UniPathway; UPA00213; -.
DR   Proteomes; UP000054771; Unassembled WGS sequence.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR   GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
DR   GO; GO:0016114; P:terpenoid biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 1.10.630.10; -; 1.
DR   InterPro; IPR001128; Cyt_P450.
DR   InterPro; IPR017972; Cyt_P450_CS.
DR   InterPro; IPR002403; Cyt_P450_E_grp-IV.
DR   InterPro; IPR036396; Cyt_P450_sf.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00465; EP450IV.
DR   SUPFAM; SSF48264; SSF48264; 1.
DR   PROSITE; PS00086; CYTOCHROME_P450; 1.
PE   3: Inferred from homology;
KW   Heme; Iron; Membrane; Metal-binding; Monooxygenase; Oxidoreductase;
KW   Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..517
FT                   /note="Cytochrome P450 monooxygenase ausI"
FT                   /id="PRO_0000453839"
FT   TRANSMEM        8..28
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         457
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000250|UniProtKB:P04798"
SQ   SEQUENCE   517 AA;  58326 MW;  F7E8BCE10004D3F3 CRC64;
     MLHETTNLAP LGQPWIAGLV VVSAVLYLLY STQRWRANNI PLLNDAGPFD FLQATAVNRF
     RRDARQLIKS GFDSHRDVFA MRTDVGVELF ASPEYADQFR NHPSLKVFPF TAKMHHGHLP
     GFELCRSQPV EDRIFIESVR VQLAQSLGKL IQPLASDIGQ AISDRWPSES GWEEIALGSV
     VERTISQGTS SVYCLDKAWP EFVVKMEMAL GMASAALSAW PVMLRRIVAK FLPECLELYR
     TMDAGRELMS RDMRRRTALQ ASTGEAPLNF FEWFKEASHG EEHDELILNL RIAFASMHGL
     CDHLVKILLR LSEDPQLVDD LRKEVIQVYK THGWSKTALY HLKLMDSAFK EVQRVDPILF
     GMPTPISLVQ THSNYETAVG RVAVDDVTLK DGLVIRKGQS IRISGHTMWD EDKYPDAAHF
     DAYRFYKLRQ APGQENTAQF TSPTSDHLGF GYGGRACPGR FFAAAVLKIS LCHLLMKYDI
     KPADGETGPH VWEFAAAINA NMAAKVLVRR RQPEIQL
 
 
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