ID   QNN2_EMEVA              Reviewed;         513 AA.
AC   A0A1Y1C7S2;
DT   02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT   30-AUG-2017, sequence version 1.
DT   03-AUG-2022, entry version 9.
DE   RecName: Full=Quiannulatic acid synthase {ECO:0000303|PubMed:27447198};
DE            EC=1.-.-.- {ECO:0000269|PubMed:27447198};
DE   AltName: Full=Cytochrome P450 monooxygenase Qnn-P450 {ECO:0000303|PubMed:27447198};
DE   AltName: Full=Quiannulatic acid biosynthesis cluster protein Qnn-P450 {ECO:0000303|PubMed:27447198};
GN   Name=Qnn-P450 {ECO:0000303|PubMed:27447198};
OS   Emericella variicolor (Aspergillus stellatus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1549217;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND PATHWAY.
RC   STRAIN=ATCC 12069 / CBS 136.55 / IMI 60316 / NBRC 32302;
RX   PubMed=27447198; DOI=10.1021/jacs.6b05799;
RA   Okada M., Matsuda Y., Mitsuhashi T., Hoshino S., Mori T., Nakagawa K.,
RA   Quan Z., Qin B., Zhang H., Hayashi F., Kawaide H., Abe I.;
RT   "Genome-based Discovery of an unprecedented cyclization mode in fungal
RT   sesterterpenoid biosynthesis.";
RL   J. Am. Chem. Soc. 138:10011-10018(2016).
CC   -!- FUNCTION: Cytochrome P450 monooxygenase; part of the gene cluster that
CC       mediates the biosynthesis of the pentacyclic sesterterpene quiannulatic
CC       acid (PubMed:27447198). The first step of the pathway is performed by
CC       the sesterterpene synthase (QS) that possesses both prenyl transferase
CC       and terpene cyclase activity, converting isopentenyl diphosphate and
CC       dimethylallyl diphosphate into geranylfarnesyl diphosphate (GFPP) and
CC       further converting GFPP into quiannulatene via an unprecedented
CC       cyclization mode which involves three rounds of hydride shifts and two
CC       successive C-C bond migrations to construct the 5-6-5-5-5 fused ring
CC       (PubMed:27447198). The cytochrome P450 monooxygenase Qnn-P450 then
CC       oxidizes quiannulatene at C-19 in 3 successive reactions to afford
CC       quiannulatic acid (PubMed:27447198). {ECO:0000269|PubMed:27447198}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3 O2 + quiannulatene + 3 reduced [NADPH--hemoprotein
CC         reductase] = 4 H(+) + 4 H2O + 3 oxidized [NADPH--hemoprotein
CC         reductase] + quiannulatate; Xref=Rhea:RHEA:66868, Rhea:RHEA-
CC         COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618,
CC         ChEBI:CHEBI:58210, ChEBI:CHEBI:167518, ChEBI:CHEBI:167519;
CC         Evidence={ECO:0000269|PubMed:27447198};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66869;
CC         Evidence={ECO:0000269|PubMed:27447198};
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000250|UniProtKB:P04798};
CC   -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC       {ECO:0000269|PubMed:27447198}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC       protein {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; LC155210; BAX76656.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y1C7S2; -.
DR   UniPathway; UPA00213; -.
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:0016114; P:terpenoid biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 1.10.630.10; -; 1.
DR   InterPro; IPR001128; Cyt_P450.
DR   InterPro; IPR036396; Cyt_P450_sf.
DR   Pfam; PF00067; p450; 1.
DR   SUPFAM; SSF48264; SSF48264; 1.
PE   3: Inferred from homology;
KW   Glycoprotein; Heme; Iron; Membrane; Metal-binding; Monooxygenase;
KW   Oxidoreductase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..513
FT                   /note="Quiannulatic acid synthase"
FT                   /id="PRO_0000452690"
FT   TRANSMEM        14..34
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         477
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"
FT   CARBOHYD        308
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   513 AA;  58675 MW;  858002B0085B2513 CRC64;
     MDAFKGAMSK TLEVFTFCNI ILALASLVVA QCVYQIIYYR FFHPLRHYPG PFWASVTRLW
     GAYHFIKGDK LDLEWQAIKQ YGPIIRTSPT MLLVADSTLM PAIYHRRDTK ARFYLSEMFE
     TSGSLVIRDP AKHAAHRRLI SATYSMSNIK RMEPLLDKHI LHFLEKLDSE YAQNAKPMDF
     STWAAYLSYD TVTDLGFRNP LGFVDSASDV GGLIYQFRLG MLLFATSGYL YPLFRWLTTT
     WLKKWLIIRP EQALGFGVIM KRANEVLEER KRALTEGRIA KAVKGDASYD FLQAFMDTRT
     PEGEYLDNKT IRAEVFVILG AGADGFSSLS SAFIAEVLSR PAVYGRVMAE IKAAAIAGEF
     SQPVPLFTEI TKNLPFFLAC MQEIFRLHPT GATQLPREIT PNDPELVLSG HKVPVGIEVT
     CNPWIINRDY NIYGDGAEVF NPDRWLGDPE KIKFYEKHSL TWGHGARFLM YFEVSICEET
     PETPKLESEI YGPVLGWKNV WLDLHKRRSW EQQ