ID   DESC_ASPDE              Reviewed;         536 AA.
AC   A0A0N9HKQ7;
DT   25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT   20-JAN-2016, sequence version 1.
DT   03-AUG-2022, entry version 18.
DE   RecName: Full=Bicoumarin synthase desC {ECO:0000303|PubMed:26389790};
DE            EC=1.14.-.- {ECO:0000269|PubMed:26389790};
DE   AltName: Full=Cytochrome P450 monooxygenase desC {ECO:0000303|PubMed:26389790};
DE   AltName: Full=Desertorin biosynthesis cluster protein C {ECO:0000303|PubMed:26389790};
GN   Name=desC {ECO:0000303|PubMed:26389790};
GN   ORFNames=EMD_0001 {ECO:0000303|PubMed:26389790};
OS   Aspergillus desertorum (Emericella desertorum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1810909;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP   PATHWAY.
RC   STRAIN=CBS 653.73 / NBRC 30840;
RX   PubMed=26389790; DOI=10.1021/jacs.5b06776;
RA   Mazzaferro L.S., Huettel W., Fries A., Mueller M.;
RT   "Cytochrome P450-catalyzed regio- and stereoselective phenol coupling of
RT   fungal natural products.";
RL   J. Am. Chem. Soc. 137:12289-12295(2015).
CC   -!- FUNCTION: Non-reducing polyketide synthase; part of the gene cluster
CC       that mediates the biosynthesis of the bicoumarin desertorin
CC       (PubMed:26389790). The non-reducing polyketide synthase desS first
CC       catalyzes the formation of the pentaketidic 4,7-dihydroxy-5-
CC       methylcoumarin from acetyl coenzyme A and 4 malonyl coenzyme A
CC       molecules (PubMed:26389790). Further O-methylation by desB leads to the
CC       formation of 7-demethylsiderin (PubMed:26389790). Then, an oxidative
CC       phenol coupling catalyzed by the cytochrome P450 monooxygenase desC
CC       forms the 6,8'-dimer M-desertorin A via dimerization the monomeric
CC       precursor, 7-demethylsiderin (PubMed:26389790). M-desertorin A is
CC       further converted to M-desertorin C (PubMed:26389790).
CC       {ECO:0000269|PubMed:26389790}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 7-demethylsiderin + NADPH + O2 = desertorin A + 2 H2O +
CC         NADP(+); Xref=Rhea:RHEA:62804, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:145991,
CC         ChEBI:CHEBI:145993; Evidence={ECO:0000269|PubMed:26389790};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62805;
CC         Evidence={ECO:0000269|PubMed:26389790};
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000250|UniProtKB:P04798};
CC   -!- PATHWAY: Secondary metabolite biosynthesis.
CC       {ECO:0000269|PubMed:26389790}.
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; KT583602; ALG03236.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0N9HKQ7; -.
DR   SMR; A0A0N9HKQ7; -.
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:0008152; P:metabolic process; IEA:UniProt.
DR   Gene3D; 1.10.630.10; -; 1.
DR   InterPro; IPR001128; Cyt_P450.
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.
PE   1: Evidence at protein level;
KW   Glycoprotein; Heme; Iron; Membrane; Metal-binding; Monooxygenase;
KW   Oxidoreductase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..536
FT                   /note="Bicoumarin synthase desC"
FT                   /id="PRO_0000442169"
FT   TRANSMEM        12..32
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         480
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        149
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        371
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   536 AA;  60207 MW;  13229B09566105C9 CRC64;
     MGALSEIFTA GYVALAGITG FFLVFLGFLV VISDYIDGWR SRRALGDIPI VDEGSNLSPI
     LRWNSQPYDA EAEFTRAYYK YSKNGKPFAA RIQHGGYAIV LPPSACRKVR SIGHEQLSFL
     DALAEFADLS LHMDVTSRRV IEATHACNNE TTIKNFQERL ALECGKHLAP VFDPPQEQES
     TELKTLKSVF AAISAVATAL ILGPDCPEAL VSEVTAGATA YNEVMIQCRI LRAQYPKILK
     PLVWRFSRTA RELRAILSRL KARLVPEIKR RIAYLEAHST SENQAESAGS FSLLDILIQT
     SFKNRHLPST PVENDKWADL LCQQALLYHF KLSRAPGTSV TFMLYRVMNH PEYATMLRDE
     MIAALKPSGG NWTADILQRA PKLESFNKET FRMHDISNFV GLRVAMRPVD LRSVSPPLHL
     KPGTMIMTPS RTVHYDAEHY VDPLTFNGLR FYDATSNTCT PRVFTTSPTY LPFSHGTGSC
     PARNFATQIA RMLFIRLLMG YEFELANEEM PAYGLMDGTA YFPNPEVRMR VRVRGK