ID   STLP4_EMEVA             Reviewed;         522 AA.
AC   A0A0P0ZEA9;
DT   02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT   20-JAN-2016, sequence version 1.
DT   03-AUG-2022, entry version 17.
DE   RecName: Full=Stellatic acid synthase {ECO:0000303|PubMed:26351860};
DE            EC=1.-.-.- {ECO:0000269|PubMed:26351860};
DE   AltName: Full=Cytochrome P450 monooxygenase Stl-P450 {ECO:0000303|PubMed:26351860};
DE   AltName: Full=Stellatic acid biosynthetis gene clusters protein Stl-P450 {ECO:0000303|PubMed:26351860};
GN   Name=Stl-P450 {ECO:0000303|PubMed:26351860};
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, CATALYTIC ACTIVITY, AND
RP   PATHWAY.
RC   STRAIN=ATCC 12069 / CBS 136.55 / IMI 60316 / NBRC 32302;
RX   PubMed=26351860; DOI=10.1021/acs.orglett.5b02404;
RA   Matsuda Y., Mitsuhashi T., Quan Z., Abe I.;
RT   "Molecular basis for stellatic acid biosynthesis: a genome mining approach
RT   for discovery of sesterterpene synthases.";
RL   Org. Lett. 17:4644-4647(2015).
CC   -!- FUNCTION: Cytochrome P450 monooxygenase; part of the gene cluster that
CC       mediates the biosynthesis of the sesterterpene stellatic acid
CC       (PubMed:26351860). The first step in the pathway is performed by the
CC       stellatatriene synthase that possesses both prenyl transferase and
CC       terpene cyclase activity, converting isopentenyl diphosphate and
CC       dimethylallyl diphosphate into geranylgeranyl diphosphate (GGDP) and
CC       then converting GGDP into stellata-2,6,19-triene (PubMed:26351860). The
CC       cytochrome P450 monooxygenase Stl-P450 then catalyzes three successive
CC       oxidation reactions on the C-20 methyl group to generate the carboxylic
CC       acid of stellatic acid (PubMed:26351860).
CC       {ECO:0000269|PubMed:26351860}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3 O2 + 3 reduced [NADPH--hemoprotein reductase] + stellata-
CC         2,6,19-triene = 4 H(+) + 4 H2O + 3 oxidized [NADPH--hemoprotein
CC         reductase] + stellatate; Xref=Rhea:RHEA:66712, Rhea:RHEA-COMP:11964,
CC         Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210,
CC         ChEBI:CHEBI:138048, ChEBI:CHEBI:167454;
CC         Evidence={ECO:0000269|PubMed:26351860};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66713;
CC         Evidence={ECO:0000269|PubMed:26351860};
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:26351860}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC       protein {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; LC073704; BAT32890.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0P0ZEA9; -.
DR   SMR; A0A0P0ZEA9; -.
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; IPR002401; Cyt_P450_E_grp-I.
DR   InterPro; IPR036396; Cyt_P450_sf.
DR   Pfam; PF00067; p450; 2.
DR   PRINTS; PR00463; EP450I.
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..522
FT                   /note="Stellatic acid synthase"
FT                   /id="PRO_0000452515"
FT   TRANSMEM        23..43
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         464
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        267
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        451
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        495
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   522 AA;  59873 MW;  E351489B1B1E6D82 CRC64;
     MEGSINDARR TNYLVLLRTC YEIYGIYEPL LALFAVYSVA VVVYRLYLHP LARFPGPKLA
     AATGWYEFYH DVFRGGQYLY EIESMHRKYG PIIRINPHEL VVNDPDFYNT VFVAANTRRT
     DKWSGLEGIG LRGSLAFTRD HDLHRIRRKR YEPFFSRLSV SRIEPIIVDE AKLLAKQLEA
     SSKTGRVIEL EHVMSAFTGD VITTLCSEKS PDMIRHPEFG KGWHTSLYNF PSCFRAGAFN
     SFLEYSTDHI NTAKREMLSV DKLEQNNKSS VFRYVLSTDM PQAERDTERL AREAALLFGA
     GSVTTTRFFS VTIYYTLRNR QIRDRLSAEL KDVMAGYPST LPTWQELDRL PYLHAIVKEG
     LRYACPFVLS SSLAAWSSLS HKFSSRLSYG VMRHLSRISP DSALHYKQWT IPPGTPVGMS
     SYSLHTDPET FPEPFKFMPE RWLGEYNPKM NRSWVPFTRG SRNCLGMNLA YAQIYWGLAV
     MFRPGGPRLE LYETNESDIR PVLDFLGPLP KSGSRGLRVT VS