ID   STTB_ASPTE              Reviewed;         530 AA.
AC   P9WEV3;
DT   12-AUG-2020, integrated into UniProtKB/Swiss-Prot.
DT   12-AUG-2020, sequence version 1.
DT   03-AUG-2022, entry version 7.
DE   RecName: Full=Cytochrome P450 monooxygenase sttB {ECO:0000303|PubMed:28604695};
DE            EC=1.-.-.- {ECO:0000305|PubMed:28604695};
DE   AltName: Full=Aspterpenacid biosynthesis cluster protein sttA {ECO:0000303|PubMed:34085529};
DE   AltName: Full=Ophiobolin family sesterterpenoid biosynthesis cluster protein B {ECO:0000303|PubMed:28604695};
GN   Name=sttB {ECO:0000303|PubMed:28604695};
OS   Aspergillus terreus.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=33178;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, DISRUPTION PHENOTYPE, AND
RP   PATHWAY.
RC   STRAIN=ATCC 20542 / MF4845;
RX   PubMed=28604695; DOI=10.1038/nchembio.2408;
RA   Clevenger K.D., Bok J.W., Ye R., Miley G.P., Verdan M.H., Velk T., Chen C.,
RA   Yang K., Robey M.T., Gao P., Lamprecht M., Thomas P.M., Islam M.N.,
RA   Palmer J.M., Wu C.C., Keller N.P., Kelleher N.L.;
RT   "A scalable platform to identify fungal secondary metabolites and their
RT   gene clusters.";
RL   Nat. Chem. Biol. 13:895-901(2017).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX   PubMed=34085529; DOI=10.1021/acs.orglett.1c01361;
RA   Jiang L., Zhang X., Sato Y., Zhu G., Minami A., Zhang W., Ozaki T., Zhu B.,
RA   Wang Z., Wang X., Lv K., Zhang J., Wang Y., Gao S., Liu C., Hsiang T.,
RA   Zhang L., Oikawa H., Liu X.;
RT   "Genome-based discovery of enantiomeric pentacyclic sesterterpenes
RT   catalyzed by fungal bifunctional terpene synthases.";
RL   Org. Lett. 23:4645-4650(2021).
CC   -!- FUNCTION: Cytochrome P450 monooxygenase; part of the gene cluster that
CC       mediates the biosynthesis of aspterpenacids (PubMed:28604695,
CC       PubMed:34085529). Performs the C22-oxidative modification of the
CC       terpene synthase sttA product preaspterpenacid I to produce
CC       preaspterpenacid II (PubMed:34085529). It has still to be determined
CC       how preaspterpenacid II is further modified to produce aspterpenacids
CC       (Probable). {ECO:0000269|PubMed:28604695, ECO:0000269|PubMed:34085529,
CC       ECO:0000305|PubMed:34085529}.
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:28604695, ECO:0000269|PubMed:34085529}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC       protein {ECO:0000255}.
CC   -!- DISRUPTION PHENOTYPE: Abolishes the production of the ophiobolin family
CC       sesterterpenoid. {ECO:0000269|PubMed:28604695}.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; KX449366; AQM58280.1; -; Genomic_DNA.
DR   AlphaFoldDB; P9WEV3; -.
DR   SMR; P9WEV3; -.
DR   VEuPathDB; FungiDB:ATEG_03567; -.
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; 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..530
FT                   /note="Cytochrome P450 monooxygenase sttB"
FT                   /id="PRO_0000450608"
FT   TRANSMEM        24..44
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         475
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        5
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        230
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   530 AA;  60066 MW;  655A82B304DEE209 CRC64;
     MSISNMTSTV WPDLQVPAVE YNHLPILTVA LLTVIASAVY INVSSAQDPY KVSSIPTVKR
     PRVLDAYRSG VWWRIFVPRL VPYIEEGYHK YNKNDQPFRI WLGGFQTYAY VLPERYLEKI
     KNMPESEASF AAMANKYFHT GLPTGEVNNL VLQVASKLVN GNLATIKTLM QGEVQKALAR
     EIGSPRQWTK INAWQVARKT TEAPGLRVVF GEELANDKTF VTGVSEFVSN ITVYAFTLRY
     INLGPLRDFI LYLVHWRHRR SLPAVLTPLN NVITERKKVR SNRHISDDEE SFDCIQWALD
     QPVSDDCKTA EAIARRLVVI SLGTIDTVAG VLVKQLTHLA SHPECHEAIR AEIRECLAED
     DKGWTLKSSA RMKKLESFIQ ESLRMSSGAI SLSGMRIVTG PGFRLDDNTI LPRDSFIAIP
     TRNILYDPEV FPEPEKFDPF RFYKIKEDEK NAGPLSNRRD IRASWLAFGY GRQACPGRFY
     AINAMKAILG EILLKYDIRL AEKQAPSIDI DLDPMLAPAR STDLEFRVRA