ID   BTCB_NEOBT              Reviewed;         528 AA.
AC   A0A2Z6FZ19;
DT   29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT   10-OCT-2018, sequence version 1.
DT   03-AUG-2022, entry version 11.
DE   RecName: Full=Cytochrome P450 monooxygenase btcB {ECO:0000303|Ref.2};
DE            EC=1.-.-.- {ECO:0000269|Ref.2};
DE   AltName: Full=Betaestacins biosynthesis cluster protein B {ECO:0000303|Ref.2};
GN   Name=btcB {ECO:0000303|PubMed:29185768};
OS   Neocamarosporium betae (Beet black rot fungus) (Pleospora betae).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae;
OC   Neocamarosporium.
OX   NCBI_TaxID=1979465;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=PS-13;
RX   PubMed=29185768; DOI=10.1021/acs.orglett.7b03418;
RA   Narita K., Sato H., Minami A., Kudo K., Gao L., Liu C., Ozaki T.,
RA   Kodama M., Lei X., Taniguchi T., Monde K., Yamazaki M., Uchiyama M.,
RA   Oikawa H.;
RT   "Focused genome mining of structurally related sesterterpenes: enzymatic
RT   formation of enantiomeric and diastereomeric products.";
RL   Org. Lett. 19:6696-6699(2017).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX   DOI=10.1016/j.tetlet.2018.02.022;
RA   Gao L., Narita K., Ozaki T., Kamukara N., Gan P., Minami A., Liu C.,
RA   Lei X., Shirasu K., Oikawa H.;
RT   "Identification of novel sesterterpenes by genome mining of phytopathogenic
RT   fungi Phoma and Colletotrichum sp.";
RL   Tetrahedron Lett. 59:1136-1139(2018).
CC   -!- FUNCTION: Cytochrome P450 monooxygenase; part of the gene cluster that
CC       mediates the biosynthesis of betaestacins (PubMed:29185768, Ref.2). The
CC       bifunctional terpene synthase btcA converts isopentenyl diphosphate
CC       (IPP) and dimethylallyl diphosphate (DMAPP) into the sesterterpene
CC       betaestacin I (PubMed:29185768, Ref.2). The C-terminal
CC       prenyltransferase (PT) domain of btcA catalyzes formation of GFPP,
CC       whereas the N-terminal terpene cyclase (TC) domain catalyzes the
CC       cyclization of GFPP into betaestacin I (PubMed:29185768, Ref.2). The
CC       cytochrome P450 monooxygenase btcB is then responsible for the six-step
CC       oxidation of betaestacin I to yield betaestacin II (Ref.2). The roles
CC       of the cytochrome P450 monooxygenase btcC and the alpha-ketoglutarate-
CC       dependent dioxygenase btcD have not been identified yet (Probable).
CC       {ECO:0000269|PubMed:29185768, ECO:0000269|Ref.2, ECO:0000305|Ref.2}.
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|Ref.2}.
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; LC274619; BBE36501.1; -; Genomic_DNA.
DR   SMR; A0A2Z6FZ19; -.
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   PRINTS; PR00385; P450.
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..528
FT                   /note="Cytochrome P450 monooxygenase btcB"
FT                   /id="PRO_0000453709"
FT   TRANSMEM        37..57
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         472
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        204
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        381
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        395
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   528 AA;  59169 MW;  0BE4BDAF972D5DED CRC64;
     MDAMNGSDVQ SDGLPNGNTL QLAYHVMPRL VQDMGPSLLL IFGPLVLVSS CIYYLFFHPL
     SKIPGPKLAA ISPVWMMKSL YGKKLNRDIK ALHDRYGDVV RVGPNTVSFA TVGALSSVHH
     EKAGGDDGTF TKEGTIEWLL GLMTWPAQNI LTKTDVKGHA RLRKAVQPAF SAKELRKQEP
     IEQEWITKFN RLLDAAAVDN TEVNITEHMS HLVWDMLSDL SFGEPLARSQ LVKFNRLKWL
     ACAMSPMLEV MQSILTFPIA GAFTRWIVTS FPQVFQLPRD ILPTGTLRTT LERADRGHDF
     LSAIVGAQEK GIVLSQDELQ SNSAMLVMVG QDATVTCLSS TLYFLLRDPQ HMANLQDEVR
     GQFKSEDEIN GLAIARLPLL NGSINEAMRL LSPANGTGTH RLSNGGFVEG IYLPAGITVA
     VDQYTIQRSP KYWRDPETYR PERWASVGEP ESEFENDVHS AYRPFLLGPR ACLGRELALQ
     IVRLVLARLV FSYDLRMVNR DFVWERDCDS SYLWLGHKVV VKVQKRES