ID   BTCD_NEOBT              Reviewed;         339 AA.
AC   A0A2Z6FZX4;
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=Alpha-ketoglutarate-dependent dioxygenase btcD {ECO:0000303|Ref.2};
DE            EC=1.14.11.- {ECO:0000305|Ref.2};
DE   AltName: Full=Betaestacins biosynthesis cluster protein D {ECO:0000303|Ref.2};
GN   Name=btcD {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, 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: Alpha-ketoglutarate-dependent dioxygenase; part of the gene
CC       cluster that mediates the biosynthesis of betaestacins
CC       (PubMed:29185768, Ref.2). The bifunctional terpene synthase btcA
CC       converts isopentenyl diphosphate (IPP) and dimethylallyl diphosphate
CC       (DMAPP) into the sesterterpene betaestacin I (PubMed:29185768, Ref.2).
CC       The C-terminal prenyltransferase (PT) domain of btcA catalyzes
CC       formation of GFPP, whereas the N-terminal terpene cyclase (TC) domain
CC       catalyzes the cyclization of GFPP into betaestacin I (PubMed:29185768,
CC       Ref.2). The cytochrome P450 monooxygenase btcB is then responsible for
CC       the six-step oxidation of betaestacin I to yield betaestacin II
CC       (Ref.2). The roles of the cytochrome P450 monooxygenase btcC and the
CC       alpha-ketoglutarate-dependent dioxygenase btcD have not been identified
CC       yet (Probable). {ECO:0000269|PubMed:29185768, ECO:0000269|Ref.2,
CC       ECO:0000305|Ref.2}.
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC         Evidence={ECO:0000250|UniProtKB:P37610};
CC       Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000250|UniProtKB:P37610};
CC   -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC       {ECO:0000305|Ref.2}.
CC   -!- SIMILARITY: Belongs to the TfdA dioxygenase family. {ECO:0000305}.
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DR   EMBL; LC274619; BBE36499.1; -; Genomic_DNA.
DR   SMR; A0A2Z6FZX4; -.
DR   UniPathway; UPA00213; -.
DR   GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016114; P:terpenoid biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.60.130.10; -; 1.
DR   InterPro; IPR042098; TauD-like_sf.
DR   InterPro; IPR003819; TauD/TfdA-like.
DR   Pfam; PF02668; TauD; 1.
PE   3: Inferred from homology;
KW   Dioxygenase; Iron; Metal-binding; Oxidoreductase.
FT   CHAIN           1..339
FT                   /note="Alpha-ketoglutarate-dependent dioxygenase btcD"
FT                   /id="PRO_0000453707"
FT   REGION          207..230
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         96
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P37610"
FT   BINDING         140
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P37610"
FT   BINDING         142
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P37610"
FT   BINDING         173
FT                   /ligand="2-oxoglutarate"
FT                   /ligand_id="ChEBI:CHEBI:16810"
FT                   /evidence="ECO:0000250|UniProtKB:P37610"
FT   BINDING         302
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P37610"
FT   BINDING         314
FT                   /ligand="2-oxoglutarate"
FT                   /ligand_id="ChEBI:CHEBI:16810"
FT                   /evidence="ECO:0000250|UniProtKB:P37610"
FT   BINDING         318
FT                   /ligand="2-oxoglutarate"
FT                   /ligand_id="ChEBI:CHEBI:16810"
FT                   /evidence="ECO:0000250|UniProtKB:P37610"
FT   BINDING         318
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P37610"
SQ   SEQUENCE   339 AA;  38046 MW;  AC8DFDA475DEAB26 CRC64;
     MALIKEPLKP TGALDEFRSF DVTPIIGTEF PDASLKAWLE DPKADDLLRE LAITVSRRGV
     VFFRRQDGLT EEMQKAIVQK LGVLSGKPAT SSLHRHAHQP DPNADPEILW INSEENKKLL
     AGTPFDPALP ARQSCRGLWH NDISYEPNPS DYALLRITQP PALVVADLPA IDTLWASGYE
     VFDRISRPIQ KFLETLTATF GELRERDGSD PKFQVPRGSP ANVGTNLRPT HPVIRTNPVT
     GWKSVYAVGL HVQTINGLAS DESDGLKKWF TKLIVENHDL QVRFRWNNAN DVAIWDNRCT
     YHTATYDHEG YGIREGYRAC GVGEKPYLDP NSTGRREAR