ID   ATR14_STAC4             Reviewed;         446 AA.
AC   A0A084R1J2;
DT   22-NOV-2017, integrated into UniProtKB/Swiss-Prot.
DT   29-OCT-2014, sequence version 1.
DT   03-AUG-2022, entry version 18.
DE   RecName: Full=Cytochrome P450 monooxygenase ATR14 {ECO:0000303|PubMed:25015739};
DE            EC=1.-.-.- {ECO:0000305|PubMed:25015739};
DE   AltName: Full=Core atranone cluster (CAC) protein 14 {ECO:0000303|PubMed:25015739};
GN   Name=ATR14 {ECO:0000303|PubMed:25015739}; ORFNames=S40285_03338;
OS   Stachybotrys chlorohalonata (strain IBT 40285).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Stachybotryaceae; Stachybotrys.
OX   NCBI_TaxID=1283841;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], IDENTIFICATION, AND
RP   FUNCTION.
RC   STRAIN=IBT 40285;
RX   PubMed=25015739; DOI=10.1186/1471-2164-15-590;
RA   Semeiks J., Borek D., Otwinowski Z., Grishin N.V.;
RT   "Comparative genome sequencing reveals chemotype-specific gene clusters in
RT   the toxigenic black mold Stachybotrys.";
RL   BMC Genomics 15:590-590(2014).
CC   -!- FUNCTION: Cytochrome P450 monooxygenase; part of the core atranone
CC       cluster (CAC) which products are predicted to catalyze most or all
CC       steps of mycotoxin atranone synthesis, starting from geranylgeranyl
CC       pyrophosphate (GGPP) (PubMed:25015739). The initial cyclization of GGPP
CC       to dolabellane is probably performed by the terpene cyclase ATR13
CC       (PubMed:25015739). The Baeyer-Villiger oxidation near the end of the
CC       atranone synthesis, which converts atranones D and E to atranones F and
CC       G is predicted to be catalyzed by the monooxygenase ATR8
CC       (PubMed:25015739). Of the CAC's other predicted gene products, the
CC       reducing PKS ATR6 might synthesize a polyketide chain
CC       (PubMed:25015739). This polyketide is probably transferred onto the
CC       atranone backbone by the polyketide transferase ATR5 (By similarity).
CC       Other predicted CAC products include 4 oxygenases (ATR2, ATR3, ATR4,
CC       and ATR14), 3 short-chain reductases (ATR7, ATR9, and ATR10), and a
CC       methyltransferase (ATR12) (PubMed:25015739). These may all be involved
CC       in the various steps of atranone biosynthesis, although their specific
CC       roles must await experimental determination (PubMed:25015739).
CC       {ECO:0000250|UniProtKB:Q4WAY4, ECO:0000305|PubMed:25015739}.
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000250|UniProtKB:P04798};
CC   -!- PATHWAY: Mycotoxin biosynthesis. {ECO:0000305|PubMed:25015739}.
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; KL659308; KFA70077.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A084R1J2; -.
DR   EnsemblFungi; KFA70077; KFA70077; S40285_03338.
DR   HOGENOM; CLU_001570_14_11_1; -.
DR   OMA; RSHCEDS; -.
DR   OrthoDB; 1247045at2759; -.
DR   Proteomes; UP000028524; Unassembled WGS sequence.
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   Gene3D; 1.10.630.10; -; 2.
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   3: Inferred from homology;
KW   Heme; Iron; Metal-binding; Monooxygenase; Oxidoreductase;
KW   Reference proteome.
FT   CHAIN           1..446
FT                   /note="Cytochrome P450 monooxygenase ATR14"
FT                   /id="PRO_0000442387"
FT   REGION          403..446
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        406..430
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         442
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"
SQ   SEQUENCE   446 AA;  49993 MW;  407C68875AF0A09B CRC64;
     MNVADIAMDL FRGAKGETIS IFAIAKVTVT GVSRGLSKLV FGVVDQANLV NLGQYVVYSV
     VSMIYNITLH PLASFPGPVF WGASRWPSIW RLFKGRLVHD VHALHGQYGH VVRIAPNELA
     FSSAQAWKDI YGHKRGNNSM EEMPKFHKFY SGISKTPSIV SEPTRDGHRF IRRILSPAFS
     DKNLRELEPI VQGYISQFID QLRSHCEDST GSKVPLDLVS WYNSATFDIV GDLTFGRPFG
     SLEQGEEDPF IKDINHFAAV GGAMLIFTSH FPGRGILRFL ASLGKVFQNG QEKHVTKMEE
     SLVDRMKNKS SRPDIIDGLV KEKDGFQIDY DRVLENAAAI TMAGSETTAS QLSGLTALLL
     QNPNCLERLK KEVRSAFKSD KDITSTSSLV GVWQYSANHS PRNFTYPDEF RPDRWLDDRD
     QKEYEHDHGD AMQPFSVGPR DCPSQK