ID   ATR2_STAC4              Reviewed;         513 AA.
AC   A0A084R1M6;
DT   22-NOV-2017, integrated into UniProtKB/Swiss-Prot.
DT   29-OCT-2014, sequence version 1.
DT   25-MAY-2022, entry version 22.
DE   RecName: Full=Cytochrome P450 monooxygenase ATR2 {ECO:0000303|PubMed:25015739};
DE            EC=1.-.-.- {ECO:0000305|PubMed:25015739};
DE   AltName: Full=Core atranone cluster (CAC) protein 2 {ECO:0000303|PubMed:25015739};
DE   Flags: Precursor;
GN   Name=ATR2 {ECO:0000303|PubMed:25015739}; ORFNames=S40285_03327;
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; KFA70111.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A084R1M6; -.
DR   SMR; A0A084R1M6; -.
DR   EnsemblFungi; KFA70111; KFA70111; S40285_03327.
DR   HOGENOM; CLU_022195_0_2_1; -.
DR   OMA; RKERYEP; -.
DR   OrthoDB; 188186at4751; -.
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; -; 1.
DR   InterPro; IPR001128; Cyt_P450.
DR   InterPro; IPR017972; Cyt_P450_CS.
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.
DR   PROSITE; PS00086; CYTOCHROME_P450; 1.
PE   3: Inferred from homology;
KW   Glycoprotein; Heme; Iron; Metal-binding; Monooxygenase; Oxidoreductase;
KW   Reference proteome; Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..513
FT                   /note="Cytochrome P450 monooxygenase ATR2"
FT                   /id="PRO_0000442384"
FT   CARBOHYD        37
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        139
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        173
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   513 AA;  57679 MW;  50253EB97E905D6C CRC64;
     MAVISLFRII VDKWHVVLAC SACLGALLFQ ALRRQSNSTK DVPFIGMELG SAEKRRKAYM
     TDARSLFRDG YQQFKDRVFG ITTTSENLVV VVPPRFLDEL GRLPDEVLSA SMAVADISQD
     KYTKMEITDP IISHAVRGNL TMSLSRLNDA ILEELRKALS LLLPTCDEWT SVNISEKLQR
     IVAVISGRVF VGPELCGSDA YLDAAIHIAH EASAAVQSIS TLPPWKRPFL SARLPELRAL
     RERQDKVHSV LRPVLEKRIQ MNEEDRPDDM LTWIISSQKK HGERSIETMA KVQTALHLAA
     IGTTSEMATN AFYNLAAMPE LVPELREEIR TVLEEHDGVV STKSLQAMKK LDSFLKETAR
     LYPPFLAAFE RKVLRTFTLS NGQVIPAGAL IKVPSQAIMT DPALFPDPDR FDAFRFYDLQ
     QQKNILKDGS VSVGASVNQF VNSNKNSLVF GYGRHACPGR FLAADELKMI LVYFLQAYEI
     RLEEGESRRY RNLEFAAFSI PDPTKTIQMK KLQ