ID   ATR4_STAC4              Reviewed;         524 AA.
AC   A0A084R1M7;
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 ATR4 {ECO:0000303|PubMed:25015739};
DE            EC=1.-.-.- {ECO:0000305|PubMed:25015739};
DE   AltName: Full=Core atranone cluster (CAC) protein 4 {ECO:0000303|PubMed:25015739};
GN   Name=ATR4 {ECO:0000303|PubMed:25015739}; ORFNames=S40285_03329;
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   -!- 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; KL659308; KFA70112.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A084R1M7; -.
DR   SMR; A0A084R1M7; -.
DR   EnsemblFungi; KFA70112; KFA70112; S40285_03329.
DR   HOGENOM; CLU_022195_0_1_1; -.
DR   OMA; KLIMARM; -.
DR   OrthoDB; 614788at2759; -.
DR   Proteomes; UP000028524; Unassembled WGS sequence.
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   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   3: Inferred from homology;
KW   Glycoprotein; Heme; Iron; Membrane; Metal-binding; Monooxygenase;
KW   Oxidoreductase; Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..524
FT                   /note="Cytochrome P450 monooxygenase ATR4"
FT                   /id="PRO_0000442386"
FT   TRANSMEM        13..36
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        291
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        444
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        454
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   524 AA;  60146 MW;  DDE60A299E842C99 CRC64;
     MRLDLLGPVA TRIITYLDSL TWVGMALPLF SLCWAISYAR GKAYPTVPGA PVYGYNSRFE
     PSFMLKSRTY TGFYDILSNG YKMLKDVPFV IPRHDTNINI LPIKYLDEIR LMPKHILNSH
     LVLISQMTPK WTWLQPAADS DLVTRVLLTK LNPDLQKYVD ITRLELDSAF KSDFPRHDEE
     WTEVDFQPLI RRVLTRISAK IFLGEPACLN EDWLRIAIGY TAGALEVTKD LHKFPSWTHF
     LVAPLLPSRR RLRRELDIAM KIVEKQIQLH EQAEKDGLKN YDTLLDWMLD NCSDKESSVE
     AMTIFQCFIA MASIHTTEFS LANVLFDLCA HPEWFPVLRE ELDEVIRVHG NIGHRLPAKQ
     WLQKLEKMDS LLAETLRLCP TMLTSIQRLA LEKVQLKDGT VIPKGSRLAW ASLHHVTDPE
     VDGTLAAWDP MRNYRKRHSG SGENLTKFVA GQINESTLGF GYGNQACPGR YFAVNEIKMM
     LARLLLEFEF KFPEGKSRPK VFFIGEIACL DHDATLMMRN VRTC