ID   VERC_CLORO              Reviewed;         502 AA.
AC   A0A1U9YHZ9;
DT   17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT   17-JUN-2020, sequence version 2.
DT   03-AUG-2022, entry version 11.
DE   RecName: Full=Cytochrome P450 monooxygenase verC {ECO:0000303|PubMed:28376389};
DE            EC=1.-.-.- {ECO:0000305|PubMed:28376389};
DE   AltName: Full=Verticillin biosynthesis cluster protein C {ECO:0000303|PubMed:28376389};
GN   Name=verC {ECO:0000303|PubMed:28376389};
OS   Clonostachys rogersoniana.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Bionectriaceae; Clonostachys.
OX   NCBI_TaxID=122658;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND PATHWAY.
RC   STRAIN=XZC04-CC-302;
RX   PubMed=28376389; DOI=10.1016/j.fgb.2017.03.007;
RA   Wang Y., Hu P., Pan Y., Zhu Y., Liu X., Che Y., Liu G.;
RT   "Identification and characterization of the verticillin biosynthetic gene
RT   cluster in Clonostachys rogersoniana.";
RL   Fungal Genet. Biol. 103:25-33(2017).
RN   [2]
RP   INDUCTION.
RX   PubMed=29058652; DOI=10.1099/mic.0.000557;
RA   Guo Z., Hao T., Wang Y., Pan Y., Ren F., Liu X., Che Y., Liu G.;
RT   "VerZ, a Zn(II)2Cys6 DNA-binding protein, regulates the biosynthesis of
RT   verticillin in Clonostachys rogersoniana.";
RL   Microbiology 163:1654-1663(2017).
CC   -!- FUNCTION: Cytochrome P450 monooxygenase; part of the gene cluster that
CC       mediates the biosynthesis of 11'-deoxyverticillin A, one of the dimeric
CC       epipolythiodioxopiperazines (ETPs) from the verticillin family that act
CC       as mycotoxins (PubMed:28376389). 11'-deoxyverticillin A is required for
CC       normal conidiation (PubMed:28376389). The nonribosomal peptide
CC       synthetase verP is speculated to be responsible for condensation of
CC       amino acids to form the carbon skeleton of verticillin, whereas the
CC       cluster-specific tailoring enzymes are involved in further
CC       modifications leading to the production of 11'-deoxyverticillin A
CC       (Probable). {ECO:0000269|PubMed:28376389, ECO:0000305|PubMed:28376389}.
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000250|UniProtKB:P04798};
CC   -!- PATHWAY: Mycotoxin biosynthesis. {ECO:0000269|PubMed:28376389}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC       protein {ECO:0000255}.
CC   -!- INDUCTION: Expression is regulated by the cluster-specific regulator
CC       verZ. {ECO:0000269|PubMed:29058652}.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AQZ42162.1; Type=Erroneous gene model prediction;
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DR   EMBL; KY359203; AQZ42162.1; ALT_SEQ; Genomic_DNA.
DR   AlphaFoldDB; A0A1U9YHZ9; -.
DR   SMR; A0A1U9YHZ9; -.
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; IPR017972; Cyt_P450_CS.
DR   InterPro; IPR002401; Cyt_P450_E_grp-I.
DR   InterPro; IPR036396; Cyt_P450_sf.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00463; EP450I.
DR   PRINTS; PR00385; P450.
DR   SUPFAM; SSF48264; SSF48264; 1.
PE   2: Evidence at transcript level;
KW   Glycoprotein; Heme; Iron; Membrane; Metal-binding; Monooxygenase;
KW   Oxidoreductase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..502
FT                   /note="Cytochrome P450 monooxygenase verC"
FT                   /id="PRO_0000450161"
FT   TRANSMEM        9..29
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         444
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        124
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        190
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        271
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        342
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   502 AA;  56554 MW;  156A982FB760054F CRC64;
     MLSEMLGEIA ALPMVSLLGA ALIVVSVLGR RLLVSNIAWA ITGQTPAKSL AKRSRLPGLP
     FKFPNGQGTE KFFGGRSAAR RWRIQYGPIY AIWAGLKREV VLSTPEHVQA FYKDSHLHVK
     ATDNNSGWLF AELLGSCVGV VSQGRWKRVR RPFEHPFSRP ESLTRPKAFI HEARDYFAVL
     NPNIQELTIN TSNDLKHCPF FMVASIFFGI HTTAQRDELK QLGPPREELF RHAFMGGMNR
     YAITKYLPGS ALALLRQFQG KWEGFVKAAY NRSIQTGDGT IVPLFEAVNR GEMSMQELLQ
     TLDESLFANL DVTAHAVSWN VIRIAHHQDI QQKVRIEIQA NNNSEKSYEN YVCRDDTLLA
     ACVLETSRLH PVLPFSNPEA AEEDKIVGGY IIPQTDVIVD THAINIDNPH WVDSNSFDPH
     RHLGQKDSSR RYNMWRFGFG PRQCLGKNVA DIILRIILCE MLNTYELGLL EEEGITGVKL
     QPDSWIGLPN GVVQMTPLKL DE