ID   VERB_CLORO              Reviewed;         514 AA.
AC   A0A1U9YI05;
DT   17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2017, sequence version 1.
DT   03-AUG-2022, entry version 12.
DE   RecName: Full=Cytochrome P450 monooxygenase verB {ECO:0000303|PubMed:28376389};
DE            EC=1.-.-.- {ECO:0000305|PubMed:28376389};
DE   AltName: Full=Verticillin biosynthesis cluster protein B {ECO:0000303|PubMed:28376389};
GN   Name=verB {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, DISRUPTION PHENOTYPE, AND
RP   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   -!- DISRUPTION PHENOTYPE: Completely abolishes the 11'-deoxyverticillin A
CC       production. {ECO:0000269|PubMed:28376389}.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; KY359203; AQZ42168.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1U9YI05; -.
DR   SMR; A0A1U9YI05; -.
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   2: Evidence at transcript level;
KW   Heme; Iron; Membrane; Metal-binding; Monooxygenase; Oxidoreductase;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..514
FT                   /note="Cytochrome P450 monooxygenase verB"
FT                   /id="PRO_0000450160"
FT   TRANSMEM        5..25
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         457
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"
SQ   SEQUENCE   514 AA;  58465 MW;  97C2D8B8568EE3A1 CRC64;
     MARPWLSASV LITAVILLVD YLNYYRLRKR LGGIPVVGDA SYFWRRIRWT ESDTNFQKVI
     QHGYDTFSKK AKPFAFWGQH EDFILVLPPG SCEEVKHLGP EKLNFLQAVE DSYHFKLHTN
     ILGRSHVDAV RQSVNKNMNQ LHEIVVKKAE ETIPKLFDDI AASNEPFAAF LTIWHLVHIV
     SASYLVGTEF CANEEYLQAI EYYCINVPNF IYGYFWVPVP LRRLYWYLSP QGYKVRACKA
     KLKTFIVPKI RETISAWQNG QKSSSYTLLG AMLDLKAQKG QIKRDPTAMT KAELERQIDI
     FSDEMIFTGF DSAGPVACMV TQLLFEALRD KDLTKALRQE LKSALEANNG QWNVQAMNLT
     PKLDSFTRES LRVNGPTLLS VTRTVMEPMQ LKSGLSLQSG SIISSPSWLI HNDEDNYENA
     HQFDPYRFYN PSTNAVTTKV TTASTNFLGY GYGTQMCPGR HLGIKMSQIL FSKLLMRYDG
     EFADAKAGKP ANIVTSGQVL PPYYAKVILK RRGI