ID   DTPC_ASPFN              Reviewed;         181 AA.
AC   B8NR71;
DT   02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 58.
DE   RecName: Full=Cytochrome P450 monooxygenase dtpC {ECO:0000303|PubMed:24677498};
DE            EC=1.-.-.- {ECO:0000269|PubMed:24677498};
DE   AltName: Full=Ditryptophenaline biosynthesis protein C {ECO:0000303|PubMed:24677498};
GN   Name=dtpC {ECO:0000303|PubMed:24677498}; ORFNames=AFLA_005460;
OS   Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357
OS   / JCM 12722 / SRRC 167).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=332952;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC
RC   167;
RX   PubMed=25883274; DOI=10.1128/genomea.00168-15;
RA   Nierman W.C., Yu J., Fedorova-Abrams N.D., Losada L., Cleveland T.E.,
RA   Bhatnagar D., Bennett J.W., Dean R., Payne G.A.;
RT   "Genome sequence of Aspergillus flavus NRRL 3357, a strain that causes
RT   aflatoxin contamination of food and feed.";
RL   Genome Announc. 3:E0016815-E0016815(2015).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, AND DISRUPTION PHENOTYPE.
RX   PubMed=24677498; DOI=10.1002/cbic.201300751;
RA   Saruwatari T., Yagishita F., Mino T., Noguchi H., Hotta K., Watanabe K.;
RT   "Cytochrome P450 as dimerization catalyst in diketopiperazine alkaloid
RT   biosynthesis.";
RL   ChemBioChem 15:656-659(2014).
CC   -!- FUNCTION: Cytochrome P450 monooxygenase; part of the gene cluster that
CC       mediates the biosynthesis of the dimeric diketopiperazine alkaloid
CC       ditryptophenaline (PubMed:24677498). The nonribosomal peptide synthase
CC       dtpA accepts L-tryptophan and L-phenylalanine as its substrates and
CC       forms the phenylalanyl-tryptophanyl cyclic dipeptide product
CC       cyclophenylalanyltryptophenyl (PubMed:24677498). The N-
CC       methyltransferase dtpB is responsible for the N-methylation of
CC       cyclophenylalanyltryptophenyl to yield cyclo-N-
CC       methylphenylalanyltryptophenyl (PubMed:24677498). The cytochrome P450
CC       monooxygenase is responsible not only for pyrroloindole ring formation
CC       but also for concurrent dimerization of N-
CC       methylphenylalanyltryptophanyl diketopiperazine monomers into a
CC       homodimeric product (PubMed:24677498). {ECO:0000269|PubMed:24677498}.
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000250|UniProtKB:P04798};
CC   -!- PATHWAY: Alkaloid biosynthesis. {ECO:0000269|PubMed:24677498}.
CC   -!- PATHWAY: Secondary metabolite biosynthesis.
CC       {ECO:0000269|PubMed:24677498}.
CC   -!- DISRUPTION PHENOTYPE: Abolishes the production of ditryptophenaline but
CC       leads to the accumulation of cyclo-N-methylphenylalanyltryptophenyl
CC       (PubMed:24677498). {ECO:0000269|PubMed:24677498}.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; EQ963482; EED47904.1; -; Genomic_DNA.
DR   RefSeq; XP_002382746.1; XM_002382705.1.
DR   AlphaFoldDB; B8NR71; -.
DR   SMR; B8NR71; -.
DR   STRING; 5059.CADAFLAP00010611; -.
DR   EnsemblFungi; EED47904; EED47904; AFLA_005460.
DR   VEuPathDB; FungiDB:AFLA_005460; -.
DR   eggNOG; KOG0158; Eukaryota.
DR   HOGENOM; CLU_1488691_0_0_1; -.
DR   OMA; YYERPLE; -.
DR   Proteomes; UP000001875; 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   GO; GO:0008152; P:metabolic process; IEA:UniProt.
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   1: Evidence at protein level;
KW   Heme; Iron; Metal-binding; Monooxygenase; Oxidoreductase.
FT   CHAIN           1..181
FT                   /note="Cytochrome P450 monooxygenase dtpC"
FT                   /id="PRO_0000438203"
FT   BINDING         125
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   181 AA;  20313 MW;  FC31540A9CDEA562 CRC64;
     MKTPEYLAPL REELAAALKQ ADNAWSFDIF KHTPKLESFT KECLRVFTPS GKKPLQLRST
     GRTLSPGTKF SLPAQQAHLD PDNYPNPNIF DGYRFCDPQS GACDIRGTIT PSAKWLIFGI
     GTSACPARLL ATRISQTLFF KVLRKYDLRL KLDNGQPEVV YAATNMFVNF NTQMYVKSAS
     I