DTPB_ASPFN
ID DTPB_ASPFN Reviewed; 357 AA.
AC B8NR70;
DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 56.
DE RecName: Full=N-methyltransferase dtpB {ECO:0000303|PubMed:24677498};
DE EC=2.1.1.- {ECO:0000269|PubMed:24677498};
DE AltName: Full=Ditryptophenaline biosynthesis protein B {ECO:0000303|PubMed:24677498};
GN Name=dtpB {ECO:0000303|PubMed:24677498}; ORFNames=AFLA_005450;
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: N-methyltransferase; part of the gene cluster that mediates
CC 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 -!- PATHWAY: Alkaloid biosynthesis. {ECO:0000269|PubMed:24677498}.
CC -!- DISRUPTION PHENOTYPE: Abolishes the production of ditryptophenaline
CC (PubMed:24677498). {ECO:0000269|PubMed:24677498}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily.
CC {ECO:0000305}.
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DR EMBL; EQ963482; EED47903.1; -; Genomic_DNA.
DR RefSeq; XP_002382745.1; XM_002382704.1.
DR AlphaFoldDB; B8NR70; -.
DR SMR; B8NR70; -.
DR STRING; 5059.CADAFLAP00010610; -.
DR EnsemblFungi; EED47903; EED47903; AFLA_005450.
DR VEuPathDB; FungiDB:AFLA_005450; -.
DR eggNOG; ENOG502QS9T; Eukaryota.
DR HOGENOM; CLU_049766_0_2_1; -.
DR OMA; WPEPYFR; -.
DR Proteomes; UP000001875; Unassembled WGS sequence.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0009820; P:alkaloid metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR019257; MeTrfase_dom.
DR InterPro; IPR017804; MeTrfase_EgtD-like.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR017805; SAM_MeTrfase_EasF-type_put.
DR Pfam; PF10017; Methyltransf_33; 1.
DR PIRSF; PIRSF018005; UCP018005; 1.
DR TIGRFAMs; TIGR03439; methyl_EasF; 1.
PE 1: Evidence at protein level;
KW Alkaloid metabolism; Methyltransferase; S-adenosyl-L-methionine;
KW Transferase.
FT CHAIN 1..357
FT /note="N-methyltransferase dtpB"
FT /id="PRO_0000438202"
SQ SEQUENCE 357 AA; 39967 MW; 720C2F61CDA46617 CRC64;
MVKNNAGIVN MFEKRRTQTT TIPIIEIMRE KRSEDLETEI VQGLQFDSLQ LPQELLWDDA
GQILFDDLCN SSTYYLTKKE KEILQKYSTD MAATIPEGST LIELGCGSLR KTGILLSALE
KSHKAVTYYA LDVSQDSLEN GLAQLHKGLG CLDHVELRGL WGTYEDAIAW LADQHPINVH
NGITFLWMGN SMTNMHLAQA QSLLSRMTKT CIGSGIPCQI LVSVDSCSAE DIVMGAYDTD
SQPLKDFIMN GLKSANRILG KDVFCASDWT FGTVLDRVRH EVQVFYAPTR DVTIHIDSHP
CKITKGEKIA VISSGKWPEP YFRSMLEGIG LQVLDLWRDS DQFYCMNPLP LICSFPG