ID   IFGB_PENRF              Reviewed;         340 AA.
AC   W6QL00;
DT   20-JUN-2018, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 21.
DE   RecName: Full=4-dimethylallyltryptophan N-methyltransferase ifgB {ECO:0000303|PubMed:28620689};
DE            EC=2.1.1.261 {ECO:0000250|UniProtKB:B6D5I7};
DE   AltName: Full=Isofumigaclavine biosynthesis cluster A protein B {ECO:0000303|PubMed:28620689};
GN   Name=ifgB {ECO:0000303|PubMed:28620689}; ORFNames=PROQFM164_S05g000509;
OS   Penicillium roqueforti (strain FM164).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=1365484;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FM164;
RX   PubMed=24407037; DOI=10.1038/ncomms3876;
RA   Cheeseman K., Ropars J., Renault P., Dupont J., Gouzy J., Branca A.,
RA   Abraham A.L., Ceppi M., Conseiller E., Debuchy R., Malagnac F., Goarin A.,
RA   Silar P., Lacoste S., Sallet E., Bensimon A., Giraud T., Brygoo Y.;
RT   "Multiple recent horizontal transfers of a large genomic region in cheese
RT   making fungi.";
RL   Nat. Commun. 5:2876-2876(2014).
RN   [2]
RP   FUNCTION, AND PATHWAY.
RX   PubMed=28620689; DOI=10.1007/s00253-017-8366-6;
RA   Fernandez-Bodega A., Alvarez-Alvarez R., Liras P., Martin J.F.;
RT   "Silencing of a second dimethylallyltryptophan synthase of Penicillium
RT   roqueforti reveals a novel clavine alkaloid gene cluster.";
RL   Appl. Microbiol. Biotechnol. 101:6111-6121(2017).
RN   [3]
RP   FUNCTION.
RX   PubMed=28902217; DOI=10.1039/c7ob02095c;
RA   Gerhards N., Li S.M.;
RT   "A bifunctional old yellow enzyme from Penicillium roqueforti is involved
RT   in ergot alkaloid biosynthesis.";
RL   Org. Biomol. Chem. 15:8059-8071(2017).
CC   -!- FUNCTION: 4-dimethylallyltryptophan N-methyltransferase; part of the
CC       gene cluster that mediates the biosynthesis of isofumigaclavines,
CC       fungal ergot alkaloids (PubMed:28620689). The tryptophan
CC       dimethylallyltransferase ifgA catalyzes the first step of ergot
CC       alkaloid biosynthesis by condensing dimethylallyl diphosphate (DMAP)
CC       and tryptophan to form 4-dimethylallyl-L-tryptophan (PubMed:28620689).
CC       The second step is catalyzed by the methyltransferase ifgB that
CC       methylates 4-dimethylallyl-L-tryptophan in the presence of S-adenosyl-
CC       L-methionine, resulting in the formation of N-methyl-dimethylallyl-L-
CC       tryptophan (PubMed:28620689). The catalase ifgD and the FAD-dependent
CC       oxidoreductase ifgC then transform N-methyl-dimethylallyl-L-tryptophan
CC       to chanoclavine-I which is further oxidized by ifgE in the presence of
CC       NAD(+), resulting in the formation of chanoclavine-I aldehyde
CC       (PubMed:28902217). The chanoclavine-I aldehyde reductases ifgG and/or
CC       fgaOx3 reduce chanoclavine-I aldehyde to dihydrochanoclavine-I aldehyde
CC       that spontaneously dehydrates to form 6,8-dimethyl-6,7-
CC       didehydroergoline (PubMed:28620689, PubMed:28902217). The festuclavine
CC       dehydrogenases ifgF1 and/or ifgF2 then catalyze the reduction of 6,8-
CC       dimethyl-6,7-didehydroergoline to form festuclavine (PubMed:28620689).
CC       Hydrolysis of festuclavine by a yet undetermined cytochrome P450
CC       monooxygenase (called ifgH) then leads to the formation of
CC       isofumigaclavine B which is in turn acetylated by ifgI to
CC       isofumigaclavine A (PubMed:28620689). Penicillium roqueforti has
CC       interestingly at least two sets of genes for the consumption of
CC       chanoclavine-I aldehyde on three different loci, the OYEs ifgG/fgaOx3
CC       and the festuclavine synthase homologs ifgF1/ifgF2 (PubMed:28620689,
CC       PubMed:28902217). The reason for the duplication of these genes is
CC       unclear, probably to ensure the conversion of chanoclavine-I aldehyde
CC       by differential gene expression under various environmental conditions
CC       (PubMed:28902217). {ECO:0000269|PubMed:28620689,
CC       ECO:0000269|PubMed:28902217}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=4-(3-methylbut-2-enyl)-L-tryptophan + S-adenosyl-L-methionine
CC         = 4-(3-methylbut-2-enyl)-L-abrine + H(+) + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:34435, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:58209, ChEBI:CHEBI:59789, ChEBI:CHEBI:67248;
CC         EC=2.1.1.261; Evidence={ECO:0000250|UniProtKB:B6D5I7};
CC   -!- PATHWAY: Alkaloid biosynthesis; ergot alkaloid biosynthesis.
CC       {ECO:0000305|PubMed:28620689}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:B6D5I7}.
CC   -!- SIMILARITY: Belongs to the methyltransferase superfamily.
CC       {ECO:0000305}.
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DR   EMBL; HG792019; CDM36676.1; -; Genomic_DNA.
DR   AlphaFoldDB; W6QL00; -.
DR   SMR; W6QL00; -.
DR   STRING; 1365484.W6QL00; -.
DR   EnsemblFungi; CDM36676; CDM36676; PROQFM164_S05g000509.
DR   OrthoDB; 762504at2759; -.
DR   UniPathway; UPA00327; -.
DR   Proteomes; UP000030686; Unassembled WGS sequence.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0035835; P:indole alkaloid biosynthetic process; IEA:UniProtKB-UniPathway.
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   3: Inferred from homology;
KW   Alkaloid metabolism; Methyltransferase; Transferase.
FT   CHAIN           1..340
FT                   /note="4-dimethylallyltryptophan N-methyltransferase ifgB"
FT                   /id="PRO_0000444537"
SQ   SEQUENCE   340 AA;  37904 MW;  6C47190C75C1D5C0 CRC64;
     MTIINSRIID IRQSTFEESI PDQVTAGLST TPKTLPALLF YSGEGIRHWI EHSTAADFYP
     RHEELRILRA RAAEMVDSIA NNSVVVDLGS ASLDKVLPLL EALEASKKNI TFYALDLSFS
     ELQSTLQSLP YEQFKFVKIG ALHGTFEDGV QWLKDTPGVQ DRPHCLLLFG LTVGNYSRPN
     AAKFLQNIAS NALAASPVQS SILLSLDSCK MPTKVLRAYT AEGVVPFALA SLDYGNTLFA
     PNKMGEKVFQ PSDWYFLSEW NYMLGRHEAS LITKGKEVRL GGPLNDIVIE KHEKIRFGCS
     YKYDTDERQV LFGSAGLTDV KEWSVEGCDV SFYQLQMCPN