FTMB_NEOFI
ID FTMB_NEOFI Reviewed; 463 AA.
AC A1DA62;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 16-OCT-2013, sequence version 2.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=Tryprostatin B synthase {ECO:0000303|PubMed:23109474};
DE EC=2.5.1.106 {ECO:0000250|UniProtKB:Q4WAW7};
DE AltName: Full=Brevianamide F prenyltransferase {ECO:0000303|PubMed:23109474};
DE AltName: Full=Fumitremorgin biosynthesis protein B;
GN Name=ftmPT1 {ECO:0000303|PubMed:23109474};
GN Synonyms=ftmB {ECO:0000250|UniProtKB:Q4WAW7}; ORFNames=NFIA_093720;
OS Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=331117;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181
RC / WB 181;
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
RN [2]
RP FUNCTION.
RX PubMed=23109474; DOI=10.1002/cbic.201200523;
RA Mundt K., Wollinsky B., Ruan H.L., Zhu T., Li S.M.;
RT "Identification of the verruculogen prenyltransferase FtmPT3 by a
RT combination of chemical, bioinformatic and biochemical approaches.";
RL ChemBioChem 13:2583-2592(2012).
CC -!- FUNCTION: Brevianamide F prenyltransferase; part of the gene cluster
CC that mediates the biosynthesis of fumitremorgins, indole alkaloids that
CC carry not only intriguing chemical structures, but also interesting
CC biological and pharmacological activities (PubMed:23109474). The
CC biosynthesis of fumitremorgin-type alkaloids begins by condensation of
CC the two amino acids L-tryptophan and L-proline to brevianamide F,
CC catalyzed by the non-ribosomal peptide synthetase ftmPS/ftmA (By
CC similarity). Brevianamide F is then prenylated by the prenyltransferase
CC ftmPT1/ftmB in the presence of dimethylallyl diphosphate, resulting in
CC the formation of tryprostatin B (By similarity). The three cytochrome
CC P450 monooxygenases, ftmP450-1/ftmC, ftmP450-2/ftmE and ftmP450-3/FtmG,
CC are responsible for the conversion of tryprostatin B to 6-
CC hydroxytryprostatin B, tryprostatin A to fumitremorgin C and
CC fumitremorgin C to 12,13-dihydroxyfumitremorgin C, respectively (By
CC similarity). The putative methyltransferase ftmMT/ftmD is expected for
CC the conversion of 6-hydroxytryprostatin B to tryprostatin A (By
CC similarity). FtmPT2/FtmH catalyzes the prenylation of 12,13-
CC dihydroxyfumitre-morgin C in the presence of dimethylallyl diphosphate,
CC resulting in the formation of fumitremorgin B (By similarity).
CC Fumitremorgin B is further converted to verruculogen by ftmOx1/ftmF via
CC the insertion of an endoperoxide bond between the two prenyl moieties
CC (By similarity). Finally, verruculogen is further converted to
CC fumitremorgin A by the verruculogen prenyltransferase ftmPT3
CC (PubMed:23109474). {ECO:0000250|UniProtKB:Q4WAW7,
CC ECO:0000269|PubMed:23109474}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=brevianamide F + dimethylallyl diphosphate = diphosphate +
CC tryprostatin B; Xref=Rhea:RHEA:35939, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:57623, ChEBI:CHEBI:64530, ChEBI:CHEBI:72760;
CC EC=2.5.1.106; Evidence={ECO:0000250|UniProtKB:Q4WAW7};
CC -!- PATHWAY: Mycotoxin biosynthesis. {ECO:0000250|UniProtKB:Q4WAW7}.
CC -!- SIMILARITY: Belongs to the tryptophan dimethylallyltransferase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EAW19752.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; DS027694; EAW19752.1; ALT_INIT; Genomic_DNA.
DR RefSeq; XP_001261649.1; XM_001261648.1.
DR AlphaFoldDB; A1DA62; -.
DR SMR; A1DA62; -.
DR STRING; 36630.CADNFIAP00008616; -.
DR MEROPS; M77.004; -.
DR EnsemblFungi; EAW19752; EAW19752; NFIA_093720.
DR GeneID; 4588682; -.
DR KEGG; nfi:NFIA_093720; -.
DR eggNOG; ENOG502S2XP; Eukaryota.
DR OrthoDB; 1531660at2759; -.
DR Proteomes; UP000006702; Unassembled WGS sequence.
DR GO; GO:0004659; F:prenyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0009820; P:alkaloid metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0044249; P:cellular biosynthetic process; IEA:UniProt.
DR GO; GO:1901576; P:organic substance biosynthetic process; IEA:UniProt.
DR CDD; cd13929; PT-DMATS_CymD; 1.
DR InterPro; IPR033964; Aro_prenylTrfase.
DR InterPro; IPR017795; Aro_prenylTrfase_DMATS.
DR InterPro; IPR012148; DMATS-type_fun.
DR PANTHER; PTHR40627; PTHR40627; 1.
DR Pfam; PF11991; Trp_DMAT; 1.
DR PIRSF; PIRSF000509; Trp_DMAT; 1.
DR SFLD; SFLDS00036; Aromatic_Prenyltransferase; 1.
DR TIGRFAMs; TIGR03429; arom_pren_DMATS; 1.
PE 3: Inferred from homology;
KW Alkaloid metabolism; Prenyltransferase; Reference proteome; Transferase.
FT CHAIN 1..463
FT /note="Tryprostatin B synthase"
FT /id="PRO_0000424113"
FT BINDING 93
FT /ligand="brevianamide F"
FT /ligand_id="ChEBI:CHEBI:64530"
FT /evidence="ECO:0000250|UniProtKB:Q4WAW7"
FT BINDING 101
FT /ligand="brevianamide F"
FT /ligand_id="ChEBI:CHEBI:64530"
FT /evidence="ECO:0000250|UniProtKB:Q4WAW7"
FT BINDING 112
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250|UniProtKB:Q4WAW7"
FT BINDING 200
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250|UniProtKB:Q4WAW7"
FT BINDING 202
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250|UniProtKB:Q4WAW7"
FT BINDING 204
FT /ligand="brevianamide F"
FT /ligand_id="ChEBI:CHEBI:64530"
FT /evidence="ECO:0000250|UniProtKB:Q4WAW7"
FT BINDING 293
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250|UniProtKB:Q4WAW7"
FT BINDING 295
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250|UniProtKB:Q4WAW7"
FT BINDING 379
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250|UniProtKB:Q4WAW7"
FT BINDING 381
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250|UniProtKB:Q4WAW7"
FT BINDING 445
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250|UniProtKB:Q4WAW7"
FT BINDING 449
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250|UniProtKB:Q4WAW7"
FT SITE 114
FT /note="Required for regioselectivity"
FT /evidence="ECO:0000250|UniProtKB:Q4WAW7"
SQ SEQUENCE 463 AA; 52594 MW; B4D81C6A70BAC451 CRC64;
MPPAPPDQKP CHLQPAPYRA LSETILFGSL NEERWWHSTA PILSRLLISS NYDVDVQYKY
LSLYRHLVLP ALGPYPQRDP ETGIIATQWR SGMVLTGLPI EFSNNVARAL IRIGVDPVTA
DSGTAQDPFN TARPKGYLET AARLLPGVDL TRFYEFETEL VITKEEEAVL QANPDLFKSP
WKSQILTAMD LQKSGTVLVK AYFYPQPKSA VTGRSTEELL VNAIRKVDRE SRFETQLANL
ERYMERRRRG LHVPVVTADK PPPTEADKTF DACSFFPHFL STDLVEPGKS RVKFYASERH
VNLKMVEDIW TFGGLRRDPD ALKGLELLRH FWADIQMREG YYTMPRGFCE LGKSSAGFEA
PMMFHFHLDG SQSPFPDPQM YVCVFGMNSR KLVEGLTTFY RRLGWEDMAS HYQGNFLANY
PDEDFEKAAH LCAYVSFAYK DGGAYVTLYN HSFNPLGDVA LAN
