FTMF_NEOFI
ID FTMF_NEOFI Reviewed; 291 AA.
AC A1DA64;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 25-MAY-2022, entry version 61.
DE RecName: Full=Verruculogen synthase {ECO:0000303|PubMed:23109474};
DE EC=1.14.11.38 {ECO:0000250|UniProtKB:Q4WAW9};
DE AltName: Full=Fumitremorgin biosynthesis protein F {ECO:0000250|UniProtKB:Q4WAW9};
GN Name=ftmOx1 {ECO:0000303|PubMed:23109474};
GN Synonyms=ftmF {ECO:0000250|UniProtKB:Q4WAW9}; ORFNames=NFIA_093740;
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: Verruculogen synthase; part of the gene cluster that mediates
CC the biosynthesis of fumitremorgins, indole alkaloids that carry not
CC only intriguing chemical structures, but also interesting biological
CC and pharmacological activities (PubMed:23109474). The biosynthesis of
CC fumitremorgin-type alkaloids begins by condensation of the two amino
CC acids L-tryptophan and L-proline to brevianamide F, catalyzed by the
CC non-ribosomal peptide synthetase ftmPS/ftmA (By similarity).
CC Brevianamide F is then prenylated by the prenyltransferase ftmPT1/ftmB
CC in the presence of dimethylallyl diphosphate, resulting in the
CC formation of tryprostatin B (By similarity). The three cytochrome P450
CC monooxygenases, ftmP450-1/ftmC, ftmP450-2/ftmE and ftmP450-3/FtmG, are
CC 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:Q4WAW9,
CC ECO:0000269|PubMed:23109474}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + AH2 + fumitremorgin B + 2 O2 = A + CO2 + H2O
CC + succinate + verruculogen; Xref=Rhea:RHEA:35975, ChEBI:CHEBI:13193,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:16810, ChEBI:CHEBI:17499, ChEBI:CHEBI:30031,
CC ChEBI:CHEBI:64531, ChEBI:CHEBI:72765; EC=1.14.11.38;
CC Evidence={ECO:0000250|UniProtKB:Q4WAW9};
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC Evidence={ECO:0000250|UniProtKB:Q4WAW9};
CC -!- PATHWAY: Mycotoxin biosynthesis. {ECO:0000250|UniProtKB:Q4WAW9}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q4WAW9}.
CC -!- SIMILARITY: Belongs to the PhyH family. {ECO:0000305}.
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DR EMBL; DS027694; EAW19754.1; -; Genomic_DNA.
DR RefSeq; XP_001261651.1; XM_001261650.1.
DR AlphaFoldDB; A1DA64; -.
DR SMR; A1DA64; -.
DR STRING; 36630.CADNFIAP00008814; -.
DR EnsemblFungi; EAW19754; EAW19754; NFIA_093740.
DR GeneID; 4588684; -.
DR KEGG; nfi:NFIA_093740; -.
DR VEuPathDB; FungiDB:NFIA_093740; -.
DR eggNOG; ENOG502S7ZW; Eukaryota.
DR HOGENOM; CLU_047725_1_0_1; -.
DR OMA; VIHAICE; -.
DR OrthoDB; 623398at2759; -.
DR Proteomes; UP000006702; Unassembled WGS sequence.
DR GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0009820; P:alkaloid metabolic process; IEA:UniProtKB-KW.
DR InterPro; IPR008775; Phytyl_CoA_dOase.
DR Pfam; PF05721; PhyH; 1.
PE 3: Inferred from homology;
KW Alkaloid metabolism; Dioxygenase; Iron; Oxidoreductase; Reference proteome;
KW Virulence.
FT CHAIN 1..291
FT /note="Verruculogen synthase"
FT /id="PRO_0000424135"
SQ SEQUENCE 291 AA; 32740 MW; BCCA28B1BA1AFE72 CRC64;
MTVDSKPQLQ RLAADVDVDL MCRLLEEDGA FILKDLLPLD VVESFNRELD VQMAIPPPKG
ERLLADKYPP HFKYVPNVAT TCPTFRNNIL INPVIHAICE GYFQRTGDYW LSAAFLREIE
SGMPAQPFHR DDATHPLMHH QPLEAPPISL SVIFPLTEFT EENGATEVIL GSHRWMEVGT
PERDQAVLAT MDPGDVLVVR QRVVHAGGGN RTTTGDPRRV VLAYFNSCQL TPFETYRTMP
RETVESMTVL GQRMLGWRTM KPSDPNIVGI NIIDDKRLEN VLQLKATDLP A
