FTMH_NEOFI
ID FTMH_NEOFI Reviewed; 393 AA.
AC A1DA66;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=12-alpha,13-alpha-dihydroxyfumitremorgin C prenyltransferase {ECO:0000303|PubMed:23109474};
DE EC=2.5.1.110 {ECO:0000250|UniProtKB:Q4WAX1};
DE AltName: Full=Fumitremorgin biosynthesis protein H {ECO:0000250|UniProtKB:Q4WAX1};
GN Name=ftmPT2 {ECO:0000303|PubMed:23109474};
GN Synonyms=ftmH {ECO:0000250|UniProtKB:Q4WAX1}; ORFNames=NFIA_093760;
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: 12-alpha,13-alpha-dihydroxyfumitremorgin C prenyltransferase;
CC part of the gene cluster that mediates the biosynthesis of
CC fumitremorgins, indole alkaloids that carry not only intriguing
CC chemical structures, but also interesting biological and
CC 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:Q4WAX1,
CC ECO:0000269|PubMed:23109474}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=12alpha,13alpha-dihydroxyfumitremorgin C + dimethylallyl
CC diphosphate = diphosphate + fumitremorgin B; Xref=Rhea:RHEA:35971,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57623, ChEBI:CHEBI:64531,
CC ChEBI:CHEBI:72764; EC=2.5.1.110;
CC Evidence={ECO:0000250|UniProtKB:Q4WAX1};
CC -!- PATHWAY: Mycotoxin biosynthesis. {ECO:0000250|UniProtKB:Q4WAX1}.
CC -!- SIMILARITY: Belongs to the tryptophan dimethylallyltransferase family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; DS027694; EAW19756.1; -; Genomic_DNA.
DR RefSeq; XP_001261653.1; XM_001261652.1.
DR AlphaFoldDB; A1DA66; -.
DR SMR; A1DA66; -.
DR STRING; 36630.CADNFIAP00008832; -.
DR EnsemblFungi; EAW19756; EAW19756; NFIA_093760.
DR GeneID; 4588782; -.
DR KEGG; nfi:NFIA_093760; -.
DR VEuPathDB; FungiDB:NFIA_093760; -.
DR eggNOG; ENOG502S2XP; Eukaryota.
DR HOGENOM; CLU_037431_0_0_1; -.
DR OMA; CLDNTID; -.
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;
KW Virulence.
FT CHAIN 1..393
FT /note="12-alpha,13-alpha-dihydroxyfumitremorgin C
FT prenyltransferase"
FT /id="PRO_0000424115"
FT BINDING 94
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q4WAW7"
FT BINDING 105
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250|UniProtKB:Q4WAW7"
FT BINDING 192
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250|UniProtKB:Q4WAW7"
FT BINDING 194
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250|UniProtKB:Q4WAW7"
FT BINDING 268
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250|UniProtKB:Q4WAW7"
FT BINDING 353
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250|UniProtKB:Q4WAW7"
FT BINDING 355
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250|UniProtKB:Q4WAW7"
SQ SEQUENCE 393 AA; 44505 MW; 2D561D0D22892CC2 CRC64;
MTIATEISCP EEEAFQLLDK YSWFPNDDQR RWWEYTGPNL LKLLRDAQYP QKDQISCLYL
LQQLLVPYLG TFPVAGQAPL PWWSNVTTYG VPFELSWNLL HNIVRIGFEP LSHLAESGVD
AFNKIAPEEC LSRLACLDNT IDLARFRHFQ HQLLVTPDEE RRLLEEKGPL PKSGRGQQAL
AVEFQNGGIS AKAYFFPGMK SLATGLSPGK LILDSIESLA LPGLKEPVHH LCNSLGLQDD
GHPTDTAIAP FLLGVDLCTP ERSRLKFYVT DQVVSWDRVA DMWTLRGKRL EDPQCADGLT
LLRKLWDLLE IPEGYRSNIR PDFAFGTPPP EDYRPVMMAN WTLSPKKKFP DPQIYLLTVG
MNDAVVMDAL VAFYEVLGWT DLASTYKDKV ASY
