NODD1_HYPPI
ID NODD1_HYPPI Reviewed; 431 AA.
AC A0A2I6PIZ7;
DT 10-APR-2019, integrated into UniProtKB/Swiss-Prot.
DT 28-MAR-2018, sequence version 1.
DT 03-AUG-2022, entry version 8.
DE RecName: Full=Indole diterpene prenyltransferase nodD1 {ECO:0000303|PubMed:29283570};
DE EC=2.5.1.- {ECO:0000305|PubMed:29283570};
DE AltName: Full=Nodulisporic acid biosynthesis cluster protein D1 {ECO:0000303|PubMed:29283570};
GN Name=nodD1 {ECO:0000303|PubMed:29283570};
OS Hypoxylon pulicicidum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Xylariomycetidae; Xylariales; Hypoxylaceae; Hypoxylon.
OX NCBI_TaxID=1243767;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], IDENTIFICATION, FUNCTION, AND PATHWAY.
RC STRAIN=MF5954 / ATCC 74245;
RX PubMed=29283570; DOI=10.1021/jacs.7b10909;
RA Van de Bittner K.C., Nicholson M.J., Bustamante L.Y., Kessans S.A., Ram A.,
RA van Dolleweerd C.J., Scott B., Parker E.J.;
RT "Heterologous biosynthesis of nodulisporic acid F.";
RL J. Am. Chem. Soc. 140:582-585(2018).
CC -!- FUNCTION: Indole diterpene prenyltransferase; part of the gene cluster
CC that mediates the biosynthesis of the indole diterpenes nodulisporic
CC acids (NA). Nodulisporic acid A (NAA) and its chemically modified
CC derivatives are of particular significance because of their highly
CC potent insecticidal activity against blood-feeding arthropods and lack
CC of observable adverse effects on mammals, in particular the
CC tremogenicity associated with the paspaline-derived IDTs is not
CC observed (PubMed:29283570). The geranylgeranyl diphosphate (GGPP)
CC synthase ggs1, localized outside of the cluster, is proposed to
CC catalyze the first step in nodulisporic acid biosynthesis via
CC conversion of farnesyl pyrophosphate and isopentyl pyrophosphate into
CC geranylgeranyl pyrophosphate (GGPP) (PubMed:29283570). Condensation of
CC indole-3-glycerol phosphate with GGPP by the prenyl transferase nodC
CC then forms 3-geranylgeranylindole (3-GGI) (PubMed:29283570).
CC Epoxidation by the FAD-dependent monooxygenase nodM leads to a single-
CC epoxidized-GGI that is substrate of the terpene cyclase nodB for
CC cyclization to yield emindole SB (PubMed:29283570). The terminal methyl
CC carbon, C28, of emindole SB is then oxidized by the cytochrome P450
CC monooxygenase nodW to produce nodulisporic acid F (NAF), the
CC pentacyclic core of NAA (PubMed:29283570). NAF is converted to
CC nodulisporic acid E (NAE) via prenylation. This step is probably
CC performed by one of the indole diterpene prenyltransferases nodD1 or
CC nodD2 (Probable). Several oxidation steps performed by the FAD-linked
CC oxidoreductase nodO and one of the cytochrome P450 monooxygenase nodR,
CC nodX or nodZ further convert NAE to nodulisporic acid D (NAD)
CC (Probable). NAD is substrate of cytochrome P450 monooxygenase nodJ to
CC produce the precursor of nodulisporic acid C (NAC), converted to NAC by
CC one of the indole diterpene prenyltransferases nodD1 or nodD2
CC (Probable). The FAD-dependent monooxygenase nodY2 then oxidizes NAC to
CC nodulisporic acid B (NAB) (Probable). Finally NAB is converted to NAA
CC by one of the cytochrome P450 monooxygenases nodR, nodX or nodZ
CC (Probable). {ECO:0000269|PubMed:29283570, ECO:0000305|PubMed:29283570}.
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000305|PubMed:29283570}.
CC -!- SIMILARITY: Belongs to the tryptophan dimethylallyltransferase family.
CC {ECO:0000305}.
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DR EMBL; MG182145; AUM60056.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2I6PIZ7; -.
DR SMR; A0A2I6PIZ7; -.
DR GO; GO:0016765; F:transferase activity, transferring alkyl or aryl (other than methyl) groups; IEA:InterPro.
DR GO; GO:0009820; P:alkaloid metabolic process; IEA:InterPro.
DR CDD; cd13929; PT-DMATS_CymD; 1.
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 TIGRFAMs; TIGR03429; arom_pren_DMATS; 1.
PE 3: Inferred from homology;
KW Transferase.
FT CHAIN 1..431
FT /note="Indole diterpene prenyltransferase nodD1"
FT /id="PRO_0000446555"
FT BINDING 85..86
FT /ligand="L-tryptophan"
FT /ligand_id="ChEBI:CHEBI:57912"
FT /evidence="ECO:0000250|UniProtKB:Q50EL0"
FT BINDING 107
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q50EL0"
FT BINDING 194
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q50EL0"
FT BINDING 268
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q50EL0"
FT BINDING 270
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q50EL0"
FT BINDING 272
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q50EL0"
FT BINDING 353
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q50EL0"
SQ SEQUENCE 431 AA; 48834 MW; 0C9EB1E37F12A70A CRC64;
MDAASTLTHA PVSQPWQSLA QGLGFVNEHE GYWWSKLGPP LGKMMNWARY STSEQYRVLA
FLYKYLLPAC GPKPGDDGEL FWKVFISYDY TPIQLSLNFH NGKMTLRTAN IPISDKSGTA
DDPINQQASV DAIIRQERVL PSQDLRWFNH FASQYFFDKD TAASLKTKVD KLRVQQGVQC
MLSHDFPERD VQCKVAFCPL WKAVATGLSN KEIIWDSILG LGDDIIPYKR ALAVLEQYTS
SENAAKAGVR PVFFAFDTVL KDNYKSSRIK IYYLTTRTAF NSMVDIYTLG GLLKGPDIQK
GVEALEVLWK AVLNVPEGWP DDKDLPMNPH RCAAVIFNFE LWPGAEFPSP KAYLPAHYYG
RPDLEIADGM DYFFKQQGLD GVYGSYKENY LKCLSEVRTH RTNSQPSTMI FLFHSKGPMP
TLRCTTSPSY L
