IBOF_AMAMK
ID IBOF_AMAMK Reviewed; 535 AA.
AC A0A0C2WKN2;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-2015, sequence version 1.
DT 03-AUG-2022, entry version 20.
DE RecName: Full=Flavin-containing monooxygenase iboF {ECO:0000303|PubMed:32233056};
DE EC=1.8.-.- {ECO:0000305|PubMed:32233056};
DE AltName: Full=Ibotenic acid biosynthesis cluster protein F {ECO:0000303|PubMed:32233056};
DE Flags: Precursor;
GN Name=iboF {ECO:0000303|PubMed:32233056}; ORFNames=M378DRAFT_88862;
OS Amanita muscaria (strain Koide BX008).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Amanitaceae; Amanita.
OX NCBI_TaxID=946122;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Koide BX008;
RX PubMed=25706625; DOI=10.1038/ng.3223;
RG Mycorrhizal Genomics Initiative Consortium;
RA Kohler A., Kuo A., Nagy L.G., Morin E., Barry K.W., Buscot F., Canbaeck B.,
RA Choi C., Cichocki N., Clum A., Colpaert J., Copeland A., Costa M.D.,
RA Dore J., Floudas D., Gay G., Girlanda M., Henrissat B., Herrmann S.,
RA Hess J., Hoegberg N., Johansson T., Khouja H.R., LaButti K., Lahrmann U.,
RA Levasseur A., Lindquist E.A., Lipzen A., Marmeisse R., Martino E.,
RA Murat C., Ngan C.Y., Nehls U., Plett J.M., Pringle A., Ohm R.A.,
RA Perotto S., Peter M., Riley R., Rineau F., Ruytinx J., Salamov A., Shah F.,
RA Sun H., Tarkka M., Tritt A., Veneault-Fourrey C., Zuccaro A., Tunlid A.,
RA Grigoriev I.V., Hibbett D.S., Martin F.;
RT "Convergent losses of decay mechanisms and rapid turnover of symbiosis
RT genes in mycorrhizal mutualists.";
RL Nat. Genet. 47:410-415(2015).
RN [2]
RP FUNCTION, INDUCTION, AND PATHWAY.
RX PubMed=32233056; DOI=10.1002/anie.202001870;
RA Obermaier S., Mueller M.;
RT "Ibotenic acid biosynthesis in the fly agaric is initiated by glutamate
RT hydroxylation.";
RL Angew. Chem. Int. Ed. 59:12432-12435(2020).
CC -!- FUNCTION: Flavin-containing monooxygenase; part of the gene cluster
CC that mediates the biosynthesis of the psychoactive metabolites ibotenic
CC acid and muscimol (PubMed:32233056). The first committed step is
CC glutamate hydroxylation by the 2-oxoglutarate-dependent dioxygenase
CC iboH, and the last step is decarboxylation of ibotenic acid to muscimol
CC by the decarboxylase iboD (PubMed:32233056). The order of the
CC intermediate reactions is somewhat ambiguous (Probable). IboA likely
CC activates the carboxylic acid at position 5 to introduce an amide bond,
CC and the flavin monooxygenase iboF generates the N-O bond (Probable).
CC There are several options for the latter step (Probable). One option is
CC that iboF directly hydroxylates the amide nitrogen formed by iboA to
CC produce a hydroxamic acid species (Probable). Another option is that
CC iboF hydroxylates an external N-containing compound, whose resulting N-
CC O bond is subsequently introduced into the hydroxyglutamate scaffold
CC (Probable). The paralogous PLP-dependent cystathionine gamma-synthase-
CC like enzymes iboG1 and iboG2 are likely involved in substitution of the
CC OH group at position 3 by the O-N moiety (Probable). The first cyclic
CC intermediate is most probably tricholomic acid which is likely
CC desaturated to ibotenic acid by the cytochrome P450 monooxygenase iboC
CC (Probable). {ECO:0000269|PubMed:32233056, ECO:0000305|PubMed:32233056}.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000255};
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000305|PubMed:32233056}.
CC -!- INDUCTION: Expression is highly induced during artificial growth in
CC symbiosis with Populus, which is close to its natural condition.
CC {ECO:0000269|PubMed:32233056}.
CC -!- SIMILARITY: Belongs to the FMO family. {ECO:0000305}.
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DR EMBL; KN818402; KIL56733.1; -; Genomic_DNA.
DR EnsemblFungi; KIL56733; KIL56733; M378DRAFT_88862.
DR HOGENOM; CLU_006909_5_2_1; -.
DR OrthoDB; 405736at2759; -.
DR BioCyc; MetaCyc:MON-21261; -.
DR Proteomes; UP000054549; Unassembled WGS sequence.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0004499; F:N,N-dimethylaniline monooxygenase activity; IEA:InterPro.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR Gene3D; 3.50.50.60; -; 2.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR020946; Flavin_mOase-like.
DR Pfam; PF00743; FMO-like; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
PE 2: Evidence at transcript level;
KW FAD; Flavoprotein; Glycoprotein; Monooxygenase; NADP; Oxidoreductase;
KW Reference proteome; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..535
FT /note="Flavin-containing monooxygenase iboF"
FT /id="PRO_5002173634"
FT BINDING 60..65
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255"
FT BINDING 307..312
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255"
FT CARBOHYD 134
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 243
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 300
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 356
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 382
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 410
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 535 AA; 60266 MW; 4DECC930B3626396 CRC64;
MFSLRPTALV SLSVVLFSIQ ETLSEQQPFV SPGWSDQWWH KSELESYTFP WPIQKVAIIG
AGPSGLAAYH ELDKAGYDVY LFERDTVPGG NWHYTDETPV KEPIPNADVS IGDFVPSLPP
EGVRLPYEEH YEGNVSDELL RAHRGPKPIW NSLQTNAPPP LQQFRDHPWP ADQPWLLPHA
VLGKYIRAFA SFNGINSNDV ENPHISYNTR VELVEKCFTS TENGPMRTGW TLTLKQVSRT
GTNTSKAVWT KENFDAVVVA TGRFNAPYIP NILGLKAWAD RFPDRIVHSR QFRRPQLYTN
QTVLVVGAAA SGVEIATDIA PNARAVYLSI RPRRISNSNS AGNPLSSRWM GRLPHNVSVV
PEIKRFLPPT SAIALSSVEL TNGTILTGIE SIIFATGFRY TFPFLPQFHN TSLTNHDLEH
KPKPIVTDGT HLRNLFLDIL SIEEPTLGFM CMNIEIQNFK YAEYIAVALS KIWGNKATIP
PVTRLWELNE RRVMEKGGYG KYFQFLGFRG EREMIRLFTG WLNDAAASHG GRQVR
