IBOA_AMAMK
ID IBOA_AMAMK Reviewed; 520 AA.
AC A0A0C2W6G2;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-2015, sequence version 1.
DT 03-AUG-2022, entry version 22.
DE RecName: Full=AMP-binding domain-containing enzyme iboA {ECO:0000303|PubMed:32233056};
DE EC=6.2.-.- {ECO:0000305|PubMed:32233056};
DE AltName: Full=Ibotenic acid biosynthesis cluster protein A {ECO:0000303|PubMed:32233056};
GN Name=iboA {ECO:0000303|PubMed:32233056}; ORFNames=M378DRAFT_88879;
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: AMP-binding domain-containing enzyme; part of the gene
CC cluster that mediates the biosynthesis of the psychoactive metabolites
CC ibotenic acid and muscimol (PubMed:32233056). The first committed step
CC is 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=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P30624};
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 -!- DOMAIN: The FACS motif is required for catalytic activity and substrate
CC specificity. {ECO:0000250|UniProtKB:P30624}.
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000305}.
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DR EMBL; KN818402; KIL56732.1; -; Genomic_DNA.
DR EnsemblFungi; KIL56732; KIL56732; M378DRAFT_88879.
DR HOGENOM; CLU_037349_1_0_1; -.
DR OrthoDB; 229565at2759; -.
DR BioCyc; MetaCyc:MON-21260; -.
DR Proteomes; UP000054549; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.12780; -; 1.
DR InterPro; IPR000873; AMP-dep_Synth/Lig.
DR InterPro; IPR042099; ANL_N_sf.
DR Pfam; PF00501; AMP-binding; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Ligase; Magnesium; Metal-binding; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..520
FT /note="AMP-binding domain-containing enzyme iboA"
FT /id="PRO_0000454917"
FT MOTIF 397..447
FT /note="FACS"
FT /evidence="ECO:0000250|UniProtKB:P30624"
FT BINDING 180..191
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P69451"
SQ SEQUENCE 520 AA; 57589 MW; 021EFB79E6EDB11E CRC64;
MDVALEDNHI ALLQHRAKNS GNTVLFKLPI LRGSEPPQEW NHITVAEFAA EVDRVAIFVM
TELKARGIPP RSAVTVLYSG SRYQDLIYAI ALARASYIPQ MCPHILTHPG VIFALMEKAG
SKIILYDPSL EPATTDCPYP KMALNPIETI DSSSTINSDS ALPTIEDLSS GHADVCFFYL
TSGSTSGSPK VVPLTQKFVS TYYKTQFGIW LDGRRFDTQN AFLSRGSICA VAPIIQYFGC
LYTGSCIVQP SKMRFSTEEL LTLVNVCGLN RMTTFGTWLA PHIQAAKKDP AALKLLQEMR
TVSYGGVPIS IADDDWCFQN GIPLMDMYAT TECGTLMVSA PGKPARFMQP VPGISYRFDP
FTDTTTGADN PASTQLLKLI LLADSPQIPQ PQLLSEDGNF HTGDLFEKQL DGSYLFRGRG
DDWIKSEDSR FIDTKAIEEK INDVCSDLVK GCIVVGHLRP SPALFIEAYH DSISTISEDG
LKELVLRRLE DFNARQLKHE RITDKRLIFI VDEGNLPRTV
