IBOH_AMAMK
ID IBOH_AMAMK Reviewed; 206 AA.
AC A0A0C2SRU5;
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=2-oxoglutarate-dependent dioxygenase iboH {ECO:0000303|PubMed:32233056};
DE EC=1.14.11.76 {ECO:0000269|PubMed:32233056};
DE AltName: Full=Ibotenic acid biosynthesis cluster protein H {ECO:0000303|PubMed:32233056};
GN Name=iboH {ECO:0000303|PubMed:32233056}; ORFNames=M378DRAFT_172437;
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, CATALYTIC ACTIVITY, 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: 2-oxoglutarate-dependent dioxygenase; 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 -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + L-glutamate + O2 = (3R)-3-hydroxy-L-glutamate
CC + CO2 + succinate; Xref=Rhea:RHEA:65752, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985,
CC ChEBI:CHEBI:30031, ChEBI:CHEBI:155841; EC=1.14.11.76;
CC Evidence={ECO:0000269|PubMed:32233056};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65753;
CC Evidence={ECO:0000269|PubMed:32233056};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00805};
CC Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000255|PROSITE-
CC ProRule:PRU00805};
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000269|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 iron/ascorbate-dependent oxidoreductase
CC family. {ECO:0000305}.
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DR EMBL; KN818402; KIL56739.1; -; Genomic_DNA.
DR SMR; A0A0C2SRU5; -.
DR EnsemblFungi; KIL56739; KIL56739; M378DRAFT_172437.
DR KEGG; ag:KIL56739; -.
DR HOGENOM; CLU_110772_0_0_1; -.
DR OrthoDB; 622449at2759; -.
DR BioCyc; MetaCyc:MON-21258; -.
DR BRENDA; 1.14.11.76; 7508.
DR Proteomes; UP000054549; Unassembled WGS sequence.
DR GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 2.60.120.330; -; 1.
DR InterPro; IPR044861; IPNS-like_FE2OG_OXY.
DR InterPro; IPR027443; IPNS-like_sf.
DR InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
DR Pfam; PF03171; 2OG-FeII_Oxy; 1.
DR PROSITE; PS51471; FE2OG_OXY; 1.
PE 1: Evidence at protein level;
KW Dioxygenase; Iron; Metal-binding; Oxidoreductase; Reference proteome.
FT CHAIN 1..206
FT /note="2-oxoglutarate-dependent dioxygenase iboH"
FT /id="PRO_0000454915"
FT DOMAIN 51..157
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 75
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 77
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 134
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 148
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
SQ SEQUENCE 206 AA; 23686 MW; 16154BC0A2651D3B CRC64;
MPPTIRNNFP LFHDFVTASH FITQTILMRL SDAMYLEGST RFENSHREDK PSTTTLVLLH
YPKNFDNAHS GHNKHTDIGS LTLLFTPQWG LQLLSPIQKS KSWLWVQPRP GHAVINVGDS
LRFLSGKRLK SCLHRVYPTG EVYQEEDRYS IAYFLRPESA ANFEDVDGKV VSAKRWHDEK
YVTYTEPHEK QDLSNILTGG MDQILA
