IBOC_AMAMK
ID IBOC_AMAMK Reviewed; 561 AA.
AC A0A0C2W6G6;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-2015, sequence version 1.
DT 03-AUG-2022, entry version 21.
DE RecName: Full=Cytochrome P450 monooxygenase iboC {ECO:0000303|PubMed:32233056};
DE EC=1.-.-.- {ECO:0000305|PubMed:32233056};
DE AltName: Full=Ibotenic acid biosynthesis cluster protein C {ECO:0000303|PubMed:32233056};
GN Name=iboC {ECO:0000303|PubMed:32233056}; ORFNames=M378DRAFT_133714;
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: Cytochrome P450 monooxygenase; part of the gene cluster that
CC mediates the biosynthesis of the psychoactive metabolites ibotenic acid
CC and muscimol (PubMed:32233056). The first committed step is glutamate
CC hydroxylation by the 2-oxoglutarate-dependent dioxygenase iboH, and the
CC last step is decarboxylation of ibotenic acid to muscimol by the
CC decarboxylase iboD (PubMed:32233056). The order of the intermediate
CC reactions is somewhat ambiguous (Probable). IboA likely activates the
CC carboxylic acid at position 5 to introduce an amide bond, and the
CC flavin monooxygenase iboF generates the N-O bond (Probable). There are
CC several options for the latter step (Probable). One option is that iboF
CC directly hydroxylates the amide nitrogen formed by iboA to produce a
CC hydroxamic acid species (Probable). Another option is that iboF
CC hydroxylates an external N-containing compound, whose resulting N-O
CC 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=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000250|UniProtKB:P04798};
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000305|PubMed:32233056}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC protein {ECO:0000255}.
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 cytochrome P450 family. {ECO:0000305}.
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DR EMBL; KN818402; KIL56737.1; -; Genomic_DNA.
DR EnsemblFungi; KIL56737; KIL56737; M378DRAFT_133714.
DR HOGENOM; CLU_001570_2_3_1; -.
DR OrthoDB; 702827at2759; -.
DR BioCyc; MetaCyc:MON-21259; -.
DR Proteomes; UP000054549; Unassembled WGS sequence.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR Gene3D; 1.10.630.10; -; 1.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR002401; Cyt_P450_E_grp-I.
DR InterPro; IPR036396; Cyt_P450_sf.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00463; EP450I.
DR SUPFAM; SSF48264; SSF48264; 1.
PE 2: Evidence at transcript level;
KW Heme; Iron; Membrane; Metal-binding; Monooxygenase; Oxidoreductase;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..561
FT /note="Cytochrome P450 monooxygenase iboC"
FT /id="PRO_0000454916"
FT TRANSMEM 8..28
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 484
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:P04798"
SQ SEQUENCE 561 AA; 63122 MW; 49C2BB2845E45EC9 CRC64;
MTLQSESRFY YQLLAAVLIP ALFVAWAARL RQNRKYPPGP KGIPIFGNLF QLSTRPWIEF
SAFKEQYGPL VYLNIVGQPL LITNTHTAAT DLFDRRGGVY SDRPRSIVAD YLTGGLYLPF
ARHGPTWLKL RRAGHAFMHK GVAHKYRDTQ FKEALTLTHH LLQSPSGRRR QLFESAEASI
HSIVYDQPSS GGPVYPKMTD FSTLINKAVT PLFTPAEFLP LMQYVPSWLA GWKRRAQQGF
VLFSELCEGL LEEVAKRVDA GDDRPSMAGG LIREREKHGL TNLEAAWLSG MMILVGTETN
TLAMSWFLYA MIAYPDKQKR CQAELDAVVG RSRMPTFEDL EKLPYLRATI REILRWRPSI
PVGARHYTTK DDWYQGYFIP KGTICFPNVW SLNHDPAIYG TDADHFNPGR FIDKDGGLSP
AIPATKDGAF LIPHHDLHNS HGLNPPKMQK VCLRFIDLHT FRSKYPLSIA VPGHVSYGFG
SRICLGRHIA NDALFINFAS ILWATSISPA MNANTGKPDV PDKLAYSNLG LLIVPTTTEC
VIQPRFDEAE GILAQTRELC M
