IBOG1_AMAMK
ID IBOG1_AMAMK Reviewed; 605 AA.
AC A0A0C2WKN7;
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=Cystathionine gamma-synthase-like enzyme iboG1 {ECO:0000303|PubMed:32233056};
DE EC=4.4.-.- {ECO:0000305|PubMed:32233056};
DE AltName: Full=Ibotenic acid biosynthesis cluster protein G1 {ECO:0000303|PubMed:32233056};
GN Name=iboG1; ORFNames=M378DRAFT_28230;
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: Cystathionine gamma-synthase-like 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=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250|UniProtKB:P32929};
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 trans-sulfuration enzymes family.
CC {ECO:0000305}.
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DR EMBL; KN818402; KIL56738.1; -; Genomic_DNA.
DR SMR; A0A0C2WKN7; -.
DR STRING; 946122.A0A0C2WKN7; -.
DR EnsemblFungi; KIL56738; KIL56738; M378DRAFT_28230.
DR HOGENOM; CLU_011302_1_0_1; -.
DR OrthoDB; 764003at2759; -.
DR BioCyc; MetaCyc:MON-21262; -.
DR Proteomes; UP000054549; Unassembled WGS sequence.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0019346; P:transsulfuration; IEA:InterPro.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR InterPro; IPR000277; Cys/Met-Metab_PyrdxlP-dep_enz.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR Pfam; PF01053; Cys_Met_Meta_PP; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
PE 2: Evidence at transcript level;
KW Lyase; Pyridoxal phosphate; Reference proteome.
FT CHAIN 1..605
FT /note="Cystathionine gamma-synthase-like enzyme iboG1"
FT /id="PRO_0000454918"
FT BINDING 289
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P32929"
FT MOD_RES 393
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:P32929"
SQ SEQUENCE 605 AA; 66794 MW; 508D541EFFC92B77 CRC64;
MAIYQVIPYG LPVPPNTPHA ILVSLPTWND TVTCIEGEDA ETRLSGYPRF FIQVAIRKLA
SLMERKYGLD GERCMLFPSY RVAEQCRLFV QASFSGVRVV SLLVCQEDNK NARIVECKED
TGLSMQPASE NHLHIVLFPT DALPVAKLFW QFTGTGISSR FADHWLSTLP DDVVRTNGIS
GSTSVQYLTN KSPGDYSVGL ELTPLPDAAS AKYVLRQRIA GALNVYDRQG GPYAVQENLQ
VGPNSHGIAD VSENDVYLFP TGMCAIWNAH RLSLAVRSAE KSVCFGFVYC DTLKVLEKWG
PGCHFFPEGN DYDIDQLEVI LEQESARDST KPPILALYTE FPSNPLLRSP NLPRLRALAD
KYDFLMVIDD TLGNFVNVDV LPYADIVVTS LSKIFSGSAN VMGGSLVLNT NGHHYTALAA
YMTAHYEDTY YDEDAICMEQ NSRDLQQRIK IIDTNAEALC DFLRSHSVAA GAAKSVIKEV
FYPKYKTPEN YERCRKTVSN HNASLSSSNE VGGYGGLFSI TFISNAASRA FYESLDCFRA
PSLGTNFTLA VLYTILAHHD ELEWAAQCGV EEGLVRVSVG MENTETLLKV FEVALSTAKK
AVATA
