IBOG2_AMAMK
ID IBOG2_AMAMK Reviewed; 628 AA.
AC A0A0C2S258;
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 iboG2 {ECO:0000303|PubMed:32233056};
DE EC=4.4.-.- {ECO:0000305|PubMed:32233056};
DE AltName: Full=Ibotenic acid biosynthesis cluster protein G2 {ECO:0000303|PubMed:32233056};
GN Name=iboG2 {ECO:0000303|PubMed:32233056}; ORFNames=M378DRAFT_88863;
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; KIL56740.1; -; Genomic_DNA.
DR STRING; 946122.A0A0C2S258; -.
DR EnsemblFungi; KIL56740; KIL56740; M378DRAFT_88863.
DR HOGENOM; CLU_011302_1_0_1; -.
DR OrthoDB; 764003at2759; -.
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..628
FT /note="Cystathionine gamma-synthase-like enzyme iboG2"
FT /id="PRO_0000454919"
FT BINDING 313
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P32929"
FT MOD_RES 417
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:P32929"
SQ SEQUENCE 628 AA; 68530 MW; FF4EE5BBF930DA3C CRC64;
MGLSRTMTAI QLNSSIPLGL PVPPHTPHAI SVSLPTWSET VAYKEGIKHI NDALLNGYPR
MFIQLNVRKL SSLLEQKFGI NGERCMLFPT YKVAEQCQLF MQARSVGARI VGLLICPEGK
QNNRVIECKE PANLSESTSS ASTNLYVVLF PPDMFSIANQ FWQHSGQGIS SRLTDHCLSI
LTENAAHANG SSLSPLTFPG NSHVAPEQLE VGHDVDLEGR CGGPLLADAA IAKQVLRQRI
AGLLIRYGSC DYRAELCVGK KNLEGNQNSR DFADVTENDV YLFPTGMTAI WNAHQLALAV
RPTAKSVCFG FPYSDTLKVL QKWGPGCHFF AGGTDSEIDE LEIILEQEFA RDSTKPPVLA
LFTEFPSNPL LCSPNLLRLR ALADKYDFLL AIDETIGNFV NVEVLPYADI LLTSLSKIFS
GNANVMGGSL VLNPNGRHYT ALKAHIAAHY QDIYYPEDAI HMEWNSRDFE QRIKIIDDNA
EAICDFLRPH SVAAGATNAV IKEVFYPKYI TPENYERCLT KGTNHDLSSS PSNGGGGYGG
LFSLTFTSGA ASAAFYDALS CFKGPSLGTN FTLACTYTLL AHFKELEWAA QYGVEAGLVR
ISVGTENTEA LLRTIEAALG AAKEAKGL
