ID   IBOD_AMAMK              Reviewed;         350 AA.
AC   A0A0C2SRU0;
DT   23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-2015, sequence version 1.
DT   03-AUG-2022, entry version 19.
DE   RecName: Full=Decarboxylase iboD {ECO:0000303|PubMed:32233056};
DE            EC=4.1.1.- {ECO:0000305|PubMed:32233056};
DE   AltName: Full=Ibotenic acid biosynthesis cluster protein D {ECO:0000303|PubMed:32233056};
GN   Name=iboD {ECO:0000303|PubMed:32233056}; ORFNames=M378DRAFT_172432;
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: Decarboxylase; part of the gene cluster that mediates the
CC       biosynthesis of the psychoactive metabolites ibotenic acid and muscimol
CC       (PubMed:32233056). The first committed step is glutamate hydroxylation
CC       by the 2-oxoglutarate-dependent dioxygenase iboH, and the last step is
CC       decarboxylation of ibotenic acid to muscimol by the decarboxylase iboD
CC       (PubMed:32233056). The order of the intermediate reactions is somewhat
CC       ambiguous (Probable). IboA likely activates the carboxylic acid at
CC       position 5 to introduce an amide bond, and the flavin monooxygenase
CC       iboF generates the N-O bond (Probable). There are several options for
CC       the latter step (Probable). One option is that iboF directly
CC       hydroxylates the amide nitrogen formed by iboA to produce a hydroxamic
CC       acid species (Probable). Another option is that iboF hydroxylates an
CC       external N-containing compound, whose resulting N-O bond is
CC       subsequently introduced into the hydroxyglutamate scaffold (Probable).
CC       The paralogous PLP-dependent cystathionine gamma-synthase-like enzymes
CC       iboG1 and iboG2 are likely involved in substitution of the OH group at
CC       position 3 by the O-N moiety (Probable). The first cyclic intermediate
CC       is most probably tricholomic acid which is likely desaturated to
CC       ibotenic acid by the cytochrome P450 monooxygenase iboC (Probable).
CC       {ECO:0000269|PubMed:32233056, ECO:0000305|PubMed:32233056}.
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 phosphatidylserine decarboxylase family.
CC       {ECO:0000305}.
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DR   EMBL; KN818402; KIL56734.1; -; Genomic_DNA.
DR   STRING; 946122.A0A0C2SRU0; -.
DR   EnsemblFungi; KIL56734; KIL56734; M378DRAFT_172432.
DR   HOGENOM; CLU_033450_0_0_1; -.
DR   OrthoDB; 1339756at2759; -.
DR   BioCyc; MetaCyc:MON-21263; -.
DR   Proteomes; UP000054549; Unassembled WGS sequence.
DR   GO; GO:0004609; F:phosphatidylserine decarboxylase activity; IEA:InterPro.
DR   GO; GO:0008654; P:phospholipid biosynthetic process; IEA:InterPro.
DR   InterPro; IPR003817; PS_Dcarbxylase.
DR   InterPro; IPR022237; PsiD-like.
DR   PANTHER; PTHR10067; PTHR10067; 1.
DR   Pfam; PF02666; PS_Dcarbxylase; 1.
DR   Pfam; PF12588; PSDC; 1.
PE   2: Evidence at transcript level;
KW   Decarboxylase; Lyase; Reference proteome.
FT   CHAIN           1..350
FT                   /note="Decarboxylase iboD"
FT                   /id="PRO_0000454920"
SQ   SEQUENCE   350 AA;  39046 MW;  B38BB3263216D3CB CRC64;
     MIDRLIVAPP EFQIYRDEHG NRLPRPFGLP ICLLFTYLCN TSAGYDLFRK PAFNTAMKTL
     LDSWGLYLTT KDSAKLLTDC EGGWFSEEAL QEFESDSRGK FEETYVCPDP DAVNRGFSSW
     DAFFTREVQP NARPVEAPDD KSVIHNPCES YLHCIARDVK CHDLFWLKGN IYSLYDMLNR
     DHKLAKQFVG GTIYQGFLSP VDYHRWRSPV DGTIKKTEIV AGTYYAALPD AGAPEGNQYQ
     AAGDLRGALK RSQTWLAMVA ARALVYIEAD NPDIGLVCFI AVGMVEVSTC EVTVKRGQKV
     SAGSELGMFH FGGSSFVLVF GPQACITFPE DVVLGKHVKL NSILARVHKA