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PSIH_PSICY
ID   PSIH_PSICY              Reviewed;         507 AA.
AC   A0A286LF02;
DT   05-DEC-2018, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2017, sequence version 1.
DT   03-AUG-2022, entry version 10.
DE   RecName: Full=Tryptamine 4-monooxygenase {ECO:0000303|PubMed:28763571};
DE            EC=1.14.99.59 {ECO:0000250|UniProtKB:P0DPA7};
DE   AltName: Full=Cytochrome P450 monooxygenase psiH {ECO:0000303|PubMed:28763571};
DE   AltName: Full=Psilocybin biosynthesis hydroxylase {ECO:0000303|PubMed:28763571};
DE   Flags: Precursor;
GN   Name=psiH {ECO:0000303|PubMed:28763571};
OS   Psilocybe cyanescens.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Strophariaceae; Psilocybe.
OX   NCBI_TaxID=93625;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], IDENTIFICATION, FUNCTION, AND PATHWAY.
RC   STRAIN=FSU 12416;
RX   PubMed=28763571; DOI=10.1002/anie.201705489;
RA   Fricke J., Blei F., Hoffmeister D.;
RT   "Enzymatic synthesis of psilocybin.";
RL   Angew. Chem. Int. Ed. 56:12352-12355(2017).
RN   [2]
RP   FUNCTION.
RX   PubMed=30283667; DOI=10.1002/evl3.42;
RA   Reynolds H.T., Vijayakumar V., Gluck-Thaler E., Korotkin H.B.,
RA   Matheny P.B., Slot J.C.;
RT   "Horizontal gene cluster transfer increased hallucinogenic mushroom
RT   diversity.";
RL   Evol. Lett. 2:88-101(2018).
CC   -!- FUNCTION: Tryptamine 4-monooxygenase; part of the gene cluster that
CC       mediates the biosynthesis of psilocybin, a psychotropic tryptamine-
CC       derived natural product (PubMed:28763571, PubMed:30283667). The first
CC       step in the pathway is the decarboxylation of L-tryptophan to
CC       tryptamine by the decarboxylase psiD. PsiD does not decarboxylate
CC       phenylalanine, tyrosine, or 5-hydroxy- L -tryptophan (5-HTP)
CC       (PubMed:30283667). 4-hydroxy-L-tryptophan is accepted as substrate by
CC       psiD as well. The cytochrome P450 monooxygenase psiH then converts
CC       tryptamine to 4-hydroxytryptamine. The kinase psiK catalyzes the 4-O-
CC       phosphorylation step by converting 4-hydroxytryptamine into
CC       norbaeocystin. The methyltransferase psiM then catalyzes iterative
CC       methyl transfer to the amino group of norbaeocystin to yield psilocybin
CC       via a monomethylated intermediate, baeocystin. PsiK kinase can also
CC       turn psilocin into psilocybin. This activity may represent a protective
CC       mechanism to rephosphorylate the unstable psilocin to the stable
CC       psilocybin in case of intracellular ester cleavage (By similarity).
CC       {ECO:0000250|UniProtKB:P0DPA7, ECO:0000269|PubMed:28763571,
CC       ECO:0000269|PubMed:30283667}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=AH2 + O2 + tryptamine = 4-hydroxytryptamine + A + H2O;
CC         Xref=Rhea:RHEA:15865, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:17499, ChEBI:CHEBI:57887,
CC         ChEBI:CHEBI:139069; EC=1.14.99.59;
CC         Evidence={ECO:0000250|UniProtKB:P0DPA7};
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000250|UniProtKB:P04798};
CC   -!- PATHWAY: Secondary metabolite biosynthesis.
CC       {ECO:0000305|PubMed:28763571}.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; MF000997; ASU62250.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A286LF02; -.
DR   SMR; A0A286LF02; -.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR   GO; GO:0140382; F:tryptamine 4-monooxygenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0140380; P:psilocybin biosynthetic process; ISS:GO_Central.
DR   Gene3D; 1.10.630.10; -; 1.
DR   InterPro; IPR001128; Cyt_P450.
DR   InterPro; IPR017972; Cyt_P450_CS.
DR   InterPro; IPR002401; Cyt_P450_E_grp-I.
DR   InterPro; IPR036396; Cyt_P450_sf.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00463; EP450I.
DR   PRINTS; PR00385; P450.
DR   SUPFAM; SSF48264; SSF48264; 1.
DR   PROSITE; PS00086; CYTOCHROME_P450; 1.
PE   2: Evidence at transcript level;
KW   Heme; Iron; Metal-binding; Monooxygenase; Oxidoreductase; Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..507
FT                   /note="Tryptamine 4-monooxygenase"
FT                   /id="PRO_5012470929"
FT   REGION          403..425
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        404..425
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         439
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   507 AA;  57259 MW;  BC4356BCB738DF7C CRC64;
     MIVLLVSLVL AGCIYYANAR RVRRSRLPPG PPGIPLPFIG NMFDMPSESP WLRFLQWGRD
     YHTDILYLNA GGTEIIILNT LDAITDLLEK RGSMYSGRLE STMVNELMGW EFDLGFITYG
     ERWREERRMF AKEFSEKNIR QFRHAQIKAA NQLVRQLIKT PDRWSQHIRH QIAAMSLDIG
     YGIDLAEDDP WIAATQLANE GLAEASVPGS FWVDSFPALK YLPSWLPGAG FKRKAKVWKE
     GADHMVNMPY ETMKKLTVQG LARPSYASAR LQAMDPDGDL EHQEHVIRNT ATEVNVGGGD
     TTVSAVSAFI LAMVKYPEVQ RQVQAELDAL TSKGVVPNYD EEDDSLPYLT ACVKEIFRWN
     QIAPLAIPHR LIKDDVYRGY LIPKNALVYA NSWAVLNDPE EYPNPSEFRP ERYLSSDGKP
     DPTVRDPRKA AFGYGRRNCP GIHLAQSTVW IAGATLLSVF NIERPVDGNG KPIDIPATFT
     TGFFRHPEPF QCRFVPRTQE ILKSVSG
 
 
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