TCPD_CLAP2
ID TCPD_CLAP2 Reviewed; 444 AA.
AC M1VV66;
DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2013, sequence version 1.
DT 03-AUG-2022, entry version 27.
DE RecName: Full=4-O-dimethylallyl-L-tyrosine synthase {ECO:0000250|UniProtKB:Q6Q874};
DE EC=2.5.1.122 {ECO:0000250|UniProtKB:Q6Q874};
DE AltName: Full=Thioclapurine biosynthesis protein D {ECO:0000303|PubMed:27390873};
DE AltName: Full=Tyrosine O-prenyltransferase tcpD {ECO:0000250|UniProtKB:Q6Q874};
GN Name=tcpD {ECO:0000303|PubMed:27390873}; ORFNames=CPUR_02678;
OS Claviceps purpurea (strain 20.1) (Ergot fungus) (Sphacelia segetum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Claviceps.
OX NCBI_TaxID=1111077;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=20.1;
RX PubMed=23468653; DOI=10.1371/journal.pgen.1003323;
RA Schardl C.L., Young C.A., Hesse U., Amyotte S.G., Andreeva K., Calie P.J.,
RA Fleetwood D.J., Haws D.C., Moore N., Oeser B., Panaccione D.G.,
RA Schweri K.K., Voisey C.R., Farman M.L., Jaromczyk J.W., Roe B.A.,
RA O'Sullivan D.M., Scott B., Tudzynski P., An Z., Arnaoudova E.G.,
RA Bullock C.T., Charlton N.D., Chen L., Cox M., Dinkins R.D., Florea S.,
RA Glenn A.E., Gordon A., Gueldener U., Harris D.R., Hollin W., Jaromczyk J.,
RA Johnson R.D., Khan A.K., Leistner E., Leuchtmann A., Li C., Liu J., Liu J.,
RA Liu M., Mace W., Machado C., Nagabhyru P., Pan J., Schmid J., Sugawara K.,
RA Steiner U., Takach J.E., Tanaka E., Webb J.S., Wilson E.V., Wiseman J.L.,
RA Yoshida R., Zeng Z.;
RT "Plant-symbiotic fungi as chemical engineers: Multi-genome analysis of the
RT Clavicipitaceae reveals dynamics of alkaloid loci.";
RL PLoS Genet. 9:E1003323-E1003323(2013).
RN [2]
RP FUNCTION, AND INDUCTION.
RX PubMed=27390873; DOI=10.1371/journal.pone.0158945;
RA Dopstadt J., Neubauer L., Tudzynski P., Humpf H.U.;
RT "The epipolythiodiketopiperazine gene cluster in Claviceps purpurea:
RT dysfunctional cytochrome P450 enzyme prevents formation of the previously
RT unknown clapurines.";
RL PLoS ONE 11:E0158945-E0158945(2016).
CC -!- FUNCTION: 4-O-dimethylallyl-L-tyrosine synthase; part of the gene
CC cluster that mediates the biosynthesis of an unusual class of
CC epipolythiodioxopiperazines (ETPs) lacking the reactive thiol group
CC important for toxicity (PubMed:27390873). Firstly, L-tyrosine is
CC prenylated by tcpD, before undergoing condensation with L-glycine in a
CC reaction catalyzed by the NRPS tcpP leading to the diketopiperazine
CC (DKP) backbone (PubMed:27390873). Afterwards the alpha-carbon of
CC tyrosine is oxidized by the cytochrome P450 tcpC to form a hydroxyl
CC group (PubMed:27390873). However, in contrast other ETP biosynthesis
CC pathways studied so far, tcpC is not able to bishydroxylate the DKP at
CC both alpha-carbon positions, but hydroxylates the alpha-carbon of the
CC tyrosine part and the nitrogen of the glycine part (PubMed:27390873).
CC The next steps involve an alpha,beta-elimination reaction catalyzed by
CC tcpI, a methylation by the methyltransferase tcpN the action of the
CC four enzyme cascade tcpG/K/J/I (PubMed:27390873). Due to a
CC dysfunctional cytochrome P450 monooxygenase tcpC, the pathway leads to
CC the biosynthesis of probable non-toxic metabolites lacking the reactive
CC thiol group (PubMed:27390873). {ECO:0000269|PubMed:27390873}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dimethylallyl diphosphate + L-tyrosine = 4-O-dimethylallyl-L-
CC tyrosine + diphosphate; Xref=Rhea:RHEA:41584, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:57623, ChEBI:CHEBI:58315, ChEBI:CHEBI:78314;
CC EC=2.5.1.122; Evidence={ECO:0000250|UniProtKB:Q6Q874};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q6Q874}.
CC -!- INDUCTION: Expression is positively regulated by the thioclapurine
CC cluster-specific transcription factor tcpZ (PubMed:27390873).
CC {ECO:0000269|PubMed:27390873}.
CC -!- SIMILARITY: Belongs to the tryptophan dimethylallyltransferase family.
CC {ECO:0000305}.
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DR EMBL; CAGA01000011; CCE28987.1; -; Genomic_DNA.
DR AlphaFoldDB; M1VV66; -.
DR SMR; M1VV66; -.
DR EnsemblFungi; CCE28987; CCE28987; CPUR_02678.
DR VEuPathDB; FungiDB:CPUR_02678; -.
DR eggNOG; ENOG502S2XP; Eukaryota.
DR HOGENOM; CLU_037431_2_2_1; -.
DR OrthoDB; 1531660at2759; -.
DR Proteomes; UP000016801; Unassembled WGS sequence.
DR GO; GO:0004659; F:prenyltransferase activity; IEA:UniProt.
DR GO; GO:0009820; P:alkaloid metabolic process; IEA:InterPro.
DR GO; GO:0044249; P:cellular biosynthetic process; IEA:UniProt.
DR GO; GO:1901576; P:organic substance biosynthetic process; IEA:UniProt.
DR CDD; cd13929; PT-DMATS_CymD; 1.
DR InterPro; IPR033964; Aro_prenylTrfase.
DR InterPro; IPR017795; Aro_prenylTrfase_DMATS.
DR InterPro; IPR012148; DMATS-type_fun.
DR PANTHER; PTHR40627; PTHR40627; 1.
DR Pfam; PF11991; Trp_DMAT; 1.
DR PIRSF; PIRSF000509; Trp_DMAT; 1.
DR SFLD; SFLDS00036; Aromatic_Prenyltransferase; 1.
DR TIGRFAMs; TIGR03429; arom_pren_DMATS; 1.
PE 2: Evidence at transcript level;
KW Reference proteome; Transferase.
FT CHAIN 1..444
FT /note="4-O-dimethylallyl-L-tyrosine synthase"
FT /id="PRO_0000437699"
SQ SEQUENCE 444 AA; 50485 MW; 38A828DD15001CFB CRC64;
MPFMFETILS RVKWTANTLV ARLTTLYEYE YPRTAKEETG IDKEYHIKLW DEDIGAMLVS
MMRLAGYSEQ SQKTHRIFFK EQVARSLGLY PTTYPHQSAW ESFMTDDHTP VEMSWSWSGN
TPTPVVRYAA EPISWHAGTA SDPLNSEATT ECLASTAPLA PSLDLRWYRH FLKHLVADDS
DGQHDTTDHL SQEFIAFDLD KDSMTVKYYF LPTLKSLACG KTNLELMEES ILSLPEADEA
VRSSLKVLTT YIRAYPQDEQ PQAEIFAVDC VNPANSRLKI YVRSRKTTFD SMLEMMTLGG
QTPDLTRDAI DSLRELWCAC FALPNNPSVT SKPLRSKEHR TGGLLYYFEL RPGAALPTSK
VYLPVRHYGK TDDQIARGLS SYLYKRGQCL EGGLSYYEGV RRICKHRSLK QGLGFQTYIT
CAVKKGVVSV NAYFNPETCQ YSRG
