TCPG_CLAP2
ID TCPG_CLAP2 Reviewed; 249 AA.
AC M1W426;
DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2013, sequence version 1.
DT 25-MAY-2022, entry version 34.
DE RecName: Full=Glutathione S-transferase tcpG {ECO:0000303|PubMed:27390873};
DE EC=2.5.1.18 {ECO:0000305|PubMed:27390873};
DE AltName: Full=Thioclapurine biosynthesis protein G {ECO:0000303|PubMed:27390873};
GN Name=tcpG {ECO:0000303|PubMed:27390873}; ORFNames=CPUR_02676;
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: Glutathione S-transferase; part of the gene cluster that
CC 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=glutathione + RX = a halide anion + an S-substituted
CC glutathione + H(+); Xref=Rhea:RHEA:16437, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16042, ChEBI:CHEBI:17792, ChEBI:CHEBI:57925,
CC ChEBI:CHEBI:90779; EC=2.5.1.18;
CC Evidence={ECO:0000305|PubMed:27390873};
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000305|PubMed:27390873}.
CC -!- INDUCTION: Expression is increases towards the late stages of rye
CC plants infection (PubMed:27390873). Expression is positively regulated
CC by the thioclapurine cluster-specific transcription factor tcpZ
CC (PubMed:27390873). {ECO:0000269|PubMed:27390873}.
CC -!- SIMILARITY: Belongs to the GST superfamily. {ECO:0000305}.
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DR EMBL; CAGA01000011; CCE28985.1; -; Genomic_DNA.
DR AlphaFoldDB; M1W426; -.
DR SMR; M1W426; -.
DR STRING; 1111077.M1W426; -.
DR EnsemblFungi; CCE28985; CCE28985; CPUR_02676.
DR VEuPathDB; FungiDB:CPUR_02676; -.
DR eggNOG; ENOG502SRT0; Eukaryota.
DR HOGENOM; CLU_011226_14_2_1; -.
DR OrthoDB; 1231780at2759; -.
DR PhylomeDB; M1W426; -.
DR Proteomes; UP000016801; Unassembled WGS sequence.
DR GO; GO:0004364; F:glutathione transferase activity; IEA:UniProtKB-EC.
DR GO; GO:0006749; P:glutathione metabolic process; IEA:InterPro.
DR InterPro; IPR010987; Glutathione-S-Trfase_C-like.
DR InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR InterPro; IPR040079; Glutathione_S-Trfase.
DR InterPro; IPR004045; Glutathione_S-Trfase_N.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR Pfam; PF13417; GST_N_3; 1.
DR SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1.
DR SUPFAM; SSF47616; SSF47616; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR PROSITE; PS50405; GST_CTER; 1.
DR PROSITE; PS50404; GST_NTER; 1.
PE 2: Evidence at transcript level;
KW Reference proteome; Transferase.
FT CHAIN 1..249
FT /note="Glutathione S-transferase tcpG"
FT /id="PRO_0000437726"
FT DOMAIN 20..109
FT /note="GST N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00684"
FT DOMAIN 115..249
FT /note="GST C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00685"
SQ SEQUENCE 249 AA; 28456 MW; 602611604899E39D CRC64;
MEAQQDFTKH PEVAQDRLVL YVRKAIPAPT ANSLKPLMIL EALEIPYSIH LISSLSQETW
YHEINPYKQL PALEDIDLVE TSGGSKRRLN VFDSSAMLIY LCDKHDKDGL FIGRNATERA
QVTSWLIAYA AGLGATGEWW LKMRHDENLK PALRVIENAI RREYDILEKR LGEPGQRWIA
LADRPTVADF AIQPLANPRV ARNAAIDFEA WPRTKAWSEA VDRLAYIDRA KRLNNKLGMT
EEEIELHGR
