ID   TCPI_CLAP2              Reviewed;         425 AA.
AC   M1W859;
DT   02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2013, sequence version 1.
DT   25-MAY-2022, entry version 28.
DE   RecName: Full=Probable aminotransferase tcpI {ECO:0000250|UniProtKB:Q4WMJ9};
DE            EC=2.6.1.- {ECO:0000250|UniProtKB:Q4WMJ9};
DE   AltName: Full=Thioclapurine biosynthesis protein I {ECO:0000303|PubMed:27390873};
GN   Name=tcpI {ECO:0000303|PubMed:27390873}; ORFNames=CPUR_02679;
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: Probable aminotransferase; 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   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000250|UniProtKB:P00509};
CC   -!- PATHWAY: Secondary metabolite biosynthesis.
CC       {ECO:0000305|PubMed:27390873}.
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 class-I pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000255}.
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DR   EMBL; CAGA01000011; CCE28988.1; -; Genomic_DNA.
DR   AlphaFoldDB; M1W859; -.
DR   SMR; M1W859; -.
DR   STRING; 1111077.M1W859; -.
DR   EnsemblFungi; CCE28988; CCE28988; CPUR_02679.
DR   VEuPathDB; FungiDB:CPUR_02679; -.
DR   eggNOG; KOG0256; Eukaryota.
DR   HOGENOM; CLU_017584_1_2_1; -.
DR   OrthoDB; 1156861at2759; -.
DR   PhylomeDB; M1W859; -.
DR   Proteomes; UP000016801; Unassembled WGS sequence.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR   GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 1.
DR   InterPro; IPR004839; Aminotransferase_I/II.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
PE   2: Evidence at transcript level;
KW   Aminotransferase; Pyridoxal phosphate; Reference proteome; Transferase.
FT   CHAIN           1..425
FT                   /note="Probable aminotransferase tcpI"
FT                   /id="PRO_0000437721"
FT   MOD_RES         256
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250|UniProtKB:P00509"
SQ   SEQUENCE   425 AA;  47106 MW;  C20C614E2F989EF9 CRC64;
     MMSKRCLKRN QTLIPELLKN HGALLYGDTS VVDLSTAENQ LLMEELLPEF QAAFDANTWS
     SQELAYSEGV GGCPKVRGLI ADLVNSHFQP HAQVDKSHIV LGAGGCFALN ALIEAICDPG
     DGILIAAPYW PGLDLSISVH NDAKAVVVRV PHEDFFRVES IRHYSKALLS APNLVKAMII
     CNPHNPLGRN YPRETLQAIV DFCAERQIHL ISDEVYALSQ HVQPTSENPS AGFVSALSLD
     ASHARGLVHV VYSLSKDFGC NGIRLGAFIS QDNKAVVMSG ALSTHCQTST MATLVAQKII
     LTDENIQFVN TYGRGLLKSA YTVMEEFLNQ HRIEFVSAEC GMYIFAKLCG DRTSVDDEWL
     FQAILRRNGL VLSAGTDYHC KTPGWFRICY GCDREKLRHG LDRLRDCLQE FGETEFKFPF
     NDACF