TCPJ_CLAP2
ID TCPJ_CLAP2 Reviewed; 425 AA.
AC M1VV65;
DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2013, sequence version 1.
DT 03-AUG-2022, entry version 30.
DE RecName: Full=Dipeptidase tcpJ {ECO:0000305};
DE EC=3.4.13.19 {ECO:0000255|PROSITE-ProRule:PRU10073};
DE AltName: Full=Thiocalpurine biosynthesis protein J {ECO:0000303|PubMed:27390873};
GN Name=tcpJ {ECO:0000303|PubMed:27390873}; ORFNames=CPUR_02673;
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: Dipeptidase; part of the gene cluster that mediates the
CC biosynthesis of an unusual class of epipolythiodioxopiperazines (ETPs)
CC lacking the reactive thiol group important for toxicity
CC (PubMed:27390873). Firstly, L-tyrosine is prenylated by tcpD, before
CC undergoing condensation with L-glycine in a reaction catalyzed by the
CC NRPS tcpP leading to the diketopiperazine (DKP) backbone
CC (PubMed:27390873). Afterwards the alpha-carbon of tyrosine is oxidized
CC by the cytochrome P450 tcpC to form a hydroxyl group (PubMed:27390873).
CC However, in contrast other ETP biosynthesis pathways studied so far,
CC tcpC is not able to bishydroxylate the DKP at both alpha-carbon
CC positions, but hydroxylates the alpha-carbon of the tyrosine part and
CC the nitrogen of the glycine part (PubMed:27390873). The next steps
CC involve an alpha,beta-elimination reaction catalyzed by tcpI, a
CC methylation by the methyltransferase tcpN the action of the four enzyme
CC cascade tcpG/K/J/I (PubMed:27390873). Due to a dysfunctional cytochrome
CC P450 monooxygenase tcpC, the pathway leads to the biosynthesis of
CC probable non-toxic metabolites lacking the reactive thiol group
CC (PubMed:27390873). {ECO:0000269|PubMed:27390873}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an L-aminoacyl-L-amino acid + H2O = 2 an L-alpha-amino acid;
CC Xref=Rhea:RHEA:48940, ChEBI:CHEBI:15377, ChEBI:CHEBI:59869,
CC ChEBI:CHEBI:77460; EC=3.4.13.19; Evidence={ECO:0000255|PROSITE-
CC ProRule:PRU10073};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10073};
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 metallo-dependent hydrolases superfamily.
CC Peptidase M19 family. {ECO:0000255|PROSITE-ProRule:PRU10073}.
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DR EMBL; CAGA01000011; CCE28982.1; -; Genomic_DNA.
DR AlphaFoldDB; M1VV65; -.
DR SMR; M1VV65; -.
DR STRING; 1111077.M1VV65; -.
DR EnsemblFungi; CCE28982; CCE28982; CPUR_02673.
DR VEuPathDB; FungiDB:CPUR_02673; -.
DR eggNOG; KOG4127; Eukaryota.
DR HOGENOM; CLU_031404_4_0_1; -.
DR OrthoDB; 1272387at2759; -.
DR Proteomes; UP000016801; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0070573; F:metallodipeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd01301; rDP_like; 1.
DR InterPro; IPR032466; Metal_Hydrolase.
DR InterPro; IPR008257; Pept_M19.
DR PANTHER; PTHR10443; PTHR10443; 1.
DR Pfam; PF01244; Peptidase_M19; 1.
DR SUPFAM; SSF51556; SSF51556; 1.
DR PROSITE; PS51365; RENAL_DIPEPTIDASE_2; 1.
PE 2: Evidence at transcript level;
KW Dipeptidase; Hydrolase; Metal-binding; Metalloprotease; Protease;
KW Reference proteome; Zinc.
FT CHAIN 1..425
FT /note="Dipeptidase tcpJ"
FT /id="PRO_0000437704"
FT BINDING 46
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10073"
FT BINDING 48
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10073"
FT BINDING 158
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10073"
FT BINDING 185
FT /ligand="substrate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10073"
FT BINDING 259
FT /ligand="substrate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10073"
FT BINDING 318
FT /ligand="substrate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10073"
SQ SEQUENCE 425 AA; 47461 MW; 0A786B472BC291E5 CRC64;
MATAAQPSLE LALELMSKVP LIGNISQSTH KIPIQCTGLT REQDGHNDWM HMIRAYYDFQ
VDDRFQPTKD LAGHVDLKRL VQGRAGAVFW SVYVECPKGE NDFSDAVHHA SMRDTFQQID
LLQRIMELYS DRMEMAHKAD DVMRIFRSGK CASLMGAEGL HQLGNSSSVL RIFHRLGVRY
VTLAHAKNNL YVDSATSEAP IHHGLSPQGR DMVREMNRIG MIVDLSHVSE KAMVDALDVS
LAPVIFSHSS AYALVPHVRN VPDHVLDRLK QNRGIIMISF IPWLTNKDPE KATVENVVDH
VLHVGNRIGF DHLGLGSDFD GMPSHVQGLE DVSKYPNVVA AMLQRGISTE NVEKIMGMNV
IRVLREVEDV AASQKGLLPV LEDAVPQLWD DGIRAYVKKL YPHAEHDRTG ASETTTVDKA
IEKDV
