M1VV65 · TCPJ_CLAP2
- ProteinDipeptidase tcpJ
- GenetcpJ
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids425 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score3/5
Function
function
Dipeptidase; part of the gene cluster that mediates the biosynthesis of an unusual class of epipolythiodioxopiperazines (ETPs) lacking the reactive thiol group important for toxicity (PubMed:27390873).
Firstly, L-tyrosine is prenylated by tcpD, before undergoing condensation with L-glycine in a reaction catalyzed by the NRPS tcpP leading to the diketopiperazine (DKP) backbone (PubMed:27390873).
Afterwards the alpha-carbon of tyrosine is oxidized by the cytochrome P450 tcpC to form a hydroxyl group (PubMed:27390873).
However, in contrast other ETP biosynthesis pathways studied so far, tcpC is not able to bishydroxylate the DKP at both alpha-carbon positions, but hydroxylates the alpha-carbon of the tyrosine part and the nitrogen of the glycine part (PubMed:27390873).
The next steps involve an alpha,beta-elimination reaction catalyzed by tcpI, a methylation by the methyltransferase tcpN the action of the four enzyme cascade tcpG/K/J/I (PubMed:27390873).
Due to a dysfunctional cytochrome P450 monooxygenase tcpC, the pathway leads to the biosynthesis of probable non-toxic metabolites lacking the reactive thiol group (PubMed:27390873).
Firstly, L-tyrosine is prenylated by tcpD, before undergoing condensation with L-glycine in a reaction catalyzed by the NRPS tcpP leading to the diketopiperazine (DKP) backbone (PubMed:27390873).
Afterwards the alpha-carbon of tyrosine is oxidized by the cytochrome P450 tcpC to form a hydroxyl group (PubMed:27390873).
However, in contrast other ETP biosynthesis pathways studied so far, tcpC is not able to bishydroxylate the DKP at both alpha-carbon positions, but hydroxylates the alpha-carbon of the tyrosine part and the nitrogen of the glycine part (PubMed:27390873).
The next steps involve an alpha,beta-elimination reaction catalyzed by tcpI, a methylation by the methyltransferase tcpN the action of the four enzyme cascade tcpG/K/J/I (PubMed:27390873).
Due to a dysfunctional cytochrome P450 monooxygenase tcpC, the pathway leads to the biosynthesis of probable non-toxic metabolites lacking the reactive thiol group (PubMed:27390873).
Catalytic activity
- an L-aminoacyl-L-amino acid + H2O = 2 an L-alpha-amino acid
Cofactor
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 46 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Binding site | 48 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: D | ||||||
Binding site | 158 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: E | ||||||
Binding site | 185 | substrate | ||||
Sequence: H | ||||||
Binding site | 259 | substrate | ||||
Sequence: R | ||||||
Binding site | 318 | substrate | ||||
Sequence: D |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | metal ion binding | |
Molecular Function | metallodipeptidase activity | |
Biological Process | proteolysis |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameDipeptidase tcpJ
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Sordariomycetes > Hypocreomycetidae > Hypocreales > Clavicipitaceae > Claviceps
Accessions
- Primary accessionM1VV65
Proteomes
Organism-specific databases
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000437704 | 1-425 | Dipeptidase tcpJ | |||
Sequence: MATAAQPSLELALELMSKVPLIGNISQSTHKIPIQCTGLTREQDGHNDWMHMIRAYYDFQVDDRFQPTKDLAGHVDLKRLVQGRAGAVFWSVYVECPKGENDFSDAVHHASMRDTFQQIDLLQRIMELYSDRMEMAHKADDVMRIFRSGKCASLMGAEGLHQLGNSSSVLRIFHRLGVRYVTLAHAKNNLYVDSATSEAPIHHGLSPQGRDMVREMNRIGMIVDLSHVSEKAMVDALDVSLAPVIFSHSSAYALVPHVRNVPDHVLDRLKQNRGIIMISFIPWLTNKDPEKATVENVVDHVLHVGNRIGFDHLGLGSDFDGMPSHVQGLEDVSKYPNVVAAMLQRGISTENVEKIMGMNVIRVLREVEDVAASQKGLLPVLEDAVPQLWDDGIRAYVKKLYPHAEHDRTGASETTTVDKAIEKDV |
Expression
Induction
Expression is positively regulated by the thioclapurine cluster-specific transcription factor tcpZ (PubMed:27390873).
Structure
Sequence
- Sequence statusComplete
- Length425
- Mass (Da)47,461
- Last updated2013-05-01 v1
- Checksum0A786B472BC291E5
Keywords
- Technical term