Q4WQY6 · TPCL_ASPFU
- ProteinAnthrone oxygenase tpcL
- GenetpcL
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids161 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score3/5
Function
function
Anthrone oxygenase; part of the gene cluster that mediates the biosynthesis of trypacidin, a mycotoxin with antiprotozoal activity and that plays a role in the infection process (PubMed:26242966, PubMed:26278536).
The pathway begins with the synthesis of atrochrysone thioester by the polyketide synthase (PKS) tpcC (PubMed:26242966).
The atrochrysone carboxyl ACP thioesterase tpcB then breaks the thioester bond and releases the atrochrysone carboxylic acid from tpcC (PubMed:26242966).
The decarboxylase tpcK converts atrochrysone carboxylic acid to atrochrysone which is further reduced into emodin anthrone (PubMed:26242966).
The next step is performed by the emodin anthrone oxygenase tpcL that catalyzes the oxidation of emodinanthrone to emodin (PubMed:26242966).
Emodin O-methyltransferase encoded by tpcA catalyzes methylation of the 8-hydroxy group of emodin to form questin (PubMed:26242966).
Ring cleavage of questin by questin oxidase tpcI leads to desmethylsulochrin via several intermediates including questin epoxide (By similarity).
Another methylation step catalyzed by tpcM leads to the formation of sulochrin which is further converted to monomethylsulfochrin by tpcH. Finally, the tpcJ catalyzes the conversion of monomethylsulfochrin to trypacidin (PubMed:26242966).
Trypacidin is toxic for human pulmonary and bronchial epithelial cells by initiating the intracellular formation of nitric oxide (NO) and hydrogen peroxide (H2O2), thus triggering host necrotic cell death (PubMed:22319557).
The trypacidin pathway is also able to produce endocrocin via a distinct route from the endocrocin Enc pathway (PubMed:26242966).
The pathway begins with the synthesis of atrochrysone thioester by the polyketide synthase (PKS) tpcC (PubMed:26242966).
The atrochrysone carboxyl ACP thioesterase tpcB then breaks the thioester bond and releases the atrochrysone carboxylic acid from tpcC (PubMed:26242966).
The decarboxylase tpcK converts atrochrysone carboxylic acid to atrochrysone which is further reduced into emodin anthrone (PubMed:26242966).
The next step is performed by the emodin anthrone oxygenase tpcL that catalyzes the oxidation of emodinanthrone to emodin (PubMed:26242966).
Emodin O-methyltransferase encoded by tpcA catalyzes methylation of the 8-hydroxy group of emodin to form questin (PubMed:26242966).
Ring cleavage of questin by questin oxidase tpcI leads to desmethylsulochrin via several intermediates including questin epoxide (By similarity).
Another methylation step catalyzed by tpcM leads to the formation of sulochrin which is further converted to monomethylsulfochrin by tpcH. Finally, the tpcJ catalyzes the conversion of monomethylsulfochrin to trypacidin (PubMed:26242966).
Trypacidin is toxic for human pulmonary and bronchial epithelial cells by initiating the intracellular formation of nitric oxide (NO) and hydrogen peroxide (H2O2), thus triggering host necrotic cell death (PubMed:22319557).
The trypacidin pathway is also able to produce endocrocin via a distinct route from the endocrocin Enc pathway (PubMed:26242966).
Catalytic activity
- emodin anthrone + O2 = emodin + H+ + H2OThis reaction proceeds in the forward direction.
Pathway
Secondary metabolite biosynthesis.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | membrane | |
Molecular Function | monooxygenase activity | |
Biological Process | secondary metabolite biosynthetic process |
Keywords
- Molecular function
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameAnthrone oxygenase tpcL
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Eurotiomycetes > Eurotiomycetidae > Eurotiales > Aspergillaceae > Aspergillus > Aspergillus subgen. Fumigati
Accessions
- Primary accessionQ4WQY6
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Membrane ; Multi-pass membrane protein
Features
Showing features for transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transmembrane | 15-35 | Helical | ||||
Sequence: VITGSFLSGLMMGLSVVDIPV | ||||||
Transmembrane | 56-74 | Helical | ||||
Sequence: IGHKMMPSLAVTTCLLYGY | ||||||
Transmembrane | 87-107 | Helical | ||||
Sequence: LPHIIAAVTTISMVPFTWLVM | ||||||
Transmembrane | 136-155 | Helical | ||||
Sequence: WAQLHAVRSLFPLMGSVLGL |
Keywords
- Cellular component
PTM/Processing
Features
Showing features for chain, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000437098 | 1-161 | Anthrone oxygenase tpcL | |||
Sequence: MPQNASVIITQATAVITGSFLSGLMMGLSVVDIPVVLDTATQASQLLQHFTRLYDIGHKMMPSLAVTTCLLYGYTASSTRTTGGSGLPHIIAAVTTISMVPFTWLVMAPTNNALFRMHANPAAANLGEVRRLLVRWAQLHAVRSLFPLMGSVLGLRQILRE | ||||||
Glycosylation | 4 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Keywords
- PTM
PTM databases
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Sequence similarities
Belongs to the anthrone oxygenase family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length161
- Mass (Da)17,361
- Last updated2007-04-17 v2
- Checksum4EF73E3BB7043B9E
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AAHF01000005 EMBL· GenBank· DDBJ | EAL89348.2 EMBL· GenBank· DDBJ | Genomic DNA |