A7XRY8 · TDID_EMENI
- ProteinAminotransferase tdiD
- GenetdiD
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids436 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
Function
function
Aminotransferase; part of the gene cluster that mediates the biosynthesis of terrequinone A, an antitumor agent (PubMed:16426969, PubMed:17291795, PubMed:17704773, PubMed:22083274).
The first step in the biosynthetic pathway for terrequinone A is formation of indole pyruvic acid (IPA) from L-tryptophan by the aminotransferase tdiD (PubMed:17704773).
The nonribosomal peptide synthase tdiA then immediately converts unstable IPA to didemethylasterriquinone D (DDAQ D), via condensation of 2 IPA molecules (PubMed:17704773).
The symmetric connectivity of the 2 IPA molecules is thought to arise by head-to-tail dual Claisen condensations facilitated by the TE domain (PubMed:17704773).
TdiB then catalyzes reverse prenylation by transferring dimethylallyl diphosphate to carbon atom 2' of DDAQ D, to yield asterriquinone C-1 (PubMed:18029206).
Finally, tdiC and tdiE enzymes robustly convert asterriquinone C-1 to terrequinone A via a transformation involving regular prenylation at carbon atom 5, which requires elimination of the hydroxy group on C-5 (PubMed:17704773, PubMed:18029206).
The first step in the biosynthetic pathway for terrequinone A is formation of indole pyruvic acid (IPA) from L-tryptophan by the aminotransferase tdiD (PubMed:17704773).
The nonribosomal peptide synthase tdiA then immediately converts unstable IPA to didemethylasterriquinone D (DDAQ D), via condensation of 2 IPA molecules (PubMed:17704773).
The symmetric connectivity of the 2 IPA molecules is thought to arise by head-to-tail dual Claisen condensations facilitated by the TE domain (PubMed:17704773).
TdiB then catalyzes reverse prenylation by transferring dimethylallyl diphosphate to carbon atom 2' of DDAQ D, to yield asterriquinone C-1 (PubMed:18029206).
Finally, tdiC and tdiE enzymes robustly convert asterriquinone C-1 to terrequinone A via a transformation involving regular prenylation at carbon atom 5, which requires elimination of the hydroxy group on C-5 (PubMed:17704773, PubMed:18029206).
Catalytic activity
- 3-phenylpyruvate + L-tryptophan = indole-3-pyruvate + L-phenylalanineThis reaction proceeds in the forward direction.
Cofactor
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
198 μM | L-tryptophan |
Pathway
Secondary metabolite biosynthesis.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 30 | substrate | ||||
Sequence: R | ||||||
Binding site | 86 | substrate | ||||
Sequence: Y | ||||||
Binding site | 148 | substrate | ||||
Sequence: Y | ||||||
Binding site | 202 | substrate | ||||
Sequence: N | ||||||
Binding site | 407 | substrate | ||||
Sequence: R |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | L-tryptophan aminotransferase activity | |
Molecular Function | pyridoxal phosphate binding | |
Molecular Function | transaminase activity | |
Molecular Function | tryptophan-phenylpyruvate transaminase activity | |
Biological Process | alpha-amino acid metabolic process | |
Biological Process | terrequinone A biosynthetic process |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameAminotransferase tdiD
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Eurotiomycetes > Eurotiomycetidae > Eurotiales > Aspergillaceae > Aspergillus > Aspergillus subgen. Nidulantes
Accessions
- Primary accessionA7XRY8
- Secondary accessions
Proteomes
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000436367 | 1-436 | Aminotransferase tdiD | |||
Sequence: MGSIGANNAVADPTPLFSSRVQKWEPGAIRSLLPLEALPGMISLVAGKPSPETFPIAEIAISLKDTPAGTGRIVVDGDELNQALQYGLPRGNAQLIQWFESLQRSVHGLDENGGWSCCIGNGSQELIHRVIQVFTDPGDPVLLETPAYPGVAGFLRADGQELIPVYSDAQGLNPASLEQALSEWPGDSPRPKVLYTTPTGSNPTGQSCTESRKAEILRLAKRFNFIILEDDAYYYLNYGDDKQRARSYLALERDVNGESGRVVRFDSLSKIVSPGMRLGILTAQAAVVDKVVRITENINLQPSSTTQLLALSLLRHWGQAGFLKHCAEAAEVYRRRRDVFVSAAERHLQGRATWVVPTAGMFVWLELKLPPEMDSFELLKSQGMKNGVLAIPGVAFMPGNEQTCYIRVSFSLVPERDMDEACRRIAGLVDRCACHS | ||||||
Modified residue | 270 | N6-(pyridoxal phosphate)lysine | ||||
Sequence: K |
Interaction
Protein-protein interaction databases
Structure
Sequence
- Sequence statusComplete
- Length436
- Mass (Da)47,705
- Last updated2007-10-23 v1
- Checksum015F606F1A48EDD8
Sequence caution
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
EF550584 EMBL· GenBank· DDBJ | ABU51605.1 EMBL· GenBank· DDBJ | mRNA | ||
BN001305 EMBL· GenBank· DDBJ | CBF80716.1 EMBL· GenBank· DDBJ | Genomic DNA | Sequence problems. | |
AACD01000154 EMBL· GenBank· DDBJ | EAA66860.1 EMBL· GenBank· DDBJ | Genomic DNA | Sequence problems. | |
AACD01000155 EMBL· GenBank· DDBJ | EAA66872.1 EMBL· GenBank· DDBJ | Genomic DNA | Sequence problems. |