A7XRY8 · TDID_EMENI

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).

Catalytic activity

Cofactor

pyridoxal 5'-phosphate (UniProtKB | Rhea| CHEBI:597326 )

Kinetics

KM SUBSTRATE pH TEMPERATURE[C] NOTES EVIDENCE
198 μML-tryptophan

Pathway

Secondary metabolite biosynthesis.

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site30substrate
Binding site86substrate
Binding site148substrate
Binding site202substrate
Binding site407substrate

GO annotations

AspectTerm
Molecular FunctionL-tryptophan aminotransferase activity
Molecular Functionpyridoxal phosphate binding
Molecular Functiontransaminase activity
Molecular Functiontryptophan-phenylpyruvate transaminase activity
Biological Processalpha-amino acid metabolic process
Biological Processterrequinone A biosynthetic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Aminotransferase tdiD
  • EC number
  • Alternative names
    • Terrequinone biosynthesis protein D

Gene names

    • Name
      tdiD
    • ORF names
      AN8516

Organism names

Accessions

  • Primary accession
    A7XRY8
  • Secondary accessions
    • C8VEN5
    • Q5AT61
    • Q5AT64

Proteomes

PTM/Processing

Features

Showing features for chain, modified residue.

TypeIDPosition(s)Description
ChainPRO_00004363671-436Aminotransferase tdiD
Modified residue270N6-(pyridoxal phosphate)lysine

Expression

Induction

Expression is positively regulated by the secondary metabolism regulator laeA (PubMed:16426969, PubMed:17291795).

Interaction

Protein-protein interaction databases

Structure

Family & Domains

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    436
  • Mass (Da)
    47,705
  • Last updated
    2007-10-23 v1
  • Checksum
    015F606F1A48EDD8
MGSIGANNAVADPTPLFSSRVQKWEPGAIRSLLPLEALPGMISLVAGKPSPETFPIAEIAISLKDTPAGTGRIVVDGDELNQALQYGLPRGNAQLIQWFESLQRSVHGLDENGGWSCCIGNGSQELIHRVIQVFTDPGDPVLLETPAYPGVAGFLRADGQELIPVYSDAQGLNPASLEQALSEWPGDSPRPKVLYTTPTGSNPTGQSCTESRKAEILRLAKRFNFIILEDDAYYYLNYGDDKQRARSYLALERDVNGESGRVVRFDSLSKIVSPGMRLGILTAQAAVVDKVVRITENINLQPSSTTQLLALSLLRHWGQAGFLKHCAEAAEVYRRRRDVFVSAAERHLQGRATWVVPTAGMFVWLELKLPPEMDSFELLKSQGMKNGVLAIPGVAFMPGNEQTCYIRVSFSLVPERDMDEACRRIAGLVDRCACHS

Sequence caution

The sequence CBF80716.1 differs from that shown. Reason: Erroneous gene model prediction
The sequence EAA66860.1 differs from that shown. Reason: Erroneous gene model prediction
The sequence EAA66872.1 differs from that shown. Reason: Erroneous gene model prediction

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
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.

Genome annotation databases

Similar Proteins

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