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B6db families:
Description Tryptophan--phenylpyruvate aminotransferase
Notes The family has been built around the characterized enzyme from Aspergillus (Emericella) nidulans. This fungal enzyme catalyzes the first step in the synthesis of bioactive alkaloids of the bis-indolylquinone type.

Proteins most similar to those showing 2-aminoadipate aminotransferase activity (family

PLP Fold Type I
PLP-dependent Domain
Domain alignment
Domain hmm
Fold type I

Number of sequences 7
Sequences in seed alignment
FungiXP_001523024 (Magnaporthe grisea 70-15); ABU51605 (Emericella nidulans); XP_017990264 (Malassezia pachydermatis); EAU86022 (Coprinopsis cinerea); XP_011387757 (Ustilago maydis 521); AGI59488 (Malassezia furfur); OAJ19145 (Tilletia walkeri);

DISPLAY: Fasta format, alignment, hmm, hmm_local

Reference sequence ABU51605
Domain interval 39-425
Catalytic site 270 K
 Preuss J, Hort W, Lang S, Netsch A, Rahlfs S, Lochnit G, Jortzik E, Becker K, Mayser PA. (2013) Characterization of tryptophan aminotransferase 1 of Malassezia furfur, the key enzyme in the production of indolic compounds by M. furfur. Exp Dermatol. 22 736-41.

 Zuther K, Mayser P, Hettwer U, Wu W, Spiteller P, Kindler BL, Karlovsky P, Basse CW, Schirawski J (2008) The tryptophan aminotransferase Tam1 catalyses the single biosynthetic step for tryptophan-dependent pigment synthesis in Ustilago maydis Mol Microbiol 68 152-72.

 Schneider P, Weber M, Rosenberger K, Hoffmeister D. (2007) A one-pot chemoenzymatic synthesis for the universal precursor of antidiabetes and antiviral bis-indolylquinones Chem Biol 14 635-44.

Articles on
last changed 2017/07/17 14:33

B6db families