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B6db families: 2.6.1.2.c

2.6.1.2 c
Activity 2.6.1.2
Description Alanine aminotransferase (family c)
Notes A group of enzymes based on the poorly characterized product of the E. coli gene yfdZ. The sequences are related to families involved in the transamination of diaminopimelate (2.6.1.83, 2.6.1.17) and of aromatic amino acids (e.g., 2.6.1.57b)
The enzyme from Aphanothece is indeed a promicuous catalyst acting also on diaminopimelate.
PDB 2X5D;
PLP Fold Type I
PLP-dependent Domain
Domain alignment
Domain hmm
Fold type I

Number of sequences 14
Sequences in seed alignment
BacteriaBBI93159 (Aphanothece halophytica); WP_040041281 (Noviherbaspirillum autotrophicum); WP_016243747 (Escherichia coli); WP_005275430 (Yersinia bercovieri); WP_096646554 (Calothrix brevissima); WP_015895915 (Acidobacterium capsulatum); WP_012417826 (Bordetella avium); WP_042878257 (Cupriavidus necator); 2X5D (Pseudomonas aeruginosa); WP_011610338 (Trichodesmium erythraeum); WP_085315792 (Derxia lacustris); WP_035037842 (Aquabacterium sp. NJ1); WP_062297096 (Nostoc piscinale); WP_068550701 (Thermosulfidibacter takaii);

DISPLAY: Fasta format, alignment, hmm, hmm_local


Reference sequence WP_016243747
Domain interval 36-390
Catalytic site 244 K
 
References
 Hasegawa D, Kito K, Maeda T, Rai V, Cha-Um S, Tanaka Y, Fukaya M, Takabe T (2019) Two groups of thermophilic amino acid aminotransferases exhibiting broad substrate specificities for the synthesis of phenylglycine derivatives Protoplasma 256 1727-1736.

 Yoneyama H, Hori H, Lim SJ, Murata T, Ando T, Isogai E, Katsumata R. (2011) Isolation of a mutant auxotrophic for L-alanine and identification of three major aminotransferases that synthesize L-alanine in Escherichia coli Biosci Biotechnol Biochem 75 930-8.

Articles on 2.6.1.2.c
last changed 2019/10/31 17:34

B6db families