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B6db families: 2.6.1.57.a

2.6.1.57 a
Activity 2.6.1.57
Description Aromatic amino acid transaminase. (family a)
Notes Sequences in this family come from Gram- bacteria, and are strict homologs of aspartate aminotransferase enzymes belonging to families 2.6.1.1_a and 2.6.1.1_c.
PDB 1AY4;
PLP Fold Type I
PLP-dependent Domain
Domain alignment
Domain hmm
Fold type I

Number of sequences
13
Sequences in seed alignment
BacteriaTYRB_PARDE (Paracoccus denitrificans); CAD14712.1 (Ralstonia solanacearum); CAC89183.1 (Yersinia pestis); NP_936948 (Vibrio vulnificus); TYRB_SALTY (Salmonella typhimurium); TYRB_ECOLI (Escherichia coli); AAQ58010 (Chromobacterium violaceum ); AAC26140.1 (Klebsiella pneumoniae); ZP_00006006 (Rhodobacter sphaeroides); PHHC_PSEAE (Pseudomonas aeruginosa); NP_931530 (Photorhabdus luminescens); ZP_00083727 (Pseudomonas fluorescens); NP_795070 (Pseudomonas syringae );

DISPLAY: Fasta format, alignment, hmm, hmm_local


Reference sequence TYRB_ECOLI
Domain interval 26-393
Catalytic site 247 K
 
References
 Heilbronn, J.; Wilson, J.; Berger, B.J. (1999) Tyrosine aminotransferase catalyzes the final step of methionine recycling in Klebsiella pneumoniae J Bacteriol 181 1739-47.

 Gu, W.; Song, J.; Bonner, C.A.; Xie, G.; Jensen, R.A. (1998) PhhC is an essential aminotransferase for aromatic amino acid catabolism in Pseudomonas aeruginosa Microbiology 144 3127-34.

 Oue, S.; Okamoto, A.; Nakai, Y.; Nakahira, M.; Shibatani, T.; Hayashi, H.; Kagamiyama, H. (1997) Paracoccus denitrificans aromatic amino acid aminotransferase: a model enzyme for the study of dual substrate recognition mechanism J Biochem (Tokyo) 121 161-71.

 Hayashi, H.; Inoue, K.; Nagata, T.; Kuramitsu, S.; Kagamiyama, H. (1993) Escherichia coli aromatic amino acid aminotransferase: characterization and comparison with aspartate aminotransferase Biochemistry 32 12229-39..

Articles on 2.6.1.57.a
last changed 2007/12/05 19:48

B6db families