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B6db families: 2.6.1.21

2.6.1.21
Activity 2.6.1.21
Description D-alanine aminotransferase.
PDB 3DAA;2DAA;1G2W;
PLP Fold Type IV
PLP-dependent Domain
Domain alignment
Domain hmm
Fold type IV

Number of sequences
25
Sequences in seed alignment
BacteriaDAAA_BACSU (Bacillus subtilis); DAAA_LISMO (Listeria monocytogenes); NP_692004 (Oceanobacillus iheyensis); WP_022465728 (Clostridium sp. CAG:277); NP_764978 (Staphylococcus epidermidis); CAE39908 (Bordetella parapertussis); AAO91869 (Bacillus cereus); ZP_00015048 (Rhodospirillum rubrum); WP_023860309 (Lactobacillus equi); NP_847638 (Bacillus anthracis); DAAA_LISIN (Listeria innocua); AAY98539 (Geobacillus toebii); DAAA_STAHA (Staphylococcus haemolyticus); AAY98538 (Geobacillus sp. KLS-1); Q1WRM6 (Lactobacillus salivarius); NP_243677 (Bacillus halodurans); DAAA_BACSH (Bacillus sphaericus); CAB82475 (Staphylococcus aureus); DAAA_BACSY (Bacillus sp.); ZP_00023345 (Ralstonia metallidurans);
ViridiplantaeNP_200593 (Arabidopsis thaliana); CAO44058 (Vitis vinifera); EDQ63982 (Physcomitrella patens); AAT74744 (Lycopersicon esculentum); BAD21824 (Oryza sativa);

DISPLAY: Fasta format, alignment, hmm, hmm_local


Reference sequence DAAA_STAHA
Domain interval 7-274
Catalytic site 146 K
 
References
 Kobayashi J.; Shimizu, Y.; Mutaguchi, Y.; Doi, K. (2013) Characterization of d-amino acid aminotransferase from Lactobacillus salivarius J. Mol. Catal. B: Enzymatic 94 1522.

 Funakoshi M, Sekine M, Katane M, Furuchi T, Yohda M, Yoshikawa T, Homma H. (2008) Cloning and functional characterization of Arabidopsis thaliana D-amino acid aminotransferase--D-aspartate behavior during germination. FEBS J 275 1188-200.

 Lee, S.G.; Hong, S.P.; Song, J.J.; Kim, S.J.; Kwak, M.S.; Sung, M.H. (2006) Functional and Structural Characterization of Thermostable D-Amino Acid Aminotransferases from Geobacillus spp Appl. Envir. Microbiol. 72 1588-94.

 Pucci, M.J.; Thanassi, J.A.; Ho, H.T.; Falk, P.J.; Dougherty, T.J. (1995) Staphylococcus haemolyticus contains two D-glutamic acid biosynthetic activities, a glutamate racemase and a D-amino acid transaminase J Bacteriol 177 336-42.

 Sugio, S.; Petsko, G. A.; Manning, J. M.; Soda, K.; Ringe, D. (1995) Crystal structure of a D-amino acid aminotransferase: how the protein controls stereoselectivity Biochemistry 34 9661-9661.

 Tanizawa K, Asano S, Masu Y, Kuramitsu S, Kagamiyama H, Tanaka H, Soda K. (1989) The primary structure of thermostable D-amino acid aminotransferase from a thermophilic Bacillus species and its correlation with L-amino acid aminotransferases J Biol Chem 264 2450-4.

Articles on 2.6.1.21
last changed 2007/09/08 13:13

B6db families