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B6db families: 4.3.1.16

4.3.1.16
Activity 4.3.1.16
Description Threo-3-hydroxyaspartate ammonia-lyase
Notes Includes validated sequences from bacteria (Pseudomonas) and yeast. Enzymes most similar to serine racemases (Family 5.1.1.18) and D-erythro-3-hydroxyaspartate deaminases (Family bhcb).
PDB 1V71;
PLP Fold Type II
PLP-dependent Domain
Domain alignment
Domain hmm
Fold type II

Number of sequences
13
Sequences in seed alignment
BacteriaBAM73342 (Pseudomonas sp. N99); NP_523075 (Ralstonia solanacearum); ZP_00222200 (Burkholderia cepacia); WP_071010816 (Cupriavidus sp. USMAHM13); WP_071483880 (Pseudomonas costantinii); NP_251373 (Pseudomonas aeruginosa PA01); BAC87894 (Acinetobacter baumannii); ZP_00169240 (Ralstonia eutropha); NP_928148 (Photorhabdus luminescens); BAF48772 (Pseudomonas sp. T62);
FungiSCW01594 (Lachancea fermentati); NP_012704 (Saccharomyces cerevisiae); CAA18316 (Schizosaccharomyces pombe);

DISPLAY: Fasta format, alignment, hmm, hmm_local


Reference sequence BAF48772
Domain interval 16-305
Catalytic site 53 K
 
References
 Nagano, H.; Shibano, K.; Matsumoto, Y.; Yokota, A.; Wada, M. (2017) Isolation and amino acid sequence of a dehydratase acting on d-erythro-3-hydroxyaspartate from Pseudomonas sp. N99, and its application in the production of optically active 3-hydroxyaspartate Biosci Biotechnol Biochem 81 1156-1164.

 Wada, M.; Nakamori, S.; Takagi, H. (2003) Serine racemase homologue of Saccharomyces cerevisiae has L-threo-3-hydroxyaspartate dehydratase activity FEMS Microbiol Lett 225 189-93.

 Wada, M.; Matsumoto, T.; Nakamori, S.; Sakamoto, M.; Kataoka, M.; Liu, J. Q.; Itoh, N.; Yamada, H.; Shimizu, S. (1999) Purification and characterization of a novel enzyme, L-threo-3- hydroxyaspartate dehydratase, from Pseudomonas sp. T62 FEMS Microbiol Lett 179 147-51.

Articles on 4.3.1.16
last changed 2019/11/25 16:34

B6db families