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B6db families: 4.3.1.27
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4.3.1.27
Activity 4.3.1.27
Description Threo-3-hydroxy-D-aspartate ammonia-lyase
PDB 4PB5;
PLP Fold Type III
PLP-dependent Domain
Domain alignment
Domain hmm		Fold type III
Number of sequences 11
Sequences in seed alignment
BacteriaNP886995 (Bordetella bronchiseptica ); YP_008599440 (Ralstonia pickettii); WP_018420721 (Burkholderia sp. WSM4176); WP_019652708 (Variovorax paradoxus); YP_001632629 (Bordetella petrii DSM 12804); WP_003271832 (Ralstonia solanacearum); WP_006158437 (Cupriavidus basilensis); B2DFG5 (Delftia sp. HT23); YP_006898691 (Bordetella bronchiseptica); WP_017232145 (Pandoraea sp. B-6); WP_007869802 (Polaromonas sp. CF318);

DISPLAY: Fasta format, alignment, hmm, hmm_local
Reference sequence B2DFG5
Domain interval 15-366
Catalytic site 46 K
 
References
 Matsumoto, Y.; Yasutake, Y.; Takeda, Y.; Tamura, T.; Yokota, A.; Wada, M. (2015) Structural insights into the substrate stereospecificity of D-threo-3-hydroxyaspartate dehydratase from Delftia sp. HT23: a useful enzyme for the synthesis of optically pure L-threo- and D-erythro-3-hydroxyaspartate Appl Microbiol Biotechnol 99 7137-50.

 Matsumoto Y, Yasutake Y, Takeda Y, Tamura T, Yokota A, Wada M. (2013) Crystallization and preliminary X-ray diffraction studies of D-threo-3-hydroxyaspartate dehydratase isolated from Delftia sp. HT23. Acta Crystallogr Sect F Struct Biol Cryst Commun 69 1131-4.

 Maeda T, Takeda Y, Murakami T, Yokota A, Wada M. (2010) Purification, characterization and amino acid sequence of a novel enzyme, D-threo-3-hydroxyaspartatedehydratase, from Delftia sp. HT23 J Biochem 148 705-12.

Articles on 4.3.1.27
last changed 2017/09/06 11:21

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