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B6db families:
Description D-threonine aldolase, low specificity
Notes Available at least two characterized sequences (from Achromobacter/Alcaligenes and from Arthrobacter sp. DK-38)
PLP Fold Type III
PLP-dependent Domain
Domain alignment
Domain hmm
Fold type III

Number of sequences
Sequences in seed alignment
BacteriaZP_00243741 (Rubrivivax gelatinosus); ZP_00192845 (Mesorhizobium sp.); ZP_00271732 (Ralstonia metallidurans); CAE44783.1 (Bordetella pertussis); BAA31547 (Arthrobacter sp.); BAA86032 (Achromobacter xylosoxidans); BAC20179 (Paracoccus denitrificans);

DISPLAY: Fasta format, alignment, hmm, hmm_local

Reference sequence BAC20179
Domain interval 20-320
Catalytic site 62 K
 Liu, J. Q.; Dairi, T.; Itoh, N.; Kataoka, M.; Shimizu, S. (2003) A novel enzyme, D-3-hydroxyaspartate aldolase from Paracoccus denitrificans IFO 13301: purification, characterization, and gene cloning Appl Microbiol Biotechnol 62 53-60.

 Liu, J. Q.; Odani, M.; Yasuoka, T.; Dairi, T.; Itoh, N.; Kataoka, M.; Shimizu, S.; Yamada, H. (2000) Gene cloning and overproduction of low-specificity D-threonine aldolase from Alcaligenes xylosoxidans and its application for production of a key intermediate for parkinsonism drug Appl Microbiol Biotechnol 54 44-51.

 Liu, J. Q.; Dairi, T.; Itoh, N.; Kataoka, M.; Shimizu, S.; Yamada, H. (1998) A novel metal-activated pyridoxal enzyme with a unique primary structure, low specificity D-threonine aldolase from Arthrobacter sp. Strain DK-38. Molecular cloning and cofactor characterization J Biol Chem 273 16678-85.

Articles on
last changed 2010/06/07 17:55

B6db families