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B6db families: dhap.transaminase

dhap transaminase
Activity dhap_transaminase
Description Dihydroxyacetone phosphate transaminase (2.6.1.-)
Notes In Bradyrhizobium japonicum the protein is single-domain, but in Bradyrhizobium elkanii and in other bacteria the protein is part of a bidomain (and bifunctional) polypeptide comprising dihydrorhizobitoxine synthase, which is also a PLP-dependent enzyme.
Accordingly, the C-terminal domain from the B. elkanii sequence has been removed and included in the dihydrorhizobitoxine synthase family.

The family is most similar to 2.6.1.37 (aminoethylphosphonate aminotransferase) and to alanine-glyoxylate transaminase.

PLP Fold Type I
PLP-dependent Domain
Domain alignment
Domain hmm
Fold type I

Number of sequences 9
Sequences in seed alignment
BacteriaWP_012916844 (Xanthomonas albilineans); WP_042628410 (Burkholderia glumae); WP_024906147 (Paraburkholderia andropogonis); YP_450308 (Xanthomonas oryzae); NP_768717 (Bradyrhizobium japonicum USDA 110); AFP89752 (Sinorhizobium meliloti); WP_009488741 (Microvirga lotononidis); BAB55900 (Bradyrhizobium elkanii); YP_001863711 (Burkholderia phymatum STM815);

DISPLAY: Fasta format, alignment, hmm, hmm_local


Reference sequence BAB55900
Domain interval 4-287
Catalytic site 170 K
 
References
 Andreessen B1, Steinbüchel A. (2012) Biotechnological conversion of glycerol to 2-amino-1,3-propanediol (serinol) in recombinant Escherichia coli Appl Microbiol Biotechnol. 93 357-65.

Articles on dhap.transaminase
last changed 2017/06/29 19:31

B6db families