B6db families : dhap

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dhap transaminase

Activity

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

PLP-dependent Domain

Domain alignment
Domain hmm

Fold type I

Number of sequences

Sequences in seed alignment

Bacteria

WP_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