Protein Family Models

This domain is found in amino transferases, and other enzymes including cysteine desulphurase EC:4.4.1.-. (from Pfam)

Date:

2024-08-14

2-aminoethylphosphonate--pyruvate transaminase is involved in phosphonate degradation, catalyzing the conversion of (2-aminoethyl)phosphonate and pyruvate to L-alanine and phosphonoacetaldehyde

Date:

2019-05-08

Catalyzes the formation of phosphonoacetaldehyde from 2-aminoethylphosphonate and pyruvate

Date:

2021-08-20

This family includes a number of 2-aminoethylphosphonate aminotransferases, some of which are indicated to operate in the catabolism of 2-aminoethylphosphonate (AEP) and others which are involved in the biosynthesis of the same compound. The catabolic enzyme (PhnW, [1]) is known to use pyruvate:alanine as the transfer partner and is modeled by the equivalog-level HMM (TIGR02326). The PhnW family is apparently a branch of a larger tree including genes (AepZ) adjacent to others responsible for the biosynthesis of phosphonoacetaldehyde [2]. The identity of the transfer partner is unknown for these enzymes and considering the reversed flux compared to PhnW, it may very well be different.

Date:

2024-05-30

Members of this family are 2-aminoethylphosphonate--pyruvate transaminase. This enzyme acts on the most common type of naturally occurring phosphonate. It interconverts 2-aminoethylphosphonate plus pyruvate with 2-phosphonoacetaldehyde plus alanine. The enzyme phosphonoacetaldehyde hydrolase (EC 3.11.1.1), usually encoded by an adjacent gene, then cleaves the C-P bond of phosphonoacetaldehyde, adding water to yield acetaldehyde plus inorganic phosphate. Species with this pathway generally have an identified phosphonate ABC transporter but do not also have the multisubunit C-P lysase complex as found in Escherichia coli.

Gene:

phnW

Date:

2021-08-26