Summary: Aminotransferase class IV
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Aminotransferase class IV Provide feedback
The D-amino acid transferases (D-AAT) are required by bacteria to catalyse the synthesis of D-glutamic acid and D-alanine, which are essential constituents of bacterial cell wall and are the building block for other D-amino acids. Despite the difference in the structure of the substrates, D-AATs and L-ATTs have strong similarity.
Sugio S, Petsko GA, Manning JM, Soda K, Ringe D; , Biochemistry 1995;34:9661-9669.: Crystal structure of a D-amino acid aminotransferase: how the protein controls stereoselectivity. PUBMED:7626635 EPMC:7626635
Okada K, Hirotsu K, Sato M, Hayashi H, Kagamiyama H; , J Biochem 1997;121:637-641.: Three-dimensional structure of Escherichia coli branched-chain amino acid aminotransferase at 2.5 A resolution. PUBMED:9163511 EPMC:9163511
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This tab holds annotation information from the InterPro database.
InterPro entry IPR001544
Aminotransferases share certain mechanistic features with other pyridoxal-phosphate dependent enzymes, such as the covalent binding of the pyridoxal-phosphate group to a lysine residue. On the basis of sequence similarity, these various enzymes can be grouped [PUBMED:1644759] into subfamilies.
One of these, called class-IV, currently consists of proteins of about 270 to 415 amino-acid residues that share a few regions of sequence similarity. Surprisingly, the best conserved region does not include the lysine residue to which the pyridoxal-phosphate group is known to be attached, in ilvE, but is located some 40 residues at the C terminus side of the pyridoxal-phosphate-lysine. The D-amino acid transferases (D-AAT), which are among the members of this entry, are required by bacteria to catalyse the synthesis of D-glutamic acid and D-alanine, which are essential constituents of bacterial cell wall and are the building block for other D-amino acids. Despite the difference in the structure of the substrates, D-AATs and L-ATTs have strong similarity [PUBMED:7626635, PUBMED:9163511].
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|Molecular function||catalytic activity (GO:0003824)|
|Biological process||metabolic process (GO:0008152)|
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|Seed source:||Pfam-B_607 (release 3.0)|
|Author:||Finn RD, Bateman A|
|Number in seed:||78|
|Number in full:||10610|
|Average length of the domain:||228.80 aa|
|Average identity of full alignment:||22 %|
|Average coverage of the sequence by the domain:||69.44 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||14|
|Download:||download the raw HMM for this family|
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