The domain within your query sequence starts at position 26 and ends at position 433; the E-value for the Aminotran_3 domain shown below is 1.3e-91.

FAADPIKIMRAQGQYMFDEKGERYLDCINNVAHVGHCHPEVVKAAAKQMELLNTNSRFLH
DNIIEFAKRLTATLPQELSVCYFTNSGSEANDLALRLARQFRGHQDVITLDHAYHGHLSS
LIEISPYKFQKGKDVKRETVHVAPAPDTYRGKYREDHEDPSTAYADEVKKIIEEAHSSGR
KIAAFIAESMQSCGGQIIPPAGYFQKVAEHIHKAGGVFIADEVQVGFGRVGRYFWSFQMY
GEDFVPDIVTMGKPMGNGHPISCVVTTKEIAEAFSSSGMEYFNTYGGNPVSCAVGLAVLD
VIEKENLQGNAVRVGTYLMELLSEQKAKHPLIGDIRGVGLFIGIDLVKDREKRTPATAEA
QHIIYEMKGKGVLLSADGPHRNVLKIKPPMCFTEDDAKFLVDHLDGIL

Aminotran_3

Aminotran_3
PFAM accession number:PF00202
Interpro abstract (IPR005814):

Aminotransferases share certain mechanistic features with other pyridoxalphosphate-dependent enzymes, such as the covalent binding of the pyridoxalphosphate group to a lysine residue. On the basis of sequence similarity, these various enzymes can be grouped [(PUBMED:1618757)] into subfamilies. One of these, called class-III, includes acetylornithine aminotransferase (EC 2.6.1.11), which catalyzes the transfer of an amino group from acetylornithine to alpha-ketoglutarate, yielding N-acetyl-glutamic-5-semi-aldehyde and glutamic acid [(PUBMED:2199330)]; ornithine aminotransferase (EC 2.6.1.13), which catalyzes the transfer of an amino group from ornithine to alpha-ketoglutarate, yielding glutamic-5-semi-aldehyde and glutamic acid [(PUBMED:3754226)]; omega-amino acid--pyruvate aminotransferase (EC 2.6.1.18), which catalyzes transamination between a variety of omega-amino acids, mono- and diamines, and pyruvate [(PUBMED:2500426)]; 4-aminobutyrate aminotransferase (EC 2.6.1.19) (GABA transaminase), which catalyzes the transfer of an amino group from GABA to alpha-ketoglutarate, yielding succinate semialdehyde and glutamic acid [(PUBMED:10989446)]; DAPA aminotransferase (EC 2.6.1.62), a bacterial enzyme (bioA), which catalyzes an intermediate step in the biosynthesis of biotin, the transamination of 7-keto-8-aminopelargonic acid to form 7,8-diaminopelargonic acid [(PUBMED:1092681)]; 2,2-dialkylglycine decarboxylase (EC 4.1.1.64), a Burkholderia cepacia (Pseudomonas cepacia) enzyme (dgdA) that catalyzes the decarboxylating amino transfer of 2,2-dialkylglycine and pyruvate to dialkyl ketone, alanine and carbon dioxide [(PUBMED:8342040)]; glutamate-1-semialdehyde aminotransferase (EC 5.4.3.8) (GSA) [(PUBMED:2349227)]; Bacillus subtilis aminotransferases yhxA and yodT; Haemophilus influenzae diaminobutyrate--2-oxoglutarate aminotransferase (HI0949) [(PUBMED:9514614)]; and Caenorhabditis elegans alanine--glyoxylate aminotransferase 2-like (T01B11.2).

GO function:transaminase activity (GO:0008483), pyridoxal phosphate binding (GO:0030170)

This is a PFAM domain. For full annotation and more information, please see the PFAM entry Aminotran_3