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B6db families:
Description Ornithine--oxo-acid aminotransferase.
Notes The enzyme from Penicillium chrysogenum employs as substrates both L-ornithine (yielding L-glutamate 5-semialdehyde) and L-lysine (yielding L-aminoadipate semialdehyde). The latter reaction is important for the biosynthesis of penicillin. Given its structural similarity to classic ornithine aminotransferases, and its preference for alpha-ketoglutarate as an amino acceptor, we have included the enzyme from Penicillium in the family, rather than among L-lysine aminotransferases (EC or omega-amino acid--pyruvate aminotransferases (EC
PLP Fold Type I
PLP-dependent Domain
Domain alignment
Domain hmm
Fold type I

Number of sequences
Sequences in seed alignment
BacteriaNP_769495 (Bradyrhizobium japonicum); ZP_00013458 (Rhodospirillum rubrum); NP_518280 (Ralstonia solanacearum); AAQ66353 (Porphyromonas gingivalis); NP_883083 (Bordetella parapertussis); OAT_BACSU (Bacillus subtilis); BAC14243.1 (Oceanobacillus iheyensis); NP_645656 (Staphylococcus aureus); NP_828288 (Streptomyces avermitilis);
FungiOAT_YEAST (Saccharomyces cerevisiae); OAT_SCHPO (Schizosaccharomyces pombe); OAT_EMENI (Emericella nidulans); AAX46759 (Penicillium chrysogenum);
MetazoaXP_002114709 (Trichoplax adhaerens); AAQ16111 (Schistosoma japonicum); OAT_MOUSE (Mus musculus); BAA08868.1 (Drosophila ananassae); OAT_HUMAN (Homo sapiens); G88481 (Caenorhabditis elegans); NP_649139.1 (Drosophila melanogaster); AAG12164 (Xenopus laevis); OAT_RAT (Rattus norvegicus);
Other_EukaryaOAT_PLAFD (Plasmodium falciparum);
ViridiplantaeCAC82185 (Medicago truncatula); NP_199430 (Arabidopsis thaliana); AF177590 (Vitis vinifera); OAT_VIGAC (Vigna aconitifolia);

DISPLAY: Fasta format, alignment, hmm, hmm_local

Reference sequence OAT_HUMAN
Domain interval 61-384
Catalytic site 292 K
 Funck D, Stadelhofer B, Koch W. (2008) Ornithine-[delta]-aminotransferase is essential for arginine catabolism but not for proline biosynthesis BMC Plant Biol 8 40.

 Valmaseda, E.M.; Campoy, S.; Naranjo, L.; Casqueiro, J.; Martin, J.F. (2005) Lysine is catabolized to 2-aminoadipic acid in Penicillium chrysogenum by an omega-aminotransferase and to saccharopine by a lysine 2-ketoglutarate reductase. Characterization of the omega-aminotransferase Mol Genet Genomics 274 272-82.

 Gafan, C.; Wilson, J.; Berger, L.C.; Berger, B.J. (2001) Characterization of the ornithine aminotransferase from Plasmodium falciparum. Mol Biochem Parasitol 118 1-10.

 Jhee, K. H.; Yoshimura, T.; Esaki, N.; Yonaha, K.; Soda, K. (1995) Thermostable ornithine aminotransferase from Bacillus sp. YM-2: purification and characterization J Biochem (Tokyo) 118 101-8.

 Delauney, A.J.; Hu, C.A.; Kishor, P.B.; Verma, D.P. (1993) Cloning of ornithine delta-aminotransferase cDNA from Vigna aconitifolia by trans-complementation in Escherichia coli and regulation of proline biosynthesis J Biol Chem 268 18673-8.

 Simmaco, M.; John, R. A.; Barra, D.; Bossa, F. (1986) The primary structure of ornithine aminotransferase. Identification of active-site sequence and site of post-translational proteolysis FEBS Lett 199 39-42.

Articles on
last changed 2007/09/08 13:07

B6db families