B6db families : 2_6_1

	Activities \| Families \| Sequences \| Fold types \| References \| Help

2.6.1.13

Activity

2.6.1.13

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 2.6.1.13 family, rather than among L-lysine aminotransferases (EC 2.6.1.36) or omega-amino acid--pyruvate aminotransferases (EC 2.6.1.18).

PDB

1GBN;2OAT;

PLP Fold Type

PLP-dependent Domain

Domain alignment
Domain hmm

Fold type I

Number of sequences

Sequences in seed alignment

Bacteria	AAQ66353 (Porphyromonas gingivalis); ZP_00013458 (Rhodospirillum rubrum); NP_645656 (Staphylococcus aureus); NP_769495 (Bradyrhizobium japonicum); NP_518280 (Ralstonia solanacearum); OAT_BACSU (Bacillus subtilis); BAC14243.1 (Oceanobacillus iheyensis); NP_883083 (Bordetella parapertussis); NP_828288 (Streptomyces avermitilis);
Fungi	OAT_EMENI (Emericella nidulans); AAX46759 (Penicillium chrysogenum); OAT_SCHPO (Schizosaccharomyces pombe); OAT_YEAST (Saccharomyces cerevisiae);
Metazoa	OAT_RAT (Rattus norvegicus); AAQ16111 (Schistosoma japonicum); AAG12164 (Xenopus laevis); OAT_PLAFD (Plasmodium falciparum); NP_649139.1 (Drosophila melanogaster); G88481 (Caenorhabditis elegans); BAA08868.1 (Drosophila ananassae); OAT_HUMAN (Homo sapiens); OAT_MOUSE (Mus musculus);
Viridiplantae	NP_199430 (Arabidopsis thaliana); AF177590 (Vitis vinifera); OAT_VIGAC (Vigna aconitifolia); CAC82185 (Medicago truncatula);

DISPLAY: Fasta format, alignment, hmm, hmm_local

Reference sequence

OAT_HUMAN

Domain interval

61-384

Catalytic site

292 K

References

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 2.6.1.13

last changed

2007/09/08 13:07