Canmetcon
You are using an unsupported browser. Please upgrade your browser to a newer version to get the best experience on Yeast Metabolome Database.
Identification
NameAcetylornithine aminotransferase, mitochondrial
Synonyms
  • ACOAT
Gene NameARG8
Enzyme Class
Biological Properties
General FunctionInvolved in transaminase activity
Specific FunctionN(2)-acetyl-L-ornithine + 2-oxoglutarate = N- acetyl-L-glutamate 5-semialdehyde + L-glutamate
Cellular LocationMitochondrion matrix
SMPDB Pathways
4-aminobutanoate degradationPW002382 ThumbThumb?image type=greyscaleThumb?image type=simple
KEGG Pathways
Arginine and proline metabolismec00330 Map00330
Lysine biosynthesisec00300 Map00300
SMPDB Reactions
gamma-Aminobutyric acid + Oxoglutaric acidL-Glutamic acid + Succinic acid semialdehyde
gamma-Aminobutyric acid + Oxoglutaric acidL-Glutamic acid + Succinic acid semialdehyde
KEGG Reactions
2-Acetamido-5-oxopentanoic acid + L-Glutamic acidOxoglutaric acid + N-Acetylornithine
Metabolites
YMDB IDNameView
YMDB00028N-AcetylornithineShow
YMDB00153Oxoglutaric acidShow
YMDB00236Succinic acid semialdehydeShow
YMDB00255N-Acetyl-L-glutamate 5-semialdehydeShow
YMDB00271L-Glutamic acidShow
YMDB00335gamma-Aminobutyric acidShow
YMDB005362-Acetamido-5-oxopentanoic acidShow
GO Classification
Component
Not Available
Function
binding
transferase activity, transferring nitrogenous groups
transaminase activity
catalytic activity
transferase activity
cofactor binding
pyridoxal phosphate binding
Process
glutamine family amino acid metabolic process
arginine metabolic process
metabolic process
cellular metabolic process
cellular amino acid and derivative metabolic process
cellular amino acid metabolic process
Gene Properties
Chromosome Locationchromosome 15
LocusYOL140W
Gene Sequence>1272 bp ATGTTTAAAAGATATTTATCCAGTACGTCATCAAGAAGATTTACAAGCATTTTAGAGGAA AAGGCCTTTCAAGTGACCACTTACTCTAGACCTGAAGATCTATGTATAACTAGAGGTAAA AATGCAAAGCTGTATGATGACGTGAATGGTAAAGAATATATCGATTTCACCGCAGGTATT GCGGTGACCGCATTAGGCCATGCAAATCCTAAAGTGGCAGAAATTCTGCACCATCAGGCT AACAAACTGGTTCATTCCTCCAACCTTTACTTCACTAAGGAATGTTTGGATTTAAGTGAA AAGATTGTTGAAAAGACCAAGCAATTCGGTGGTCAACACGACGCCTCAAGAGTATTTTTA TGTAATTCTGGTACGGAAGCAAATGAAGCTGCTTTGAAGTTTGCAAAGAAACATGGTATA ATGAAAAATCCTAGCAAGCAAGGCATTGTTGCATTTGAGAACTCTTTTCATGGCCGTACT ATGGGCGCTTTATCTGTCACTTGGAATAGTAAATATAGAACTCCTTTTGGGGATTTGGTT CCCCATGTCTCATTCTTAAATTTGAATGACGAAATGACCAAACTACAAAGTTATATCGAG ACCAAAAAGGACGAGATTGCTGGTTTAATTGTCGAGCCCATACAAGGTGAAGGTGGGGTT TTTCCCGTAGAAGTTGAAAAGCTAACCGGATTGAAGAAAATATGTCAAGATAATGATGTG ATTGTCATTCATGATGAAATTCAATGCGGTTTGGGCCGTTCAGGTAAACTATGGGCTCAT GCTTATTTACCAAGTGAGGCTCATCCGGATATTTTTACATCTGCCAAAGCATTGGGAAAT GGCTTCCCCATCGCTGCCACCATCGTCAATGAAAAAGTTAATAATGCTTTGAGAGTTGGT GACCACGGCACCACGTATGGTGGTAATCCGCTGGCCTGTTCTGTAAGCAACTATGTTTTG GATACCATAGCAGACGAAGCTTTTTTGAAACAAGTCTCTAAGAAGAGTGATATCTTACAA AAGCGCTTGCGCGAAATTCAAGCCAAATATCCAAATCAAATAAAGACTATCAGAGGAAAA GGTTTGATGCTTGGTGCTGAGTTCGTCGAACCACCCACCGAGGTCATCAAAAAGGCCAGA GAATTGGGACTTTTGATCATTACCGCTGGTAAGAGTACCGTTAGATTTGTTCCCGCATTA ACGATTGAAGACGAACTAATCGAAGAAGGGATGGATGCTTTTGAAAAGGCTATTGAAGCG GTTTACGCTTAA
Protein Properties
Pfam Domain Function
Protein Residues423
Protein Molecular Weight46681.10156
Protein Theoretical pI7.62
Signalling Regions
  • None
Transmembrane Regions
  • None
Protein Sequence>Acetylornithine aminotransferase, mitochondrial MFKRYLSSTSSRRFTSILEEKAFQVTTYSRPEDLCITRGKNAKLYDDVNGKEYIDFTAGI AVTALGHANPKVAEILHHQANKLVHSSNLYFTKECLDLSEKIVEKTKQFGGQHDASRVFL CNSGTEANEAALKFAKKHGIMKNPSKQGIVAFENSFHGRTMGALSVTWNSKYRTPFGDLV PHVSFLNLNDEMTKLQSYIETKKDEIAGLIVEPIQGEGGVFPVEVEKLTGLKKICQDNDV IVIHDEIQCGLGRSGKLWAHAYLPSEAHPDIFTSAKALGNGFPIAATIVNEKVNNALRVG DHGTTYGGNPLACSVSNYVLDTIADEAFLKQVSKKSDILQKRLREIQAKYPNQIKTIRGK GLMLGAEFVEPPTEVIKKARELGLLIITAGKSTVRFVPALTIEDELIEEGMDAFEKAIEA VYA
References
External Links
ResourceLink
Saccharomyces Genome Database ARG8
Uniprot IDP18544
Uniprot NameARGD_YEAST
GenBank Gene IDM32795
Genebank Protein ID171083
General Reference
  • Heimberg, H., Boyen, A., Crabeel, M., Glansdorff, N. (1990). "Escherichia coli and Saccharomyces cerevisiae acetylornithine aminotransferase: evolutionary relationship with ornithine aminotransferase." Gene 90:69-78.2199330
  • Casas, C., Aldea, M., Casamayor, A., Lafuente, M. J., Gamo, F. J., Gancedo, C., Arino, J., Herrero, E. (1995). "Sequence analysis of a 9873 bp fragment of the left arm of yeast chromosome XV that contains the ARG8 and CDC33 genes, a putative riboflavin synthase beta chain gene, and four new open reading frames." Yeast 11:1061-1067.7502581
  • Dujon, B., Albermann, K., Aldea, M., Alexandraki, D., Ansorge, W., Arino, J., Benes, V., Bohn, C., Bolotin-Fukuhara, M., Bordonne, R., Boyer, J., Camasses, A., Casamayor, A., Casas, C., Cheret, G., Cziepluch, C., Daignan-Fornier, B., Dang, D. V., de Haan, M., Delius, H., Durand, P., Fairhead, C., Feldmann, H., Gaillon, L., Kleine, K., et, a. l. .. (1997). "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV." Nature 387:98-102.9169874
  • Ghaemmaghami, S., Huh, W. K., Bower, K., Howson, R. W., Belle, A., Dephoure, N., O'Shea, E. K., Weissman, J. S. (2003). "Global analysis of protein expression in yeast." Nature 425:737-741.14562106