Acetylornithine/succinyldiaminopimelate aminotransferase (P18335)

Identification
Name:Acetylornithine/succinyldiaminopimelate aminotransferase
Synonyms:
  • ACOAT
  • DapATase
  • Succinyldiaminopimelate transferase
Gene Name:argD
Enzyme Class:
Biological Properties
General Function:Involved in transaminase activity
Specific Function:Involved in both the arginine and lysine biosynthetic pathways
Cellular Location:Cytoplasm (Probable)
SMPDB Pathways:
KEGG Pathways:
KEGG Reactions:
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0N-Acetylornithine + 1.0alpha-Ketoglutarate ↔ 1.0N-Acetyl-L-glutamate 5-semialdehyde + 1.0L-Glutamate
ReactionCard
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0alpha-Ketoglutarate + 1.0N-Succinyl-L,L-2,6-diaminopimelate ↔ 1.0L-Glutamate + 1.0N-Succinyl-2-amino-6-ketopimelate
ReactionCard
SMPDB Reactions:
1.0Thumb+1.0L-Glutamic acid+1.0Thumb → 1.0Thumb+1.0Thumb
1.0N-Succinyl-2-amino-6-ketopimelate + 1.0L-Glutamic acid + 1.0L-Glutamate → 1.0N-Succinyl-L,L-2,6-diaminopimelate + 1.0Oxoglutaric acid
ReactionCard
1.0Thumb+1.0L-Glutamic acid+1.0Thumb → 1.0Thumb+1.0Thumb
1.0N-Acetyl-L-glutamate 5-semialdehyde + 1.0L-Glutamic acid + 1.0L-Glutamate → 1.0Oxoglutaric acid + 1.0N-Acetylornithine
ReactionCard
EcoCyc Reactions:
1.0Thumb+1.0Thumb ← 1.0Thumb+1.0Thumb
1.0N-Acetylornithine + 1.0Oxoglutaric acid ← 1.0N-Acetyl-L-glutamate 5-semialdehyde + 1.0L-Glutamate
ReactionCard
Complex Reactions:
1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb
1.0N-Acetylornithine + 1.0Oxoglutaric acid → 1.0N-Acetyl-L-glutamate 5-semialdehyde + 1.0L-Glutamate
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB02812alpha-KetoglutarateMetaboCard
ECMDB00148L-GlutamateMetaboCard
ECMDB06488N-Acetyl-L-glutamate 5-semialdehydeMetaboCard
ECMDB03357N-AcetylornithineMetaboCard
ECMDB12266N-Succinyl-2-amino-6-ketopimelateMetaboCard
ECMDB12267N-Succinyl-L,L-2,6-diaminopimelateMetaboCard
ECMDB04123Oxoglutaric acidMetaboCard
GO Classification:
Function
binding
catalytic activity
cofactor binding
pyridoxal phosphate binding
transaminase activity
transferase activity
transferase activity, transferring nitrogenous groups
Process
arginine metabolic process
cellular amino acid and derivative metabolic process
cellular amino acid metabolic process
cellular metabolic process
glutamine family amino acid metabolic process
metabolic process
Gene Properties
Blattner:b3359
Gene OrientationCounterclockwise
Centisome Percentage:75.16
Left Sequence End3486982
Right Sequence End3488202
Gene Sequence:
>1221 bp
ATGTTTAAGTCTTTTTTCCCAAAGCCGGGAACGTTTTTTCTCTCGGCCTTCGTTTGGGCA
TTGATTGCCGTTATCTTCTGGCAAGCCGGTGGGGGTGACTGGGTGGCGCGTATCACCGGC
GCTTCCGGGCAGATCCCGATTAGCGCCGCGCGTTTCTGGTCGTTGGATTTCCTGATTTTT
TACGCTTACTACATTGTTTGCGTAGGACTTTTTGCATTGTTCTGGTTTATCTACAGCCCG
CATCGTTGGCAATACTGGTCAATACTCGGTACTGCACTGATCATCTTCGTCACCTGGTTT
TTGGTGGAAGTCGGGGTCGCCGTCAACGCCTGGTATGCGCCGTTCTATGATCTGATTCAA
ACCGCGCTAAGTTCGCCGCATAAAGTCACCATCGAACAATTTTACCGCGAAGTGGGCGTC
TTTCTGGGGATTGCGCTGATCGCTGTGGTGATCAGTGTGCTGAACAACTTCTTTGTCAGT
CACTACGTGTTCCGCTGGCGTACAGCGATGAACGAATATTACATGGCGAACTGGCAACAA
CTGCGTCATATCGAAGGGGCCGCACAGCGTGTGCAGGAAGACACCATGCGTTTTGCTTCA
ACGCTGGAGAATATGGGCGTCAGTTTTATCAACGCCATCATGACGTTGATCGCCTTCCTG
CCGGTGCTGGTAACGCTCTCCGCGCATGTGCCGGAGCTGCCGATTATCGGGCACATTCCG
TATGGTCTGGTGATTGCCGCAATCGTCTGGTCGCTGATGGGGACCGGATTGCTGGCAGTG
GTAGGGATCAAACTGCCGGGGCTGGAGTTTAAAAACCAGCGTGTAGAGGCTGCCTACCGT
AAAGAGCTGGTTTATGGTGAAGACGATGCCACGCGCGCGACGCCGCCTACGGTACGCGAG
CTGTTTAGCGCCGTACGGAAAAACTATTTCCGCCTCTATTTTCACTATATGTATTTCAAC
ATCGCCCGCATTCTCTATTTGCAGGTCGATAACGTTTTCGGTTTGTTCTTGCTGTTTCCG
TCAATTGTTGCCGGTACGATTACGCTCGGCCTGATGACGCAGATTACCAACGTTTTTGGT
CAGGTTCGCGGTGCTTTCCAGTACCTGATTAACTCATGGACCACACTGGTTGAGTTGATG
TCTATCTACAAACGTCTGCGCAGCTTTGAACATGAGCTGGATGGTGACAAAATTCAGGAA
GTAACCCATACCTTGAGCTAA
Protein Properties
Pfam Domain Function:
Protein Residues:406
Protein Molecular Weight:43767
Protein Theoretical pI:6
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Acetylornithine/succinyldiaminopimelate aminotransferase
MAIEQTAITRATFDEVILPIYAPAEFIPVKGQGSRIWDQQGKEYVDFAGGIAVTALGHCH
PALVNALKTQGETLWHISNVFTNEPALRLGRKLIEATFAERVVFMNSGTEANETAFKLAR
HYACVRHSPFKTKIIAFHNAFHGRSLFTVSVGGQPKYSDGFGPKPADIIHVPFNDLHAVK
AVMDDHTCAVVVEPIQGEGGVTAATPEFLQGLRELCDQHQALLVFDEVQCGMGRTGDLFA
YMHYGVTPDILTSAKALGGGFPISAMLTTAEIASAFHPGSHGSTYGGNPLACAVAGAAFD
IINTPEVLEGIQAKRQRFVDHLQKIDQQYDVFSDIRGMGLLIGAELKPQYKGRARDFLYA
GAEAGVMVLNAGPDVMRFAPSLVVEDADIDEGMQRFAHAVAKVVGA
References
External Links:
ResourceLink
Uniprot ID:P18335
Uniprot Name:ARGD_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:85674518
Ecogene ID:EG10066
Ecocyc:EG10066
ColiBase:b3359
Kegg Gene:b3359
EchoBASE ID:EB0064
CCDB:ARGD_ECOLI
BacMap:16131238
General Reference:
  • Blattner, F. R., Plunkett, G. 3rd, Bloch, C. A., Perna, N. T., Burland, V., Riley, M., Collado-Vides, J., Glasner, J. D., Rode, C. K., Mayhew, G. F., Gregor, J., Davis, N. W., Kirkpatrick, H. A., Goeden, M. A., Rose, D. J., Mau, B., Shao, Y. (1997). "The complete genome sequence of Escherichia coli K-12." Science 277:1453-1462. Pubmed: 9278503
  • Hayashi, K., Morooka, N., Yamamoto, Y., Fujita, K., Isono, K., Choi, S., Ohtsubo, E., Baba, T., Wanner, B. L., Mori, H., Horiuchi, T. (2006). "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Mol Syst Biol 2:2006.0007. Pubmed: 16738553
  • 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. Pubmed: 2199330
  • Ledwidge, R., Blanchard, J. S. (1999). "The dual biosynthetic capability of N-acetylornithine aminotransferase in arginine and lysine biosynthesis." Biochemistry 38:3019-3024. Pubmed: 10074354
  • Link, A. J., Robison, K., Church, G. M. (1997). "Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12." Electrophoresis 18:1259-1313. Pubmed: 9298646