Identification
Name:Aspartate aminotransferase
Synonyms:
  • AspAT
  • Transaminase A
Gene Name:aspC
Enzyme Class:
Biological Properties
General Function:Involved in transferase activity
Specific Function:L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate
Cellular Location:Cytoplasm
SMPDB Pathways:
KEGG Pathways:
  • Alanine, aspartate and glutamate metabolism ec00250
  • Arginine and proline metabolism ec00330
  • Carbon fixation in photosynthetic organisms ec00710
  • Cysteine and methionine metabolism ec00270
  • Isoquinoline alkaloid biosynthesis ec00950
  • Metabolic pathways eco01100
  • Microbial metabolism in diverse environments ec01120
  • Novobiocin biosynthesis ec00401
  • Phenylalanine metabolism ec00360
  • Phenylalanine, tyrosine and tryptophan biosynthesis ec00400
  • Tropane, piperidine and pyridine alkaloid biosynthesis ec00960
  • Tyrosine metabolism ec00350
KEGG Reactions:
Thumb+ThumbThumb+Thumb
Thumb+ThumbThumb+Thumb
Thumb+ThumbThumb+Thumb
Thumb+ThumbThumb+Thumb
Thumb+ThumbThumb+Thumb
Thumb+ThumbThumb+Thumb
Thumb+ThumbThumb+Thumb
Thumb+ThumbThumb+Thumb
L-erythro-4-Hydroxyglutamate+ThumbThumb+Thumb
SMPDB Reactions:
L-Aspartic acid+Thumb+ThumbThumb+L-Glutamic acid+Thumb
L-Aspartic acid + Oxoglutaric acid + L-Aspartic acidOxalacetic acid + L-Glutamic acid + L-Glutamate
ReactionCard
L-Glutamic acid+Thumb+ThumbL-Aspartic acid+Thumb+Thumb
L-Glutamic acid + Oxalacetic acid + L-Glutamate → L-Aspartic acid + Oxoglutaric acid + L-Aspartic acid
ReactionCard
Thumb+L-Glutamic acid+ThumbThumb+L-Phenylalanine+Thumb
Thumb+ThumbThumb+Thumb
Thumb+ThumbThumb+Thumb
EcoCyc Reactions:
Thumb+ThumbThumb+Thumb
Complex Reactions:
Thumb+ThumbThumb+Thumb
Metabolites:
ECMDB IDNameView
ECMDB013683-Mercaptopyruvic acidMetaboCard
ECMDB009963-SulfinoalanineMetaboCard
ECMDB014053-Sulfinylpyruvic acidMetaboCard
ECMDB210023-Sulfopyruvic acidMetaboCard
ECMDB007074-Hydroxyphenylpyruvic acidMetaboCard
ECMDB02812alpha-KetoglutarateMetaboCard
ECMDB02757Cysteic acidMetaboCard
ECMDB20135D-4-Hydroxy-2-oxoglutarateMetaboCard
ECMDB00191L-Aspartic acidMetaboCard
ECMDB00574L-CysteineMetaboCard
ECMDB00148L-GlutamateMetaboCard
ECMDB00159L-PhenylalanineMetaboCard
ECMDB00158L-TyrosineMetaboCard
ECMDB00223Oxalacetic acidMetaboCard
ECMDB04123Oxoglutaric acidMetaboCard
ECMDB00205Phenylpyruvic acidMetaboCard
GO Classification:
Function
binding
catalytic activity
cofactor binding
pyridoxal phosphate binding
transaminase activity
transferase activity
transferase activity, transferring nitrogenous groups
Process
biosynthetic process
cellular amino acid and derivative metabolic process
cellular amino acid metabolic process
cellular metabolic process
metabolic process
Gene Properties
Blattner:b0928
Gene OrientationCounterclockwise
Centisome Percentage:21.20
Left Sequence End983742
Right Sequence End984932
Gene Sequence:
>1191 bp
ATGTTTGAGAACATTACCGCCGCTCCTGCCGACCCGATTCTGGGCCTGGCCGATCTGTTT
CGTGCCGATGAACGTCCCGGCAAAATTAACCTCGGGATTGGTGTCTATAAAGATGAGACG
GGCAAAACCCCGGTACTGACCAGCGTGAAAAAGGCTGAACAGTATCTGCTCGAAAATGAA
ACCACCAAAAATTACCTCGGCATTGACGGCATCCCTGAATTTGGTCGCTGCACTCAGGAA
CTGCTGTTTGGTAAAGGTAGCGCCCTGATCAATGACAAACGTGCTCGCACGGCACAGACT
CCGGGGGGCACTGGCGCACTACGCGTGGCTGCCGATTTCCTGGCAAAAAATACCAGCGTT
AAGCGTGTGTGGGTGAGCAACCCAAGCTGGCCGAACCATAAGAGCGTCTTTAACTCTGCA
GGTCTGGAAGTTCGTGAATACGCTTATTATGATGCGGAAAATCACACTCTTGACTTCGAT
GCACTGATTAACAGCCTGAATGAAGCTCAGGCTGGCGACGTAGTGCTGTTCCATGGCTGC
TGCCATAACCCAACCGGTATCGACCCTACGCTGGAACAATGGCAAACACTGGCACAACTC
TCCGTTGAGAAAGGCTGGTTACCGCTGTTTGACTTCGCTTACCAGGGTTTTGCCCGTGGT
CTGGAAGAAGATGCTGAAGGACTGCGCGCTTTCGCGGCTATGCATAAAGAGCTGATTGTT
GCCAGTTCCTACTCTAAAAACTTTGGCCTGTACAACGAGCGTGTTGGCGCTTGTACTCTG
GTTGCTGCCGACAGTGAAACCGTTGATCGCGCATTCAGCCAAATGAAAGCGGCGATTCGC
GCTAACTACTCTAACCCACCAGCACACGGCGCTTCTGTTGTTGCCACCATCCTGAGCAAC
GATGCGTTACGTGCGATTTGGGAACAAGAGCTGACTGATATGCGCCAGCGTATTCAGCGT
ATGCGTCAGTTGTTCGTCAATACGCTGCAGGAAAAAGGCGCAAACCGCGACTTCAGCTTT
ATCATCAAACAGAACGGCATGTTCTCCTTCAGTGGCCTGACAAAAGAACAAGTGCTGCGT
CTGCGCGAAGAGTTTGGCGTATATGCGGTTGCTTCTGGTCGCGTAAATGTGGCCGGGATG
ACACCAGATAACATGGCTCCGCTGTGCGAAGCGATTGTGGCAGTGCTGTAA
Protein Properties
Pfam Domain Function:
Protein Residues:396
Protein Molecular Weight:43573
Protein Theoretical pI:6
PDB File:1CQ8
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Aspartate aminotransferase
MFENITAAPADPILGLADLFRADERPGKINLGIGVYKDETGKTPVLTSVKKAEQYLLENE
TTKNYLGIDGIPEFGRCTQELLFGKGSALINDKRARTAQTPGGTGALRVAADFLAKNTSV
KRVWVSNPSWPNHKSVFNSAGLEVREYAYYDAENHTLDFDALINSLNEAQAGDVVLFHGC
CHNPTGIDPTLEQWQTLAQLSVEKGWLPLFDFAYQGFARGLEEDAEGLRAFAAMHKELIV
ASSYSKNFGLYNERVGACTLVAADSETVDRAFSQMKAAIRANYSNPPAHGASVVATILSN
DALRAIWEQELTDMRQRIQRMRQLFVNTLQEKGANRDFSFIIKQNGMFSFSGLTKEQVLR
LREEFGVYAVASGRVNVAGMTPDNMAPLCEAIVAVL
References
External Links:
ResourceLink
Uniprot ID:P00509
Uniprot Name:AAT_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:1651449
PDB ID:1CQ8
Ecogene ID:EG10096
Ecocyc:EG10096
ColiBase:b0928
Kegg Gene:b0928
EchoBASE ID:EB0094
CCDB:AAT_ECOLI
BacMap:16128895
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
  • Danishefsky, A. T., Onnufer, J. J., Petsko, G. A., Ringe, D. (1991). "Activity and structure of the active-site mutants R386Y and R386F of Escherichia coli aspartate aminotransferase." Biochemistry 30:1980-1985. Pubmed: 1993208
  • Fotheringham, I. G., Dacey, S. A., Taylor, P. P., Smith, T. J., Hunter, M. G., Finlay, M. E., Primrose, S. B., Parker, D. M., Edwards, R. M. (1986). "The cloning and sequence analysis of the aspC and tyrB genes from Escherichia coli K12. Comparison of the primary structures of the aspartate aminotransferase and aromatic aminotransferase of E. coli with those of the pig aspartate aminotransferase isoenzymes." Biochem J 234:593-604. Pubmed: 3521591
  • 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
  • Inoue, K., Kuramitsu, S., Okamoto, A., Hirotsu, K., Higuchi, T., Kagamiyama, H. (1991). "Site-directed mutagenesis of Escherichia coli aspartate aminotransferase: role of Tyr70 in the catalytic processes." Biochemistry 30:7796-7801. Pubmed: 1868057
  • Kondo, K., Wakabayashi, S., Kagamiyama, H. (1987). "Structural studies on aspartate aminotransferase from Escherichia coli. Covalent structure." J Biol Chem 262:8648-8657. Pubmed: 3298240
  • Kondo, K., Wakabayashi, S., Yagi, T., Kagamiyama, H. (1984). "The complete amino acid sequence of aspartate aminotransferase from Escherichia coli: sequence comparison with pig isoenzymes." Biochem Biophys Res Commun 122:62-67. Pubmed: 6378205
  • Kuramitsu, S., Okuno, S., Ogawa, T., Ogawa, H., Kagamiyama, H. (1985). "Aspartate aminotransferase of Escherichia coli: nucleotide sequence of the aspC gene." J Biochem 97:1259-1262. Pubmed: 3897210
  • 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
  • Liu, D., Pozharski, E., Lepore, B. W., Fu, M., Silverman, R. B., Petsko, G. A., Ringe, D. (2007). "Inactivation of Escherichia coli L-aspartate aminotransferase by (S)-4-amino-4,5-dihydro-2-thiophenecarboxylic acid reveals "a tale of two mechanisms"." Biochemistry 46:10517-10527. Pubmed: 17713924
  • Mahon, M. M., Graber, R., Christen, P., Malthouse, J. P. (1999). "The aspartate aminotransferase-catalysed exchange of the alpha-protons of aspartate and glutamate: the effects of the R386A and R292V mutations on this exchange reaction." Biochim Biophys Acta 1434:191-201. Pubmed: 10556573
  • Mizuguchi, H., Hayashi, H., Okada, K., Miyahara, I., Hirotsu, K., Kagamiyama, H. (2001). "Strain is more important than electrostatic interaction in controlling the pKa of the catalytic group in aspartate aminotransferase." Biochemistry 40:353-360. Pubmed: 11148029
  • Oshima, T., Aiba, H., Baba, T., Fujita, K., Hayashi, K., Honjo, A., Ikemoto, K., Inada, T., Itoh, T., Kajihara, M., Kanai, K., Kashimoto, K., Kimura, S., Kitagawa, M., Makino, K., Masuda, S., Miki, T., Mizobuchi, K., Mori, H., Motomura, K., Nakamura, Y., Nashimoto, H., Nishio, Y., Saito, N., Horiuchi, T., et, a. l. .. (1996). "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map." DNA Res 3:137-155. Pubmed: 8905232
  • Oue, S., Okamoto, A., Yano, T., Kagamiyama, H. (1999). "Redesigning the substrate specificity of an enzyme by cumulative effects of the mutations of non-active site residues." J Biol Chem 274:2344-2349. Pubmed: 9891001
  • Smith, D. L., Almo, S. C., Toney, M. D., Ringe, D. (1989). "2.8-A-resolution crystal structure of an active-site mutant of aspartate aminotransferase from Escherichia coli." Biochemistry 28:8161-8167. Pubmed: 2513875
  • Yano, T., Kuramitsu, S., Tanase, S., Morino, Y., Hiromi, K., Kagamiyama, H. (1991). "The role of His143 in the catalytic mechanism of Escherichia coli aspartate aminotransferase." J Biol Chem 266:6079-6085. Pubmed: 2007566