Identification |
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Name: | Arginine N-succinyltransferase |
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Synonyms: | |
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Gene Name: | astA |
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Enzyme Class: | |
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Biological Properties |
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General Function: | Involved in arginine N-succinyltransferase activity |
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Specific Function: | Catalyzes the transfer of succinyl-CoA to arginine to produce N(2)-succinylarginine |
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Cellular Location: | Not Available |
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SMPDB Pathways: | |
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KEGG Pathways: | - Arginine and proline metabolism ec00330
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KEGG Reactions: | |
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SMPDB Reactions: | |
1.0 | + | 1.0Succinyl-CoA | + | 1.0 | → | 1.0 | + | 1.0 | + | 1.0 N2-succinyl-L-arginine | + | 1.0 |
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EcoCyc Reactions: | |
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Metabolites: | |
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GO Classification: | Function |
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acyltransferase activity | arginine N-succinyltransferase activity | catalytic activity | N-acyltransferase activity | N-succinyltransferase activity | transferase activity | transferase activity, transferring acyl groups | transferase activity, transferring acyl groups other than amino-acyl groups | Process |
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arginine catabolic 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 |
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Gene Properties |
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Blattner: | b1747 |
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Gene Orientation | Counterclockwise |
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Centisome Percentage: | 39.39 |
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Left Sequence End | 1827755 |
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Right Sequence End | 1828789 |
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Gene Sequence: | >1035 bp
ATGGCAAAGCCGATCATCACGCTCAATGGCCTAAAAATCGTCATTATGTTGGGAATGCTG
GTCATTATTCTCTGCGGTATCCGTTTTGCCGCCGAGATCATCGTGCCGTTTATTCTCGCA
TTATTTATTGCTGTTATTCTTAACCCGCTGGTGCAACACATGGTCCGCTGGCGTGTGCCG
CGTGTACTGGCGGTGTCGATTTTGATGACCATCATCGTGATGGCGATGGTGTTGCTATTA
GCTTATCTGGGTTCCGCGCTCAACGAGTTGACGCGGACGTTACCGCAATATCGCAACTCT
ATTATGACGCCGCTGCAAGCGCTTGAACCGTTGTTGCAACGCGTAGGGATTGACGTCTCA
GTTGACCAGCTGGCGCATTATATTGATCCGAACGCGGCGATGACGTTGCTCACCAACTTA
TTGACGCAGTTATCTAATGCCATGTCATCAATATTTTTATTGCTGCTGACGGTGCTGTTT
ATGCTGCTCGAAGTGCCACAATTGCCCGGAAAATTTCAGCAAATGATGGCGCGTCCGGTT
GAAGGGATGGCGGCGATTCAACGTGCGATTGACAGTGTTTCTCATTATCTGGTGCTGAAA
ACAGCCATCAGCATCATCACCGGCCTGGTCGCCTGGGCGATGCTCGCCGCACTCGATGTT
CGCTTCGCTTTTGTCTGGGGATTGCTGGCCTTTGCGCTTAATTACATCCCGAATATTGGT
TCAGTCCTCGCGGCAATCCCCCCTATCGCTCAGGTACTGGTGTTTAATGGCTTCTACGAA
GCGTTGCTGGTGCTGGCGGGATATCTGCTGATTAATCTGGTCTTCGGCAATATTCTGGAG
CCGCGTATCATGGGGCGTGGGCTGGGGCTTTCCACATTGGTGGTATTTTTGTCGTTGATT
TTTTGGGGATGGTTGTTAGGACCGGTGGGTATGCTGCTTTCCGTGCCGTTGACAATTATT
GTCAAAATTGCGCTTGAACAAACAGCGGGAGGTCAAAGCATCGCCGTTCTGTTAAGCGAT
CTCAATAAAGAGTGA |
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Protein Properties |
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Pfam Domain Function: | |
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Protein Residues: | 344 |
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Protein Molecular Weight: | 38456 |
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Protein Theoretical pI: | 6 |
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Signaling Regions: | |
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Transmembrane Regions: | |
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Protein Sequence: | >Arginine N-succinyltransferase
MMVIRPVERSDVSALMQLASKTGGGLTSLPANEATLSARIERAIKTWQGELPKSEQGYVF
VLEDSETGTVAGICAIEVAVGLNDPWYNYRVGTLVHASKELNVYNALPTLFLSNDHTGSS
ELCTLFLDPDWRKEGNGYLLSKSRFMFMAAFRDKFNDKVVAEMRGVIDEHGYSPFWQSLG
KRFFSMDFSRADFLCGTGQKAFIAELMPKHPIYTHFLSQEAQDVIGQVHPQTAPARAVLE
KEGFRYRNYIDIFDGGPTLECDIDRVRAIRKSRLVEVAEGQPAQGDFPACLVANENYHHF
RVVLVRTDPATERLILTAAQLDALKCHAGDRVRLVRLCAEEKTA |
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References |
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External Links: | |
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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
- Kiupakis, A. K., Reitzer, L. (2002). "ArgR-independent induction and ArgR-dependent superinduction of the astCADBE operon in Escherichia coli." J Bacteriol 184:2940-2950. Pubmed: 12003934
- Schneider, B. L., Kiupakis, A. K., Reitzer, L. J. (1998). "Arginine catabolism and the arginine succinyltransferase pathway in Escherichia coli." J Bacteriol 180:4278-4286. Pubmed: 9696779
- Shirai, H., Mizuguchi, K. (2003). "Prediction of the structure and function of AstA and AstB, the first two enzymes of the arginine succinyltransferase pathway of arginine catabolism." FEBS Lett 555:505-510. Pubmed: 14675764
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