| Identification |
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| Name: | N-succinylarginine dihydrolase |
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| Synonyms: | Not Available |
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| Gene Name: | astB |
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| Enzyme Class: | |
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| Biological Properties |
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| General Function: | Involved in N-succinylarginine dihydrolase activity |
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| Specific Function: | Catalyzes the hydrolysis of N(2)-succinylarginine into N(2)-succinylornithine, ammonia and CO(2) |
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| Cellular Location: | Cytoplasmic |
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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 N2-succinyl-L-arginine | + | 2.0 | + | 2.0 | + | 1.0 | → | 1.0 | + | 2.0 | + | 1.0 |
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| EcoCyc Reactions: | |
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| Complex Reactions: | |
2.0 | + | 2.0 | + | 1.0 | → | 1.0 | + | 2.0 | + | 1.0 |
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| Metabolites: | |
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| GO Classification: | | Function |
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| catalytic activity | | hydrolase activity | | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds | | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines | | N-succinylarginine dihydrolase activity | | Process |
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| 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: | b1745 |
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| Gene Orientation | Counterclockwise |
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| Centisome Percentage: | 39.33 |
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| Left Sequence End | 1824940 |
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| Right Sequence End | 1826283 |
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| Gene Sequence: | >1344 bp
GTGAGCAATCTGTCGCTCGATTTTTCGGATAATACTTTTCAACCTCTGGCCGCGCGTATG
CGGCCAGAAAATTTAGCACAGTATATCGGCCAGCAACATTTGCTGGCTGCGGGGAAGCCG
TTGCCGCGCGCTATCGAAGCCGGGCATTTACATTCTATGATCCTCTGGGGGCCGCCGGGT
ACCGGCAAAACAACTCTCGCTGAAGTGATTGCCCGCTATGCGAACGCTGATGTGGAACGT
ATTTCTGCCGTCACCTCTGGCGTGAAAGAGATTCGCGAGGCGATCGAGCGCGCCCGGCAA
AACCGCAATGCAGGTCGCCGCACTATTCTTTTTGTTGACGAAGTTCACCGTTTCAACAAA
AGCCAGCAGGATGCATTTCTGCCACATATTGAAGACGGCACCATCACTTTTATTGGCGCA
ACCACTGAAAACCCGTCGTTTGAGCTTAATTCGGCACTGCTTTCCCGTGCCCGTGTCTAT
CTGTTGAAATCCCTGAGTACAGAGGATATTGAGCAAGTACTAACTCAGGCGATGGAAGAC
AAAACCCGTGGCTATGGTGGTCAGGATATTGTTCTGCCAGATGAAACACGACGCGCCATT
GCTGAACTGGTGAATGGCGACGCGCGCCGGGCGTTAAATACGCTGGAAATGATGGCGGAT
ATGGCCGAAGTCGATGATAGCGGTAAGCGGGTCCTGAAGCCTGAATTACTGACCGAAATC
GCCGGTGAACGTAGCGCCCGCTTTGATAACAAAGGCGATCGCTTTTACGATCTGATTTCC
GCACTGCATAAGTCGGTACGTGGTAGCGCACCCGATGCGGCGCTGTACTGGTATGCGCGA
ATTATTACCGCTGGTGGCGATCCGTTATATGTCGCGCGTCGCTGTCTGGCGATTGCGTCT
GAAGACGTCGGTAATGCCGATCCACGGGCGATGCAGGTGGCAATTGCGGCCTGGGATTGC
TTTACTCGCGTTGGCCCGGCGGAAGGTGAACGCGCCATTGCTCAGGCGATTGTTTACCTG
GCCTGCGCGCCAAAAAGCAACGCTGTCTACACTGCGTTTAAAGCCGCGCTGGCCGATGCT
CGCGAACGCCCGGATTATGACGTGCCGGTTCATTTGCGTAATGCGCCGACGAAATTAATG
AAGGAAATGGGCTACGGGCAGGAATATCGTTACGCTCATGATGAAGCAAACGCTTATGCT
GCCGGTGAGGTTTACTTCCCGCCGGAAATAGCACAAACACGCTATTATTTCCCGACAAAC
AGGGGCCTTGAAGGCAAGATTGGCGAAAAGCTCGCCTGGCTGGCTGAACAGGATCAAAAT
AGCCCCATAAAACGCTACCGTTAA |
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| Protein Properties |
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| Pfam Domain Function: | |
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| Protein Residues: | 447 |
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| Protein Molecular Weight: | 49298 |
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| Protein Theoretical pI: | 6 |
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| PDB File: | 1YNH |
| Signaling Regions: | |
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| Transmembrane Regions: | |
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| Protein Sequence: | >N-succinylarginine dihydrolase
MNAWEVNFDGLVGLTHHYAGLSFGNEASTRHRFQVSNPRLAAKQGLLKMKALADAGFPQA
VIPPHERPFIPVLRQLGFSGSDEQVLEKVARQAPHWLSSVSSASPMWVANAATIAPSADT
LDGKVHLTVANLNNKFHRSLEAPVTESLLKAIFNDEEKFSVHSALPQVALLGDEGAANHN
RLGGHYGEPGMQLFVYGREEGNDTRPSRYPARQTREASEAVARLNQVNPQQVIFAQQNPD
VIDQGVFHNDVIAVSNRQVLFCHQQAFARQSQLLANLRARVNGFMAIEVPATQVSVSDTV
STYLFNSQLLSRDDGSMMLVLPQECREHAGVWGYLNELLAADNPISELKVFDLRESMANG
GGPACLRLRVVLTEEERRAVNPAVMMNDTLFNALNDWVDRYYRDRLTAADLADPQLLREG
REALDVLSQLLNLGSVYPFQREGGGNG |
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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
- Tocilj, A., Schrag, J. D., Li, Y., Schneider, B. L., Reitzer, L., Matte, A., Cygler, M. (2005). "Crystal structure of N-succinylarginine dihydrolase AstB, bound to substrate and product, an enzyme from the arginine catabolic pathway of Escherichia coli." J Biol Chem 280:15800-15808. Pubmed: 15703173
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