Identification
Name:N-succinylarginine dihydrolase
Synonyms:Not Available
Gene Name:astB
Enzyme Class:
Biological Properties
General Function:Involved in N-succinylarginine dihydrolase activity
Specific Function:Catalyzes the hydrolysis of N(2)-succinylarginine into N(2)-succinylornithine, ammonia and CO(2)
Cellular Location:Cytoplasmic
SMPDB Pathways:
KEGG Pathways:
  • Arginine and proline metabolism ec00330
KEGG Reactions:
Thumb+2 ThumbThumb+Thumb+2 Thumb
Thumb+ThumbThumb+Thumb+Thumb
SMPDB Reactions:
N2-succinyl-L-arginine+2 Thumb+2 Thumb+ThumbThumb+2 Thumb+Thumb
EcoCyc Reactions:
Thumb+ThumbThumb+Thumb+Thumb
Complex Reactions:
2 Thumb+2 Thumb+ThumbThumb+2 Thumb+Thumb
Thumb+2 ThumbThumb+2 Thumb+Thumb
Metabolites:
ECMDB IDNameView
ECMDB24190 N2-succinyl-L-arginineMetaboCard
ECMDB00051AmmoniaMetaboCard
ECMDB21186AmmoniumMetaboCard
ECMDB04030Carbon dioxideMetaboCard
ECMDB21225Hydrogen ionMetaboCard
ECMDB20179N2-Succinyl-L-arginineMetaboCard
ECMDB01199N2-Succinyl-L-ornithineMetaboCard
ECMDB00494WaterMetaboCard
GO Classification:
Function
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
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:b1745
Gene OrientationCounterclockwise
Centisome Percentage:39.33
Left Sequence End1824940
Right Sequence End1826283
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
Protein Properties
Pfam Domain Function:
Protein Residues:447
Protein Molecular Weight:49298
Protein Theoretical pI:6
PDB File:1YNH
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>N-succinylarginine dihydrolase
MNAWEVNFDGLVGLTHHYAGLSFGNEASTRHRFQVSNPRLAAKQGLLKMKALADAGFPQA
VIPPHERPFIPVLRQLGFSGSDEQVLEKVARQAPHWLSSVSSASPMWVANAATIAPSADT
LDGKVHLTVANLNNKFHRSLEAPVTESLLKAIFNDEEKFSVHSALPQVALLGDEGAANHN
RLGGHYGEPGMQLFVYGREEGNDTRPSRYPARQTREASEAVARLNQVNPQQVIFAQQNPD
VIDQGVFHNDVIAVSNRQVLFCHQQAFARQSQLLANLRARVNGFMAIEVPATQVSVSDTV
STYLFNSQLLSRDDGSMMLVLPQECREHAGVWGYLNELLAADNPISELKVFDLRESMANG
GGPACLRLRVVLTEEERRAVNPAVMMNDTLFNALNDWVDRYYRDRLTAADLADPQLLREG
REALDVLSQLLNLGSVYPFQREGGGNG
References
External Links:
ResourceLink
Uniprot ID:P76216
Uniprot Name:ASTB_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:4062469
PDB ID:1YNH
Ecogene ID:EG13996
Ecocyc:EG13996
ColiBase:b1745
Kegg Gene:b1745
EchoBASE ID:EB3752
CCDB:ASTB_ECOLI
BacMap:16129699
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