N-succinylarginine dihydrolase
Details
- Name
- N-succinylarginine dihydrolase
- Kind
- protein
- Synonyms
- 3.5.3.23
- ydjT
- Gene Name
- astB
- UniProtKB Entry
- P76216Swiss-Prot
- Organism
- Escherichia coli (strain K12)
- NCBI Taxonomy ID
- 83333
- Amino acid sequence
>lcl|BSEQ0011342|N-succinylarginine dihydrolase MNAWEVNFDGLVGLTHHYAGLSFGNEASTRHRFQVSNPRLAAKQGLLKMKALADAGFPQA VIPPHERPFIPVLRQLGFSGSDEQVLEKVARQAPHWLSSVSSASPMWVANAATIAPSADT LDGKVHLTVANLNNKFHRSLEAPVTESLLKAIFNDEEKFSVHSALPQVALLGDEGAANHN RLGGHYGEPGMQLFVYGREEGNDTRPSRYPARQTREASEAVARLNQVNPQQVIFAQQNPD VIDQGVFHNDVIAVSNRQVLFCHQQAFARQSQLLANLRARVNGFMAIEVPATQVSVSDTV STYLFNSQLLSRDDGSMMLVLPQECREHAGVWGYLNELLAADNPISELKVFDLRESMANG GGPACLRLRVVLTEEERRAVNPAVMMNDTLFNALNDWVDRYYRDRLTAADLADPQLLREG REALDVLSQLLNLGSVYPFQREGGGNG
- Number of residues
- 447
- Molecular Weight
- 49298.18
- Theoretical pI
- 6.06
- GO Classification
- FunctionsN-succinylarginine dihydrolase activityProcessesarginine catabolic process / arginine catabolic process to glutamate / arginine catabolic process to succinate
- General Function
- Catalyzes the hydrolysis of N(2)-succinylarginine into N(2)-succinylornithine, ammonia and CO(2).
- Specific Function
- N-succinylarginine dihydrolase activity
- Pfam Domain Function
- AstB (PF04996)
- Signal Regions
- Not Available
- Transmembrane Regions
- Not Available
- Cellular Location
- Cytoplasmic
- Gene sequence
>lcl|BSEQ0011343|N-succinylarginine dihydrolase (astB) ATGAACGCCTGGGAAGTCAATTTCGACGGGCTGGTAGGGCTGACGCATCATTACGCGGGC CTGTCGTTTGGTAATGAAGCCTCTACCCGTCACCGTTTTCAGGTGTCTAACCCGCGACTG GCGGCGAAGCAGGGCTTACTGAAAATGAAAGCCCTTGCCGATGCGGGATTCCCCCAGGCC GTGATCCCGCCGCACGAGCGTCCGTTTATTCCGGTGCTGCGTCAGTTGGGATTCAGTGGT AGCGATGAGCAGGTACTGGAAAAAGTTGCACGCCAGGCACCGCACTGGCTTTCCAGCGTC AGTTCCGCTTCGCCAATGTGGGTAGCCAATGCGGCAACGATCGCGCCATCTGCCGATACG CTGGATGGCAAAGTGCATCTCACCGTTGCCAACCTGAACAATAAATTTCACCGTTCGCTG GAAGCGCCCGTCACTGAATCGCTGTTAAAAGCGATTTTTAACGACGAAGAGAAATTTAGC GTCCATTCGGCGTTGCCACAGGTAGCGTTGCTCGGTGATGAGGGGGCGGCAAACCACAAT CGTCTCGGCGGTCATTACGGTGAACCGGGTATGCAACTTTTTGTCTACGGGCGAGAAGAA GGCAATGATACCCGGCCTTCCCGTTATCCGGCGCGACAGACTCGCGAAGCCAGCGAGGCG GTGGCAAGGCTGAATCAGGTGAATCCCCAACAGGTGATTTTCGCCCAGCAAAACCCGGAC GTTATCGACCAGGGCGTTTTTCATAATGACGTGATTGCCGTGAGTAACCGCCAGGTGCTG TTTTGCCACCAACAGGCGTTCGCTCGCCAGTCACAGTTACTGGCAAACCTGCGTGCGCGG GTCAATGGTTTTATGGCGATAGAAGTTCCGGCAACTCAGGTTTCCGTGTCTGATACGGTG TCTACCTATCTGTTTAACAGCCAACTGCTGAGCCGCGATGATGGTTCCATGATGTTGGTG CTGCCTCAGGAGTGTCGGGAACACGCCGGAGTATGGGGTTATCTCAATGAACTCCTTGCC GCTGACAACCCGATTAGCGAACTAAAAGTCTTTGATTTACGTGAAAGCATGGCGAATGGC GGCGGCCCGGCGTGCCTGCGGTTGCGGGTGGTATTGACAGAAGAAGAACGCCGGGCGGTG AATCCGGCGGTGATGATGAACGATACGCTGTTTAATGCGCTCAATGACTGGGTGGATCGT TACTACCGCGATCGCCTTACTGCTGCCGATCTGGCCGACCCGCAATTGCTGCGCGAAGGG CGGGAAGCACTGGATGTATTGAGCCAATTACTGAATCTCGGTTCGGTTTATCCGTTCCAG CGCGAGGGAGGGGGCAATGGATAA
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID P76216 UniProtKB Entry Name ASTB_ECOLI GenBank Protein ID 1788040 GenBank Gene ID U00096 PDB ID(s) 1YNF, 1YNH, 1YNI KEGG ID ecj:JW1734 NCBI Gene ID 946259 - General References
- Blattner FR, Plunkett G 3rd, Bloch CA, Perna NT, Burland V, Riley M, Collado-Vides J, Glasner JD, Rode CK, Mayhew GF, Gregor J, Davis NW, Kirkpatrick HA, Goeden MA, Rose DJ, Mau B, Shao Y: The complete genome sequence of Escherichia coli K-12. Science. 1997 Sep 5;277(5331):1453-62. [Article]
- Hayashi K, Morooka N, Yamamoto Y, Fujita K, Isono K, Choi S, Ohtsubo E, Baba T, Wanner BL, Mori H, Horiuchi T: Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110. Mol Syst Biol. 2006;2:2006.0007. Epub 2006 Feb 21. [Article]
- Schneider BL, Kiupakis AK, Reitzer LJ: Arginine catabolism and the arginine succinyltransferase pathway in Escherichia coli. J Bacteriol. 1998 Aug;180(16):4278-86. [Article]
- Kiupakis AK, Reitzer L: ArgR-independent induction and ArgR-dependent superinduction of the astCADBE operon in Escherichia coli. J Bacteriol. 2002 Jun;184(11):2940-50. [Article]
- Shirai H, Mizuguchi K: Prediction of the structure and function of AstA and AstB, the first two enzymes of the arginine succinyltransferase pathway of arginine catabolism. FEBS Lett. 2003 Dec 18;555(3):505-10. [Article]
- Tocilj A, Schrag JD, Li Y, Schneider BL, Reitzer L, Matte A, Cygler M: 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. 2005 Apr 22;280(16):15800-8. Epub 2005 Feb 9. [Article]
Associated Data
- Drug Relations
Drug Drug group Pharmacological action? Type Actions Details N(2)-succinyl-L-arginine experimental unknown target Details N~2~-Succinylornithine experimental unknown target Details