N-succinylarginine dihydrolase

Details

Name
N-succinylarginine dihydrolase
Synonyms
  • 3.5.3.23
  • ydjT
Gene Name
astB
Organism
Escherichia coli (strain K12)
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
Functions
N-succinylarginine dihydrolase activity
Processes
arginine catabolic process / arginine catabolic process to glutamate / arginine catabolic process to succinate
General Function
N-succinylarginine dihydrolase activity
Specific Function
Catalyzes the hydrolysis of N(2)-succinylarginine into N(2)-succinylornithine, ammonia and CO(2).
Pfam Domain Function
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
ResourceLink
UniProtKB IDP76216
UniProtKB Entry NameASTB_ECOLI
GenBank Protein ID1788040
GenBank Gene IDU00096
General References
  1. 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]
  2. 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]
  3. 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]
  4. 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]
  5. 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]
  6. 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]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB02501N(2)-succinyl-L-arginineexperimentalunknownDetails
DB03582N~2~-SuccinylornithineexperimentalunknownDetails