Argininosuccinate synthase

Details

Name
Argininosuccinate synthase
Synonyms
  • 6.3.4.5
  • Citrulline--aspartate ligase
Gene Name
argG
Organism
Escherichia coli (strain K12)
Amino acid sequence
>lcl|BSEQ0011251|Argininosuccinate synthase
MTTILKHLPVGQRIGIAFSGGLDTSAALLWMRQKGAVPYAYTANLGQPDEEDYDAIPRRA
MEYGAENARLIDCRKQLVAEGIAAIQCGAFHNTTGGLTYFNTTPLGRAVTGTMLVAAMKE
DGVNIWGDGSTYKGNDIERFYRYGLLTNAELQIYKPWLDTDFIDELGGRHEMSEFMIACG
FDYKMSVEKAYSTDSNMLGATHEAKDLEYLNSSVKIVNPIMGVKFWDESVKIPAEEVTVR
FEQGHPVALNGKTFSDDVEMMLEANRIGGRHGLGMSDQIENRIIEAKSRGIYEAPGMALL
HIAYERLLTGIHNEDTIEQYHAHGRQLGRLLYQGRWFDSQALMLRDSLQRWVASQITGEV
TLELRRGNDYSILNTVSENLTYKPERLTMEKGDSVFSPDDRIGQLTMRNLDITDTREKLF
GYAKTGLLSSSAASGVPQVENLENKGQ
Number of residues
447
Molecular Weight
49898.01
Theoretical pI
5.04
GO Classification
Functions
argininosuccinate synthase activity / ATP binding
Processes
arginine biosynthetic process / argininosuccinate metabolic process / urea cycle
Components
cytoplasm / cytosol
General Function
Atp binding
Specific Function
Not Available
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Cytoplasm
Gene sequence
>lcl|BSEQ0011252|Argininosuccinate synthase (argG)
ATGACGACGATTCTCAAGCATCTCCCGGTAGGTCAACGTATTGGTATCGCTTTTTCTGGC
GGTCTGGACACCAGTGCCGCACTGCTGTGGATGCGACAAAAGGGAGCGGTTCCTTATGCA
TATACTGCAAACCTGGGCCAGCCAGACGAAGAGGATTATGATGCGATCCCTCGTCGTGCC
ATGGAATACGGCGCGGAGAACGCACGTCTGATCGACTGCCGCAAACAACTGGTGGCCGAA
GGTATTGCCGCTATTCAGTGTGGCGCATTTCATAACACCACCGGCGGCCTGACCTATTTC
AACACGACGCCGCTGGGCCGCGCCGTGACTGGTACCATGCTGGTTGCTGCGATGAAAGAA
GATGGCGTGAATATCTGGGGTGACGGTAGCACCTACAAAGGAAACGATATCGAACGTTTC
TATCGTTATGGTCTGCTGACCAATGCTGAACTGCAGATTTACAAACCGTGGCTTGATACT
GACTTTATTGATGAACTGGGCGGCCGTCATGAGATGTCTGAATTTATGATTGCCTGCGGT
TTCGACTACAAAATGTCTGTCGAAAAAGCCTACTCCACAGACTCCAACATGCTTGGTGCA
ACGCATGAAGCGAAGGATCTGGAATACCTCAACTCCAGCGTCAAAATCGTCAACCCGATT
ATGGGCGTGAAATTCTGGGATGAGAGCGTGAAGATCCCGGCAGAAGAAGTCACAGTACGC
TTTGAACAAGGTCATCCGGTGGCGCTGAACGGTAAAACCTTTAGCGACGACGTAGAAATG
ATGCTGGAAGCTAACCGCATCGGCGGTCGTCACGGCCTGGGCATGAGCGACCAGATTGAA
AACCGTATCATCGAAGCGAAAAGCCGTGGTATTTACGAAGCTCCGGGGATGGCACTGCTG
CACATTGCGTATGAACGCCTGTTGACCGGTATTCACAACGAAGACACCATTGAGCAGTAT
CACGCGCATGGTCGTCAGTTGGGCCGTCTGCTGTACCAGGGGCGTTGGTTTGACTCCCAG
GCGCTGATGCTGCGTGACTCTCTGCAACGCTGGGTTGCCAGCCAGATCACTGGTGAAGTT
ACCCTGGAGCTGCGCCGTGGGAACGATTATTCAATCCTGAATACCGTCTCAGAGAACCTG
ACCTACAAGCCAGAGCGTCTGACGATGGAAAAAGGCGACTCGGTGTTCTCGCCAGATGAT
CGTATTGGTCAATTGACCATGCGTAACCTGGATATCACTGATACCCGCGAGAAACTTTTC
GGTTATGCCAAAACTGGCCTGCTTTCCTCCTCTGCCGCTTCAGGCGTGCCGCAGGTGGAG
AATCTGGAAAACAAAGGCCAGTAA
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDP0A6E4
UniProtKB Entry NameASSY_ECOLI
GenBank Protein ID145342
GenBank Gene IDM35236
General References
  1. Van Vliet F, Crabeel M, Boyen A, Tricot C, Stalon V, Falmagne P, Nakamura Y, Baumberg S, Glansdorff N: Sequences of the genes encoding argininosuccinate synthetase in Escherichia coli and Saccharomyces cerevisiae: comparison with methanogenic archaebacteria and mammals. Gene. 1990 Oct 30;95(1):99-104. [Article]
  2. 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]
  3. 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]
  4. Link AJ, Robison K, Church GM: Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12. Electrophoresis. 1997 Aug;18(8):1259-313. [Article]
  5. Lemke C, Yeung M, Howell PL: Expression, purification, crystallization and preliminary X-ray analysis of Escherichia coli argininosuccinate synthetase. Acta Crystallogr D Biol Crystallogr. 1999 Dec;55(Pt 12):2028-30. [Article]
  6. Lemke CT, Howell PL: The 1.6 A crystal structure of E. coli argininosuccinate synthetase suggests a conformational change during catalysis. Structure. 2001 Dec;9(12):1153-64. [Article]
  7. Lemke CT, Howell PL: Substrate induced conformational changes in argininosuccinate synthetase. J Biol Chem. 2002 Apr 12;277(15):13074-81. Epub 2002 Jan 23. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails