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
- Functionsargininosuccinate synthase activity / ATP bindingProcessesarginine biosynthetic process / argininosuccinate metabolic process / urea cycleComponentscytoplasm / cytosol
- General Function
- Atp binding
- Specific Function
- Not Available
- Pfam Domain Function
- Arginosuc_synth (PF00764)
- 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
Resource Link UniProtKB ID P0A6E4 UniProtKB Entry Name ASSY_ECOLI GenBank Protein ID 145342 GenBank Gene ID M35236 - General References
- 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]
- 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]
- 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]
- 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]
- 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]
- 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 ID Name Drug group Pharmacological action? Actions Details