T3DB: Argininosuccinate synthase

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 ATP binding argininosuccinate synthase activity Processes urea cycle arginine biosynthetic process argininosuccinate metabolic process Components cytoplasm cytosol
General Function	Atp binding
Specific Function	Not Available
Pfam Domain Function	Arginosuc_synth (PF00764 )
Transmembrane Regions	Not Available
GenBank Protein ID	145342
UniProtKB ID	P0A6E4
UniProtKB Entry Name	ASSY_ECOLI
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
GenBank Gene ID	M35236
GeneCard ID	Not Available
GenAtlas ID	Not Available
HGNC ID	Not Available
Chromosome Location	Not Available
Locus	Not Available
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. 2123815 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. 9278503 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. 16738553 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. 9298646 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. 10666579 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. 11738042 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. 11809762