Asparagine synthetase [glutamine-hydrolyzing] 1 (P49089)

Identification
NameAsparagine synthetase [glutamine-hydrolyzing] 1
Synonyms
  • Glutamine-dependent asparagine synthetase 1
Gene NameASN1
Enzyme Class
Biological Properties
General FunctionInvolved in asparagine synthase (glutamine-hydrolyzing) activity
Specific FunctionATP + L-aspartate + L-glutamine + H(2)O = AMP + diphosphate + L-asparagine + L-glutamate
Cellular LocationNot Available
SMPDB Pathways
Asparagine metabolismPW002274 ThumbThumb?image type=greyscaleThumb?image type=simple
Nitrogen metabolismPW002504 ThumbThumb?image type=greyscaleThumb?image type=simple
KEGG Pathways
Alanine, aspartate and glutamate metabolismec00250 Map00250
Nitrogen metabolismec00910 Map00910
SMPDB Reactions
L-Aspartic acid + water + Adenosine triphosphate + L-Glutamine → L-Asparagine + hydron + Adenosine monophosphate + L-Glutamic acid + Pyrophosphate
L-Aspartic acid + Adenosine triphosphate + Ammonium → L-Asparagine + Adenosine monophosphate + Pyrophosphate + hydron
Adenosine triphosphate + L-Aspartic acid + L-Glutamine + water → Adenosine monophosphate + Pyrophosphate + L-Asparagine + L-Glutamic acid
KEGG Reactions
L-Aspartic acid + Adenosine triphosphate + water + L-Glutamine → Adenosine monophosphate + Pyrophosphate + L-Asparagine + L-Glutamic acid + hydron
Metabolites
YMDB IDNameView
YMDB00002L-GlutamineShow
YMDB00097Adenosine monophosphateShow
YMDB00109Adenosine triphosphateShow
YMDB00219PyrophosphateShow
YMDB00226L-AsparagineShow
YMDB00271L-Glutamic acidShow
YMDB00423AmmoniumShow
YMDB00862hydronShow
YMDB00890waterShow
YMDB00896L-Aspartic acidShow
GO Classification
Component
Not Available
Function
carbon-nitrogen ligase activity, with glutamine as amido-N-donor
asparagine synthase (glutamine-hydrolyzing) activity
catalytic activity
ligase activity
ligase activity, forming carbon-nitrogen bonds
Process
cellular metabolic process
cellular amino acid and derivative metabolic process
cellular amino acid metabolic process
aspartate family amino acid metabolic process
asparagine metabolic process
asparagine biosynthetic process
metabolic process
Gene Properties
Chromosome Locationchromosome 16
LocusYPR145W
Gene Sequence>1719 bp ATGTGTGGTATTTTCGCCGCTTTCAGGCACGAAGACGTGCATAGATATAAGCCAAAGGCT CTACAACTATCAAAAAGAATCAGACACCGTGGTCCAGATTGGTCCGGTAATGCTATCAAG AACTCCACTATATTTGTTCATGAAAGACTAGCCATTGTCGGTGTGGAATCCGGTGCTCAA CCAATTACTTCTTCAGACGGAGAGTACATGCTATGTGTTAACGGTGAAATCTACAACCAC ATTCAATTAAGAGAAGAATGCGCAGACTACGAGTTTGGAACACTGAGTGACTGTGAGCCT ATCATCCCAATGTACTTAAAGCACGATATCGACGCTCCTAAGTACTTGGATGGTATGTTT GCTTGGACTCTTTACGACGCTAAACAAGATCGTATTGTGGCAGCCAGAGACCCAATCGGT ATTACGACATTATATATGGGACGCTCTTCCGCTTCTCCAAAGACCGTTTATTTTGCATCC GAACTAAAATGTTTGACTGACGACTGTGACACTATCACTGCATTCCCACCGGGCCACGTA TACGATTCTAAGACTGACAAGATCACCCGTTACTTCACACCAGATTGGCTGGACGAAAAA CGCATTCCTTCCACCCCAATAGATTACATGGCAATTAGACACTCCTTAGAAAAAGCCGTT AGAAAGAGATTAATGGCCGAAGTCCCATACGGTGTTCTATTGTCGGGTGGTTTGGACTCC TCTTTAATCGCTTCCATTGCTGCCCGTGAAACTGCAAAGGCCACTAACGATGTCGAACCA TCAACTTACGATAGTAAGGCAAGACATCTAGCAGGTATCGACGATGACGGTAAGCTACAC ACTGCTGGTTGGACAAGTCTCCATTCCTTTGCCATCGGTTTACCAAATGCTCCAGATTTG CAAGCCGCAAGAAAGGTTGCCAAATTCATCGGCTCTATTCATCATGAACACACCTTTACA TTACAAGAAGGTTTGGATGCTTTGGACGACGTGATCTACCATTTGGAAACTTACGACGTT ACCACTATCAGAGCTTCCACTCCAATGTTCTTACTATCCAGAAAGATTAAGGCCCAAGGG GTCAAGATGGTTCTTTCCGGTGAAGGTTCCGATGAAATCTTCGGTGGTTATCTATATTTC GCACAAGCTCCTTCTGCGGCAGAATTTCACACTGAATCCGTGCAACGTGTCAAGAACTTG CATTTGGCAGATTGTTTGAGAGCTAACAAGTCTACGATGGCTTGGGGTCTAGAAGCTCGT GTTCCATTCTTAGACAGAGAATTTTTGCAATTGTGTATGAACATCGATCCAAATGAAAAG ATGATTAAACCAAAGGAAGGACGTATTGAAAAGTACATTCTAAGGAAGGCATTCGACACC ACAGGAGAACCAGATGCTAAGCCATATTTACCAGAAGAAATTTTATGGAGACAAAAAGAA CAATTTTCCGACGGTGTTGGTTACTCCTGGATCGACGGATTAAAAGATACCGCCGAAGCA GTCATTTCAGATGAAATGTTTGCCAGTCCAAAGGCCGAATGGGGTAGTGACATTCCAACC ACAAAAGAGGCTTTCTGGTACAGACTAAAATTCGATGCTTTGTTCCCTCAAAAGACCGTG GCTGACACCGTTATGAGATGGATTCCAAAGGCCGACTGGGGTTGTGCTGAAGATCCTTCT GGTAGATATGCCCAAATTCATGAAAAACATATCGAATAA
Protein Properties
Pfam Domain Function
Protein Residues572
Protein Molecular Weight64469.60156
Protein Theoretical pI6.02
Signalling Regions
  • None
Transmembrane Regions
  • None
Protein Sequence>Asparagine synthetase [glutamine-hydrolyzing] 1 MCGIFAAFRHEDVHRYKPKALQLSKRIRHRGPDWSGNAIKNSTIFVHERLAIVGVESGAQ PITSSDGEYMLCVNGEIYNHIQLREECADYEFGTLSDCEPIIPMYLKHDIDAPKYLDGMF AWTLYDAKQDRIVAARDPIGITTLYMGRSSASPKTVYFASELKCLTDDCDTITAFPPGHV YDSKTDKITRYFTPDWLDEKRIPSTPIDYMAIRHSLEKAVRKRLMAEVPYGVLLSGGLDS SLIASIAARETAKATNDVEPSTYDSKARHLAGIDDDGKLHTAGWTSLHSFAIGLPNAPDL QAARKVAKFIGSIHHEHTFTLQEGLDALDDVIYHLETYDVTTIRASTPMFLLSRKIKAQG VKMVLSGEGSDEIFGGYLYFAQAPSAAEFHTESVQRVKNLHLADCLRANKSTMAWGLEAR VPFLDREFLQLCMNIDPNEKMIKPKEGRIEKYILRKAFDTTGEPDAKPYLPEEILWRQKE QFSDGVGYSWIDGLKDTAEAVISDEMFASPKAEWGSDIPTTKEAFWYRLKFDALFPQKTV ADTVMRWIPKADWGCAEDPSGRYAQIHEKHIE
References
External Links
ResourceLink
Saccharomyces Genome Database ASN1
Uniprot IDP49089
Uniprot NameASNS1_YEAST
GenBank Gene IDU40829
Genebank Protein ID1066479
General Reference
  • Dang, V. D., Valens, M., Bolotin-Fukuhara, M., Daignan-Fornier, B. (1996). "Cloning of the ASN1 and ASN2 genes encoding asparagine synthetases in Saccharomyces cerevisiae: differential regulation by the CCAAT-box-binding factor." Mol Microbiol 22:681-692.8951815
  • Bussey, H., Storms, R. K., Ahmed, A., Albermann, K., Allen, E., Ansorge, W., Araujo, R., Aparicio, A., Barrell, B., Badcock, K., Benes, V., Botstein, D., Bowman, S., Bruckner, M., Carpenter, J., Cherry, J. M., Chung, E., Churcher, C., Coster, F., Davis, K., Davis, R. W., Dietrich, F. S., Delius, H., DiPaolo, T., Hani, J., et, a. l. .. (1997). "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI." Nature 387:103-105.9169875
  • Smolka, M. B., Albuquerque, C. P., Chen, S. H., Zhou, H. (2007). "Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases." Proc Natl Acad Sci U S A 104:10364-10369.17563356
  • Albuquerque, C. P., Smolka, M. B., Payne, S. H., Bafna, V., Eng, J., Zhou, H. (2008). "A multidimensional chromatography technology for in-depth phosphoproteome analysis." Mol Cell Proteomics 7:1389-1396.18407956