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asnB
asparagine synthase (glutamine-hydrolysing)
function
control of peptidoglycan hydrolysis
product
asparagine synthase (glutamine-hydrolysing))
Genomic Context
categories
[category|SW 2|Metabolism] → [category|SW 2.3|Amino acid/ nitrogen metabolism] → [category|SW 2.3.1|Biosynthesis/ acquisition of amino acids] → [category|SW 2.3.1.5|Biosynthesis/ acquisition of aspartate/ asparagine]Gene
Coordinates
3,125,777 3,127,675
Phenotypes of a mutant
the mutant requires excess Mg2+ for growth [pubmed|28317238]The protein
Catalyzed reaction/ biological activity
ATP + H2O + L-aspartate + L-glutamine --> AMP + diphosphate + H+ + L-asparagine + L-glutamate (according to UniProt)amidation of meso-diaminopimelic (mDAP) acid in peptidoglycan [pubmed|28317238]Protein family
asparagine synthetase family (with [protein|15D150B53A25325DBC414F0C2B0D44AEF4B115A9|AsnO] and [protein|9446D9C88CBBBC5A08495D8AA49A92A9F47F2C9B|AsnH], according to UniProt)[SW|Domains]
[SW|Glutamine amidotransferase type-2 domain] (aa 2-214) (according to UniProt)Structure
[PDB|1CT9] (from ''E. coli'', 29% identity) [Pubmed|10587437]Expression and Regulation
Operons
genes
[gene|6F5BBCBA02EA1C016AA37EB63D252A4C07CE6617|asnB]-[gene|219586A3F378DC38EA076FD39B99D41136BDE722|ytnA]
description
[Pubmed|10498721]
regulation
constitutiveview in new tabBiological materials
Mutant
MGNA-A141 (asnB::erm), available at the [https://shigen.nig.ac.jp/bsub/resource/strainGeneDisrupted/detail/141 NBRP B. subtilis, Japan]References
Reviews
Original publications
10498721,10587437,28317238