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InterPro: IPR001962 Asparagine synthase

Protein matchesHelp
UniProtKB
Matches:
2424 proteins
AccessionHelp IPR001962 Asn_synthase
TypeHelp Domain
SignaturesHelp
InterPro RelationshipsHelp
Parent IPR014729 Rossmann-like alpha/beta/alpha sandwich fold
Found in IPR006426 Asparagine synthase, glutamine-hydrolyzing
IPR017535 Asparagine synthase family amidotransferase
IPR017539 Exosortase 1 system-associated amidotransferase 1
GO Term annotationHelp
Process GO:0006529 asparagine biosynthetic process
Function GO:0004066 asparagine synthase (glutamine-hydrolyzing) activity
InterPro annotation
BioMart Logo Entry Details in BioMart
AbstractHelp

This domain is always found associated with (IPR000583). Family members that contain this domain catalyse the conversion of aspartate to asparagine. Asparagine synthetase B (EC:6.3.5.4) catalyzes the assembly of asparagine from aspartate, Mg(2+)ATP, and glutamine. The three-dimensional architecture of the N-terminal domain of asparagine synthetase B is similar to that observed for glutamine phosphoribosylpyrophosphate amidotransferase while the molecular motif of the C-domain is reminiscent to that observed for GMP synthetase [1].

Structural linksHelp
SCOP: c.26.2.1
CATH: 3.40.50.620
Database linksHelp
PANDIT: PF00733
Blocks: IPB001962
Pfam Clan: CL0039.8

Taxonomic coverageHelp

Overlapping InterPro entriesHelp
IPR001962 Numbers of overlapping proteins Average numbers of overlapping amino acids

Example proteinsHelp
P08243 Asparagine synthetase [glutamine-hydrolyzing]

P49078 Asparagine synthetase [glutamine-hydrolyzing]

P49089 Asparagine synthetase [glutamine-hydrolyzing] 1

Q5LJP9 Asparagine synthetase domain-containing protein CG17486

Q61024 Asparagine synthetase [glutamine-hydrolyzing]

More proteins


Example Proteins Key


InterPro entry accession number/name and structure databases Colour code
IPR000583 Glutamine amidotransferase, class-II
IPR006426 Asparagine synthase, glutamine-hydrolyzing
IPR001962 Asparagine synthase
IPR014729 Rossmann-like alpha/beta/alpha sandwich fold
IPR017932 Glutamine amidotransferase, type II
SWISS-MODEL
ModBase

PublicationsHelp
1. Larsen TM, Boehlein SK, Schuster SM, Richards NG, Thoden JB, Holden HM, Rayment I.
Three-dimensional structure of Escherichia coli asparagine synthetase B: a short journey from substrate to product.
Biochemistry 38 16146-57 1999 [PubMed: 10587437]
http://dx.doi.org/10.1021/bi9915768

Additional ReadingHelp
Miller MT, Gerratana B, Stapon A, Townsend CA, Rosenzweig AC.
Crystal structure of carbapenam synthetase (CarA).
J. Biol. Chem. 278 2003 40996-1002 [PubMed: 12890666]
http://dx.doi.org/10.1074/jbc.M307901200
Miller MT, Bachmann BO, Townsend CA, Rosenzweig AC.
The catalytic cycle of beta -lactam synthetase observed by x-ray crystallographic snapshots.
Proc. Natl. Acad. Sci. U.S.A. 99 2002 14752-7 [PubMed: 12409610]
http://dx.doi.org/10.1073/pnas.232361199
Miller MT, Bachmann BO, Townsend CA, Rosenzweig AC.
Structure of beta-lactam synthetase reveals how to synthesize antibiotics instead of asparagine.
Nat. Struct. Biol. 8 2001 684-9 [PubMed: 11473258]
http://dx.doi.org/10.1038/90394
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InterPro 23.1