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InterPro: IPR004618 Aspartate--ammonia ligase

Protein matchesHelp
UniProtKB
Matches:
563 proteins
AccessionHelp IPR004618 AsnA
TypeHelp Family
SignaturesHelp
InterPro RelationshipsHelp
Parent IPR006195 Aminoacyl-tRNA synthetase, class II, conserved region
GO Term annotationHelp
Process GO:0006529 asparagine biosynthetic process
Function GO:0004071 aspartate-ammonia ligase activity
Component GO:0005737 cytoplasm
InterPro annotation
BioMart Logo Entry Details in BioMart
AbstractHelp

Aspartate--ammonia ligase (asparagine synthetase) EC:6.3.1.1 catalyses the conversion of L-aspartate to L-asparagine in the presence of ATP and ammonia. This family represents one of two non-homologous forms of aspartate--ammonia ligase found in Escherichia coli. This type is also found in Haemophilus influenzae, Treponema pallidum and Lactobacillus delbrueckii, but appears to have a very limited distribution. The fact that the protein from the H. influenzae is more than 70% identical to that from the spirochete T. pallidum, but less than 65% identical to that from the closely related E. coli, strongly suggests lateral transfer.

Structural linksHelp
SCOP: d.104.1.1
CATH: 3.30.930.10
Database linksHelp
Enzyme: EC:6.3.1.1
PANDIT: PF03590
Blocks: IPB004618
Pfam Clan: CL0040.13

Taxonomic coverageHelp

Overlapping InterPro entriesHelp
IPR004618 Numbers of overlapping proteins Average numbers of overlapping amino acids

Example proteinsHelp
P00963 Aspartate--ammonia ligase

More proteins


Example Proteins Key


InterPro entry accession number/name and structure databases Colour code
IPR004618 Aspartate--ammonia ligase
IPR006195 Aminoacyl-tRNA synthetase, class II, conserved region
PDB Chain
ModBase
CATH Domain
SCOP Domain

PublicationsHelp

Additional ReadingHelp
Nakatsu T, Kato H, Oda J.
Crystal structure of asparagine synthetase reveals a close evolutionary relationship to class II aminoacyl-tRNA synthetase.
Nat. Struct. Biol. 5 1998 15-9 [PubMed: 9437423]
http://dx.doi.org/10.1038/nsb0198-15
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InterPro 23.1