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InterPro: IPR004708 Aspartate ammonia-lyase

Protein matches Help

UniProtKB

Matches:

574 proteins

Overview:	sorted by AC,	sorted by name,	of known structure,	proteins with splice variants
Detailed:	sorted by AC,	sorted by name,	of known structure	proteins with splice variants
Table:	For all matching proteins,	of known structure
Architectures
Accession List
Matches in BioMart

Accession

IPR004708 ApsA

Type

Family

Signatures Help

Database	ID	Name	Proteins
TIGRFAMs	TIGR00839	aspA	574
Signatures in BioMart

InterPro Relationships Help

Contains

IPR000362 Fumarate lyase
IPR003031 Delta crystallin
IPR018951 Fumarase C, C-terminal
IPR020557 Fumarate lyase, conserved site

GO Term annotation Help

Process

GO:0006531 aspartate metabolic process

Function

GO:0008797 aspartate ammonia-lyase activity

InterPro annotation

Entry Details in BioMart

Abstract

A number of enzymes, belonging to the lyase class, for which fumarate is a substrate have been shown [1, 2] to share a short conserved sequence around a methionine which is probably involved in the catalytic activity of this type of enzymes.

Aspartate ammonia-lyase catalyses the conversion of aspartate to fumarate.

Structural links Help

PDB - click here

SCOP: a.127.1.1

CATH: 1.10.275.10 , 1.10.40.30 , 1.20.200.10

Database links Help

Enzyme: EC:4.3.1.1

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR004708

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

P0AC38 Aspartate ammonia-lyase

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR018951	Fumarase C, C-terminal
IPR000362	Fumarate lyase
IPR020557	Fumarate lyase, conserved site
IPR003031	Delta crystallin
IPR004708	Aspartate ammonia-lyase
IPR008948	L-Aspartase-like
	PDB Chain
	ModBase
	CATH Domain
	SCOP Domain

Publications Open in usermanual
1.	Woods SA, Schwartzbach SD, Guest JR. Two biochemically distinct classes of fumarase in Escherichia coli. Biochim. Biophys. Acta 954 14-26 1988 [PubMed: 3282546]
2.	Guest JR, Woods SA, Miles JS. Sequence homologies between arginosuccinase, aspartase and fumarase - a family of strycturally related enzymes. FEMS Microbiol. Lett. 51 181-6 1988

Additional Reading Open in usermanual
	Shi W, Dunbar J, Jayasekera MM, Viola RE, Farber GK. The structure of L-aspartate ammonia-lyase from Escherichia coli. Biochemistry 36 1997 9136-44 [PubMed: 9230045] http://dx.doi.org/10.1021/bi9704515
	Fujii T, Sakai H, Kawata Y, Hata Y. Crystal structure of thermostable aspartase from Bacillus sp. YM55-1: structure-based exploration of functional sites in the aspartase family. J. Mol. Biol. 328 2003 635-54 [PubMed: 12706722] http://dx.doi.org/10.1016/S0022-2836(03)00310-3

InterPro 23.1