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InterPro: IPR009049 Argininosuccinate lyase

Protein matches Help

UniProtKB

Matches:

1869 proteins

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

Accession

IPR009049 Argininosuccinate_lyase

Secondary

IPR003031

Type

Domain

Signatures Help

Database	ID	Name	Proteins
HAMAP	MF_00006	Argininosuccinate_lyase	1428
PANTHER	PTHR11444:SF3	argH	1858
TIGRFAMs	TIGR00838	argH	1716
Signatures in BioMart

InterPro Relationships Help

Parent

IPR003031 Delta crystallin

Found in

IPR011244 Bifunctional argininosuccinate lyase/acetyltransferase

Contains

IPR020557 Fumarate lyase, conserved site

GO Term annotation Help

Process

GO:0042450 arginine biosynthetic process via ornithine

Function

GO:0004056 argininosuccinate lyase activity

InterPro annotation

Entry Details in BioMart

Abstract

This entry represents argininosuccinate lyase, but may include examples of avian delta crystallins, in which argininosuccinate lyase activity may or may not be present and the biological role is to provide the optically clear cellular protein of the eye lens.

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:4.3.2.1

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR009049

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

P04076 Argininosuccinate lyase

P04424 Argininosuccinate lyase

P11447 Argininosuccinate lyase

P73257 Argininosuccinate lyase

Q91YI0 Argininosuccinate lyase

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR000362	Fumarate lyase
IPR020557	Fumarate lyase, conserved site
IPR003031	Delta crystallin
IPR009049	Argininosuccinate lyase
IPR008948	L-Aspartase-like
	SWISS-MODEL
	PDB Chain
	ModBase
	CATH Domain
	SCOP Domain

Publications Help

Additional Reading Open in usermanual
	Tsai M, Sampaleanu LM, Greene C, Creagh L, Haynes C, Howell PL. A duck delta1 crystallin double loop mutant provides insight into residues important for argininosuccinate lyase activity. Biochemistry 43 2004 11672-82 [PubMed: 15362851] http://dx.doi.org/10.1021/bi0489006
	Sampaleanu LM, Codding PW, Lobsanov YD, Tsai M, Smith GD, Horvatin C, Howell PL. Structural studies of duck delta2 crystallin mutants provide insight into the role of Thr161 and the 280s loop in catalysis. Biochem. J. 384 2004 437-47 [PubMed: 15320872] http://www.pubmedcentral.nih.gov/picrender.fcgi?tool=EBI&pubmedid=15320872&action=stream&blobtype=pdf
	Sampaleanu LM, Yu B, Howell PL. Mutational analysis of duck delta 2 crystallin and the structure of an inactive mutant with bound substrate provide insight into the enzymatic mechanism of argininosuccinate lyase. J. Biol. Chem. 277 2002 4166-75 [PubMed: 11698398] http://dx.doi.org/10.1074/jbc.M107465200
	Bhaumik P, Koski MK, Bergmann U, Wierenga RK. Structure determination and refinement at 2.44 A resolution of argininosuccinate lyase from Escherichia coli. Acta Crystallogr. D Biol. Crystallogr. 60 2004 1964-70 [PubMed: 15502303] http://dx.doi.org/10.1107/S0907444904021912
	Lee HJ, Lai YH, Wu SY, Chen YH. The effect of N-terminal truncation on double-dimer assembly of goose delta-crystallin. Biochem. J. 392 2005 545-54 [PubMed: 16101585] http://dx.doi.org/10.1042/BJ20050860

InterPro 23.1